Lysozyme
Enterobacteria phage T4
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain A； UniProt 1–164 | Mutation：C54T, C97A, L99A | No other associated polymer | SOLUTION NMR NMR measurement conditions：pH 5.5；298 K；Ionic strength (raw mmCIF value) 85；Pressure ambient NMR sample composition：1.5 mM [U-15N; U-2H] T4 L99A, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：1.5 mM [U-13C; U-15N; U-2H] T4 L99A, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：1.5 mM [U-13Ca; U-15N] T4 L99A, 100% D2O | 100% D2O NMR sample composition：1.5 mM [U-13C; U-15N; U-50% 2H] T4 L99A, 100% D2O | 100% D2O NMR sample composition：1.5 mM [ U-15N] 13CH3 Met T4 L99A, 100% D2O | 100% D2O | Resolution not provided |
Other States of the Same Protein in the Database
Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.
| Other PDB | Difference from Current Entry 2LCB | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 102L HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME Deposited 1992-09-29 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.74 Å |
| 103L HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME Deposited 1992-09-29 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 104L HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME Deposited 1992-09-29 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.80 Å |
| 104L HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME Deposited 1992-09-29 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.80 Å |
| 107L STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Deposited 1992-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 108L STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Deposited 1992-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 109L STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Deposited 1992-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 110L STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Deposited 1992-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 111L STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Deposited 1992-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 112L STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Deposited 1992-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 113L STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Deposited 1992-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 114L STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Deposited 1992-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 115L STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Deposited 1992-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 118L 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 Deposited 1993-05-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 119L 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 Deposited 1993-05-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.65 Å |
| 120L 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 Deposited 1993-05-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 122L 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 Deposited 1993-05-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 123L 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 Deposited 1993-05-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 125L 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 Deposited 1993-05-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 126L 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 Deposited 1993-05-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 127L 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 Deposited 1993-05-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 3 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 128L 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 Deposited 1993-05-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 1 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 129L 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 Deposited 1993-05-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 130L 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 Deposited 1993-05-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 131L 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 Deposited 1993-05-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 137L STRUCTURAL BASIS OF AMINO ACID ALPHA HELIX PROPENSITY Deposited 1993-08-17 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 137L STRUCTURAL BASIS OF AMINO ACID ALPHA HELIX PROPENSITY Deposited 1993-08-17 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 138L RAPID CRYSTALLIZATION OF T4 LYSOZYME BY INTERMOLECULAR DISULFIDE CROSSLINKING Deposited 1993-09-01 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 139L RAPID CRYSTALLIZATION OF T4 LYSOZYME BY INTERMOLECULAR DISULFIDE CROSSLINKING Deposited 1993-09-01 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 139L RAPID CRYSTALLIZATION OF T4 LYSOZYME BY INTERMOLECULAR DISULFIDE CROSSLINKING Deposited 1993-09-01 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 4 BME BETA-MERCAPTOETHANOL × 4 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 140L ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME Deposited 1993-10-15 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.10 Å |
| 141L ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME Deposited 1993-10-15 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 142L ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME Deposited 1993-10-15 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 143L ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME Deposited 1993-10-15 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 144L ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME Deposited 1993-10-15 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.10 Å |
| 145L ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME Deposited 1993-10-15 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 146L ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME Deposited 1993-10-15 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 147L ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME Deposited 1993-10-15 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 1 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 148L A COVALENT ENZYME-SUBSTRATE INTERMEDIATE WITH SACCHARIDE DISTORTION IN A MUTANT T4 LYSOZYME Deposited 1993-10-27 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric |
Chain E
1–164（164 aa）
|
Not recorded | BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 149L CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1994-01-25 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.60 Å |
| 150L CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1994-01-25 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.20 Å |
| 150L CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1994-01-25 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.20 Å |
| 150L CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1994-01-25 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.20 Å |
| 150L CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1994-01-25 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.20 Å |
| 151L CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1994-01-25 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | PO4 PHOSPHATE ION × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.20 Å |
| 152L CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1994-01-26 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–163（163 aa）
|
Not recorded | SO4 SULFATE ION × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 155L CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND Deposited 1994-06-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 156L CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND Deposited 1994-06-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 157L CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND Deposited 1994-06-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 158L CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND Deposited 1994-06-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 159L CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND Deposited 1994-06-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 160L CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND Deposited 1994-06-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 161L CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND Deposited 1994-06-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 162L CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND Deposited 1994-06-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 163L CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND Deposited 1994-06-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 164L CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND Deposited 1994-06-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 165L CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND Deposited 1994-06-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.75 Å |
| 166L CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND Deposited 1994-06-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.75 Å |
| 167L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–163（163 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.20 Å |
| 167L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–163（163 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.20 Å |
| 168L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.90 Å |
| 168L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.90 Å |
| 168L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.90 Å |
| 168L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.90 Å |
| 168L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain E
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.90 Å |
| 169L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 3.00 Å |
| 169L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 3.00 Å |
| 169L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 3.00 Å |
| 169L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 3.00 Å |
| 169L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain E
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 3.00 Å |
| 170L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.60 Å |
| 171L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.50 Å |
| 172L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 173L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 174L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | SO4 SULFATE ION × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.30 Å |
| 174L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.30 Å |
| 175L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.10 Å |
| 175L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.10 Å |
| 176L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.20 Å |
| 176L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.20 Å |
| 177L Protein flexibility and adaptability seen in 25 crystal forms of T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, D127C, R154C | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 8.6；pH 8.6
|
Resolution 2.50 Å |
| 178L Protein flexibility and adaptability seen in 25 crystal forms of T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, D127C, R154C | CL CHLORIDE ION × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.71 Å |
| 180L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T26E, C54T, C97A | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.75 Å |
| 180L PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Deposited 1995-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T26E, C54T, C97A | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.75 Å |
| 181L SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY Deposited 1995-04-19 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 BNZ BENZENE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 182L SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY Deposited 1995-04-19 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 BZF BENZOFURAN × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 183L SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY Deposited 1995-04-19 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 DEN INDENE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 184L SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY Deposited 1995-04-19 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 I4B ISOBUTYLBENZENE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 185L SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY Deposited 1995-04-19 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 IND INDOLE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 186L SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY Deposited 1995-04-19 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 N4B N-BUTYLBENZENE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 187L SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY Deposited 1995-04-19 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 PXY PARA-XYLENE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 188L SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY Deposited 1995-04-19 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 OXE ORTHO-XYLENE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 189L ENHANCEMENT OF PROTEIN STABILITY BY THE COMBINATION OF POINT MUTATIONS IN T4 LYSOZYME IS ADDITIVE Deposited 1995-05-09 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.50 Å |
| 190L A HELIX INITIATION SIGNAL IN T4 LYSOZYME IDENTIFIED BY POLYALANINE MUTAGENESIS Deposited 1995-06-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：N53A, N55A, V57A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 191L A HELIX INITIATION SIGNAL IN T4 LYSOZYME IDENTIFIED BY POLYALANINE MUTAGENESIS Deposited 1995-06-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：N53A, N55A, V57A, E128A, V131A, N132A | CL CHLORIDE ION × 3 HED 2-HYDROXYETHYL DISULFIDE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.95 Å |
| 192L A HELIX INITIATION SIGNAL IN T4 LYSOZYME IDENTIFIED BY POLYALANINE MUTAGENESIS Deposited 1995-06-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：N40A, S44A, E45A, D47A, K48A, C54T, C97A, D127A, E128A, V131A, N132A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 195L THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME Deposited 1995-11-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, A129L | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；pH 6.7
|
Resolution 1.90 Å |
| 196L THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME Deposited 1995-11-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, A129M | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；pH 6.7
|
Resolution 2.30 Å |
| 197L THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME Deposited 1995-11-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, A129M, F153A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；pH 6.7
|
Resolution 2.10 Å |
| 198L THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME Deposited 1995-11-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L121A, A129L | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；pH 6.7
|
Resolution 2.00 Å |
| 199L THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME Deposited 1995-11-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L121A, A129M | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；pH 6.7
|
Resolution 1.85 Å |
| 1B6I 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) Deposited 1999-01-14 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T,C97A,T21C,K124C | HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；pH 7.0
|
Resolution 1.90 Å |
| 1C60 T4 LYSOZYME MUTANT C54T/C97A/F153A IN THE PRESENCE OF 8 ATM ARGON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 2.00 Å |
| 1C61 T4 LYSOZYME MUTANT C54T/C97A/F153A IN THE PRESENCE OF 8 ATM KRYPTON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 KR KRYPTON × 3 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 2.00 Å |
| 1C62 T4 LYSOZYME MUTANT C54T/C97A/F153A IN THE PRESENCE OF 8 ATM XENON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 XE XENON × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 2.30 Å |
| 1C63 T4 LYSOZYME MUTANT C54T/C97A/L121A IN THE PRESENCE OF 8 ATM ARGON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 2.00 Å |
| 1C64 T4 LYSOZYME MUTANT C54T/C97A/L121A IN THE PRESENCE OF 8 ATM KRYPTON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 KR KRYPTON × 1 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 2.00 Å |
| 1C65 T4 LYSOZYME MUTANT C54T/C97A/L121A IN THE PRESENCE OF 8 ATM XENON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 XE XENON × 1 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 2.00 Å |
| 1C66 T4 LYSOZYME MUTANT C54T/C97A/L121A/L133A IN THE PRESENCE OF 8 ATM ARGON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 AR ARGON × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 2.10 Å |
| 1C67 T4 LYSOZYME MUTANT C54T/C97A/L121A/L133A IN THE PRESENCE OF 8 ATM KRYPTON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 KR KRYPTON × 3 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 2.20 Å |
| 1C68 T4 LYSOZYME MUTANT C54T/C97A/L121A/L133A IN THE PRESENCE OF 8 ATM XENON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 XE XENON × 3 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 2.50 Å |
| 1C69 T4 LYSOZYME MUTANT C54T/C97A/L133A IN THE PRESENCE OF 8 ATM ARGON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 1.80 Å |
| 1C6A T4 LYSOZYME MUTANT C54T/C97A/L133A IN THE PRESENCE OF 8 ATM KRYPTON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 KR KRYPTON × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 2.10 Å |
| 1C6B T4 LYSOZYME MUTANT C54T/C97A/L133A IN THE PRESENCE OF 8 ATM XENON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 XE XENON × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 2.20 Å |
| 1C6C T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 16 ATM ARGON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 AR ARGON × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 2.00 Å |
| 1C6D T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 16 ATM KRYPTON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 KR KRYPTON × 3 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 2.00 Å |
| 1C6E T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 2 ATM XENON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 1 XE XENON × 3 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 1.90 Å |
| 1C6F T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 32 ATM ARGON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 AR ARGON × 3 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 2.00 Å |
| 1C6G T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 4 ATM KRYPTON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 KR KRYPTON × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 1.90 Å |
| 1C6H T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 4 ATM XENON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 XE XENON × 3 BME BETA-MERCAPTOETHANOL × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 1.90 Å |
| 1C6I T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 8 ATM ARGON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 AR ARGON × 1 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 1.90 Å |
| 1C6J T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 8 ATM KRYPTON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 KR KRYPTON × 3 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 1.90 Å |
| 1C6K T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 8 ATM XENON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 XE XENON × 3 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 1.90 Å |
| 1C6L T4 LYSOZYME MUTANT C54T/C97A/L99A/F153A IN THE PRESENCE OF 8 ATM ARGON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 1.90 Å |
| 1C6M T4 LYSOZYME MUTANT C54T/C97A/L99A/F153A IN THE PRESENCE OF 8 ATM KRYPTON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 KR KRYPTON × 4 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 2.10 Å |
| 1C6N T4 LYSOZYME MUTANT C54T/C97A/L99A/F153A IN THE PRESENCE OF 8 ATM XENON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 XE XENON × 4 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 2.20 Å |
| 1C6P T4 LYSOZYME MUTANT C54T/C97A IN THE PRESENCE OF 8 ATM ARGON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 1.90 Å |
| 1C6Q T4 LYSOZYME MUTANT C54T/C97A IN THE PRESENCE OF 8 ATM KRYPTON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 KR KRYPTON × 1 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 1.90 Å |
| 1C6T T4 LYSOZYME MUTANT C54T/C97A IN THE PRESENCE OF 8 ATM XENON Deposited 1999-12-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 XE XENON × 1 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
1.8-2.2 M NAH2/K2HPO4, PH 6.9-7.1, 50 MM BETA-MERCAPTOETHANOL AND/OR 50 MM HYDROXYETHYL DISULFIDE
|
Resolution 2.00 Å |
| 1CTW T4 LYSOZYME MUTANT I78A Deposited 1999-08-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, I78A, C97A | CL CHLORIDE ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.6；277 K；NA2PO4, NACL, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.10 Å |
| 1CU0 T4 LYSOZYME MUTANT I78M Deposited 1999-08-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, I78M, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277 K；NA2PO4, NACL, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.20 Å |
| 1CU2 T4 LYSOZYME MUTANT L84M Deposited 1999-08-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, L84M, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277 K；NA2PO4, NACL, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.85 Å |
| 1CU3 T4 LYSOZYME MUTANT V87M Deposited 1999-08-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, V87M, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277 K；NA2PO4, NACL, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.12 Å |
| 1CU5 T4 LYSOZYME MUTANT L91M Deposited 1999-08-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, L91M, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277 K；NA2PO4, NACL, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.05 Å |
| 1CU6 T4 LYSOZYME MUTANT L91A Deposited 1999-08-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, L91A, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；NA2PO4, NACL, VAPOR DIFFUSION, HANGING DROP
|
Resolution 2.10 Å |
| 1CUP METHIONINE CORE MUTANT OF T4 LYSOZYME Deposited 1999-08-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, I100M, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277 K；NA2PO4, NACL, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.89 Å |
| 1CUQ T4 LYSOZYME MUTANT V103M Deposited 1999-08-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, V103M | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277 K；NA2PO4, NACL, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.05 Å |
| 1CV0 T4 LYSOZYME MUTANT F104M Deposited 1999-08-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, F104M | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277 K；NA2PO4, NACL, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.12 Å |
| 1CV1 T4 LYSOZYME MUTANT V111M Deposited 1999-08-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, V111M, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277 K；NA2PO4, NACL, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.10 Å |
| 1CV3 T4 LYSOZYME MUTANT L121M Deposited 1999-08-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L121M | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277 K；NA2PO4, NACL, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å |
| 1CV4 T4 LYSOZYME MUTANT L118M Deposited 1999-08-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L118M | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277 K；NA2PO4, NACL, VAPOR DIFFUSION, HANGING DROP
|
Resolution 1.90 Å |
| 1CV5 T4 LYSOZYME MUTANT L133M Deposited 1999-08-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L133M | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277 K；NA2PO4, NACL, VAPOR DIFFUSION, HANGING DROP
|
Resolution 1.87 Å |
| 1CV6 T4 LYSOZYME MUTANT V149M Deposited 1999-08-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, V149M | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277 K；NA2PO4, NACL, VAPOR DIFFUSION, HANGING DROP
|
Resolution 1.90 Å |
| 1CVK T4 LYSOZYME MUTANT L118A Deposited 1999-08-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L118A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277 K；NA2PO4, NACL, VAPOR DIFFUSION, HANGING DROP
|
Resolution 1.80 Å |
| 1CX6 T4 LYSOZYME SUBSTITUTED WITH SELENOMETHIONINE Deposited 1999-08-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, L84(MSE), L91(MSE), C97A, L99(MSE), L118(MSE), L121(MSE), L133(MSE), F153(MSE) Non-standard monomer：Yes (specific site not provided by mmCIF) | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277 K；NA2PO4, NACL, VAPOR DIFFUSION, HANGING DROP
|
Resolution 2.01 Å |
| 1CX7 T4 LYSOZYME METHIONINE CORE MUTANT Deposited 1999-08-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, L84M, L91M, C97A, L99M, L118M, L121M, L133M, F153M | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277 K；Na2PO4, NaCl, VAPOR DIFFUSION, HANGING DROP
|
Resolution 1.94 Å |
| 1D2W N-TERMINAL DOMAIN CORE METHIONINE MUTATION Deposited 1999-09-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：I27M, C54T, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；NA2PO4, NACL, pH 6.9, VAPOR DIFFUSION, HANGING DROP
|
Resolution 1.89 Å |
| 1D2Y N-TERMINAL DOMAIN CORE METHIONINE MUTATION Deposited 1999-09-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：I50M, C54T, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；NA2PO4, NACL, pH 6.9, VAPOR DIFFUSION, HANGING DROP
|
Resolution 2.06 Å |
| 1D3F N-TERMINAL DOMAIN CORE METHIONINE MUTATION Deposited 1999-09-29 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, I58M, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；NA2PO4, NACL , pH 6.9, VAPOR DIFFUSION, HANGING DROP
|
Resolution 2.05 Å |
| 1D3J N-TERMINAL DOMAIN CORE METHIONINE MUTATION Deposited 1999-09-29 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, L66M, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；NA2PO4, NACL , pH 6.9, VAPOR DIFFUSION, HANGING DROP
|
Resolution 1.97 Å |
| 1D3M METHIONINE CORE MUTATION Deposited 1999-09-29 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, L84M, L91M, C97A, L99M, L118M, L121M | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；NA2PO4, NACL, pH 6.9, VAPOR DIFFUSION, HANGING DROP
|
Resolution 2.12 Å |
| 1D3N METHIONINE CORE MUTATION Deposited 1999-09-29 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, L84(MSE), L91(MSE), C97A, L99(MSE), L118(MSE), L121(MSE) Non-standard monomer：Yes (specific site not provided by mmCIF) | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；NA2PO4, NACL, pH 7.0, VAPOR DIFFUSION, HANGING DROP
|
Resolution 2.00 Å |
| 1D9W BACTERIOPHAGE T4 LYSOZYME MUTANT Deposited 1999-10-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：K124D | BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；2.1-M phosphate, 10 mM BME, 20 mM oxBME, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.91 Å |
| 1DYA DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME Deposited 1993-05-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1DYB DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME Deposited 1993-05-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.75 Å |
| 1DYC DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME Deposited 1993-05-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.10 Å |
| 1DYD DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME Deposited 1993-05-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.10 Å |
| 1DYE DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME Deposited 1993-05-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1DYF DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME Deposited 1993-05-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1DYG DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME Deposited 1993-05-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.10 Å |
| 1EPY T4 LYSOZYME MUTANT, T21H/C54T/C97A/Q141H/T142H Deposited 2000-03-29 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21H,C54T,C97A,Q141H,T142H | SO4 SULFATE ION × 1 CL CHLORIDE ION × 1 CO COBALT (II) ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；12-16% PEG 8000, 10% isopropanol, sodium chloride, HEPES, 0.002 M cobalt chloride, pH 7.0, VAPOR DIFFUSION, HANGING
DROP, temperature 4K
|
Resolution 1.85 Å |
| 1G06 CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT V149S Deposited 2000-10-05 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T; C97A; V149S | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；300 K；Phosphate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 300K
|
Resolution 1.85 Å |
| 1G07 CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT V149C Deposited 2000-10-05 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T; C97A; V149S | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；300 K；Phosphate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 300K
|
Resolution 1.70 Å |
| 1G0G CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT T152A Deposited 2000-10-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T; C97A; T152A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；277 K；Phosphate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.90 Å |
| 1G0J CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT T152S Deposited 2000-10-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T; C97A; T152S | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；277 K；Phosphate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å |
| 1G0K CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT T152C Deposited 2000-10-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T; C97A; T152C | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；277 K；Phosphate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.85 Å |
| 1G0L CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT T152V Deposited 2000-10-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T; C97A; T152V | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；277 K；Phosphate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å |
| 1G0M CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT T152I Deposited 2000-10-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T; C97A; T152I | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；277 K；Phosphate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.70 Å |
| 1G0P CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT V149G Deposited 2000-10-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T; C97A; T152S | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；277 K；Phosphate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å |
| 1G0Q CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT V149I Deposited 2000-10-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T; C97A; V149I | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；277 K；Phosphate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å |
| 1G1V T4 LYSOZYME MUTANT C54T/C97A/I58T Deposited 2000-10-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T/C97A/I58T | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；277 K；2.1 M NAH2/K2HPO4, 50 MM HYDROXYETHYL DISULFIDE, pH 7.10, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.90 Å |
| 1G1W T4 LYSOZYME MUTANT C54T/C97A/Q105M Deposited 2000-10-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T/C97A/Q105M | CL CHLORIDE ION × 1 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；277 K；1.8 M NAH2/K2HPO4, 50 MM BETA-MERCAPTOETHANOL, pH 7.10, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å |
| 1I6S T4 LYSOZYME MUTANT C54T/C97A/N101A Deposited 2001-03-04 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T,C97A,N101A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1JQU Are Carboxy Terminii of Helices Coded by the Local Sequence or by Tertiary Structure Contacts Deposited 2001-08-08 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, W158L | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.75；277 K；30% PEG4000, PIPES buffer ph7.0, 0.2M LiSO4, pH 6.75, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.60 Å R-free 0.316 |
| 1JQU Are Carboxy Terminii of Helices Coded by the Local Sequence or by Tertiary Structure Contacts Deposited 2001-08-08 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：C54T, C97A, W158L | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.75；277 K；30% PEG4000, PIPES buffer ph7.0, 0.2M LiSO4, pH 6.75, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.60 Å R-free 0.316 |
| 1JQU Are Carboxy Terminii of Helices Coded by the Local Sequence or by Tertiary Structure Contacts Deposited 2001-08-08 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
1–164（164 aa）
|
Mutation：C54T, C97A, W158L | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.75；277 K；30% PEG4000, PIPES buffer ph7.0, 0.2M LiSO4, pH 6.75, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.60 Å R-free 0.316 |
| 1JQU Are Carboxy Terminii of Helices Coded by the Local Sequence or by Tertiary Structure Contacts Deposited 2001-08-08 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
1–164（164 aa）
|
Mutation：C54T, C97A, W158L | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.75；277 K；30% PEG4000, PIPES buffer ph7.0, 0.2M LiSO4, pH 6.75, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.60 Å R-free 0.316 |
| 1JTM Alternative Structures of a Sequence Extended T4 Lysozyme Show that the Highly Conserved Beta-Sheet has Weak Intrinsic Folding Propensity Deposited 2001-08-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A | BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；50MM TRIS-GLYCINE, 20% PEG 8000, 10% Isopropanol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.90 Å R-free 0.265 |
| 1JTN Alternative Structures of a Sequence Extended T4 Lysozyme Show that the Highly Conserved Beta-Sheet Region has weak intrinsic Folding Propensity Deposited 2001-08-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A | SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；298 K；50m Tris-Glycine, 200mM Lisulfate, 18% PEG 4000, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.30 Å R-free 0.314 |
| 1JTN Alternative Structures of a Sequence Extended T4 Lysozyme Show that the Highly Conserved Beta-Sheet Region has weak intrinsic Folding Propensity Deposited 2001-08-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：C54T, C97A | SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；298 K；50m Tris-Glycine, 200mM Lisulfate, 18% PEG 4000, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.30 Å R-free 0.314 |
| 1KNI Stabilizing Disulfide Bridge Mutant of T4 Lysozyme Deposited 2001-12-18 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C,T142C,C54T,C97A | CL CHLORIDE ION × 1 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1KS3 METHIONINE CORE MUTANT OF T4 LYSOZYME Deposited 2002-01-10 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T,C97A,L118M,L121M | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；Na2PO4, NaCl, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.16 Å |
| 1KW5 METHIONINE CORE MUTANT OF T4 LYSOZYME Deposited 2002-01-28 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T,L84M,L91M,C97A,L99M | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；Na2PO4, NaCl, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.75 Å |
| 1KW7 METHIONINE CORE MUTANT OF T4 LYSOZYME Deposited 2002-01-28 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T,L84M,L91M,C97A,L99M,L133M | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；Na2Po4, NaCl, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.89 Å |
| 1KY0 METHIONINE CORE MUTANT OF T4 LYSOZYME Deposited 2002-02-01 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T,L84M,L91M,C97A,L99M,F153M | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；Na2PO4, NaCl, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.97 Å |
| 1KY1 METHIONINE CORE MUTANT OF T4 LYSOZYME Deposited 2002-02-01 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T,L84M,L91M,C97A,L99M,L118M,L121M,L133M | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；Na2PO4, NaCl, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.05 Å |
| 1L00 PERTURBATION OF TRP 138 IN T4 LYSOZYME BY MUTATIONS AT GLN 105 USED TO CORRELATE CHANGES IN STRUCTURE, STABILITY, SOLVATION, AND SPECTROSCOPIC PROPERTIES Deposited 1992-07-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1L01 STRUCTURAL STUDIES OF MUTANTS OF THE LYSOZYME OF BACTERIOPHAGE T4. THE TEMPERATURE-SENSITIVE MUTANT PROTEIN THR157 (RIGHT ARROW) ILE Deposited 1988-02-05 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L02 CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME Deposited 1988-02-05 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L03 CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME Deposited 1988-02-05 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L04 CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME Deposited 1988-02-05 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L05 CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME Deposited 1988-02-05 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L06 CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME Deposited 1988-02-05 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L07 CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME Deposited 1988-02-05 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L08 CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME Deposited 1988-02-05 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L09 CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME Deposited 1988-02-05 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L0J METHIONINE CORE MUTANT OF T4 LYSOZYME Deposited 2002-02-11 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T,L84M,L91M,C97A,L99M,L118M,L121M,F153M | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；Na2PO4, NaCl, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.98 Å |
| 1L0K METHIONINE CORE MUTANT OF T4 LYSOZYME Deposited 2002-02-11 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T,L84M,L91M,C97A,L99M,V111M,L118M,L121M,L133M | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；Na2PO4, NaCl, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.02 Å |
| 1L10 STRUCTURAL STUDIES OF MUTANTS OF THE LYSOZYME OF BACTERIOPHAGE T4. THE TEMPERATURE-SENSITIVE MUTANT PROTEIN THR157 (RIGHT ARROW) ILE Deposited 1988-02-05 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L11 CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME Deposited 1988-02-05 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L12 CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME Deposited 1988-02-05 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L13 CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME Deposited 1988-02-05 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L14 CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME Deposited 1988-02-05 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L15 CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME Deposited 1988-02-05 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L16 STRUCTURAL ANALYSIS OF THE TEMPERATURE-SENSITIVE MUTANT OF BACTERIOPHAGE T4 LYSOZYME, GLYCINE 156 (RIGHT ARROW) ASPARTIC ACID Deposited 1988-02-05 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L17 HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3 Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L18 HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3 Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L19 ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L20 ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 1L21 CONTRIBUTIONS OF LEFT-HANDED HELICAL RESIDUES TO THE STRUCTURE AND STABILITY OF BACTERIOPHAGE T4 LYSOZYME Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 1L22 CONTRIBUTIONS OF LEFT-HANDED HELICAL RESIDUES TO THE STRUCTURE AND STABILITY OF BACTERIOPHAGE T4 LYSOZYME Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L23 ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L24 ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L25 REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1L26 REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY Deposited 1989-05-01 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L27 REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1L28 REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1L29 REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L30 REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L31 REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1L32 REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L33 CONTRIBUTIONS OF LEFT-HANDED HELICAL RESIDUES TO THE STRUCTURE AND STABILITY OF BACTERIOPHAGE T4 LYSOZYME Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L34 HIGH-RESOLUTION STRUCTURE OF THE TEMPERATURE-SENSITIVE MUTANT OF PHAGE LYSOZYME, ARG 96 (RIGHT ARROW) HIS Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1L35 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 Deposited 1989-10-26 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–163（163 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1L36 TOWARD A SIMPLIFICATION OF THE PROTEIN FOLDING PROBLEM: A STABILIZING POLYALANINE ALPHA-HELIX ENGINEERED IN T4 LYSOZYME Deposited 1990-12-26 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 3 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L37 CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS Deposited 1991-01-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 1L38 CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS Deposited 1991-01-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1L39 CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS Deposited 1991-01-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 1L40 CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS Deposited 1991-01-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 1L41 CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS Deposited 1991-01-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.75 Å |
| 1L42 CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY Deposited 1991-01-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1L43 CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY Deposited 1991-01-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1L44 CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY Deposited 1991-01-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L45 CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY Deposited 1991-01-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L46 CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY Deposited 1991-01-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L47 CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY Deposited 1991-01-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L48 STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME Deposited 1991-01-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L49 STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME Deposited 1991-01-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1L50 STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME Deposited 1991-01-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 1L51 STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME Deposited 1991-01-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1L52 STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME Deposited 1991-01-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L53 STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME Deposited 1991-01-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 1L54 THE STRUCTURAL AND THERMODYNAMIC CONSEQUENCES OF BURYING A CHARGED RESIDUE WITHIN THE HYDROPHOBIC CORE OF T4 LYSOZYME Deposited 1991-01-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1L55 ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME Deposited 1991-05-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1L56 ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME Deposited 1991-05-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1L57 ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME Deposited 1991-05-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1L58 ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME Deposited 1991-05-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.65 Å |
| 1L59 ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME Deposited 1991-05-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.75 Å |
| 1L60 ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME Deposited 1991-05-06 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L61 ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME Deposited 1991-05-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1L62 ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME Deposited 1991-05-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L63 ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME Deposited 1991-05-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.75 Å |
| 1L64 TOLERANCE OF T4 LYSOZYME TO MULTIPLE XAA (RIGHT ARROW) ALA SUBSTITUTIONS: A POLYALANINE ALPHA-HELIX CONTAINING TEN CONSECUTIVE ALANINES Deposited 1991-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1L65 TOLERANCE OF T4 LYSOZYME TO MULTIPLE XAA (RIGHT ARROW) ALA SUBSTITUTIONS: A POLYALANINE ALPHA-HELIX CONTAINING TEN CONSECUTIVE ALANINES Deposited 1991-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L66 TOLERANCE OF T4 LYSOZYME TO MULTIPLE XAA (RIGHT ARROW) ALA SUBSTITUTIONS: A POLYALANINE ALPHA-HELIX CONTAINING TEN CONSECUTIVE ALANINES Deposited 1991-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L67 TOLERANCE OF T4 LYSOZYME TO MULTIPLE XAA (RIGHT ARROW) ALA SUBSTITUTIONS: A POLYALANINE ALPHA-HELIX CONTAINING TEN CONSECUTIVE ALANINES Deposited 1991-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1L68 TOLERANCE OF T4 LYSOZYME TO MULTIPLE XAA (RIGHT ARROW) ALA SUBSTITUTIONS: A POLYALANINE ALPHA-HELIX CONTAINING TEN CONSECUTIVE ALANINES Deposited 1991-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L69 MULTIPLE STABILIZING ALANINE REPLACEMENTS WITHIN ALPHA-HELIX 126-134 OF T4 LYSOZYME HAVE INDEPENDENT, ADDITIVE EFFECTS ON BOTH STRUCTURE AND STABILITY Deposited 1991-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1L70 MULTIPLE STABILIZING ALANINE REPLACEMENTS WITHIN ALPHA-HELIX 126-134 OF T4 LYSOZYME HAVE INDEPENDENT, ADDITIVE EFFECTS ON BOTH STRUCTURE AND STABILITY Deposited 1991-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 3 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1L71 MULTIPLE STABILIZING ALANINE REPLACEMENTS WITHIN ALPHA-HELIX 126-134 OF T4 LYSOZYME HAVE INDEPENDENT, ADDITIVE EFFECTS ON BOTH STRUCTURE AND STABILITY Deposited 1991-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 1L72 MULTIPLE STABILIZING ALANINE REPLACEMENTS WITHIN ALPHA-HELIX 126-134 OF T4 LYSOZYME HAVE INDEPENDENT, ADDITIVE EFFECTS ON BOTH STRUCTURE AND STABILITY Deposited 1991-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 1L73 MULTIPLE STABILIZING ALANINE REPLACEMENTS WITHIN ALPHA-HELIX 126-134 OF T4 LYSOZYME HAVE INDEPENDENT, ADDITIVE EFFECTS ON BOTH STRUCTURE AND STABILITY Deposited 1991-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 3 BME BETA-MERCAPTOETHANOL × 3 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.05 Å |
| 1L74 MULTIPLE STABILIZING ALANINE REPLACEMENTS WITHIN ALPHA-HELIX 126-134 OF T4 LYSOZYME HAVE INDEPENDENT, ADDITIVE EFFECTS ON BOTH STRUCTURE AND STABILITY Deposited 1991-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 3 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L75 MULTIPLE STABILIZING ALANINE REPLACEMENTS WITHIN ALPHA-HELIX 126-134 OF T4 LYSOZYME HAVE INDEPENDENT, ADDITIVE EFFECTS ON BOTH STRUCTURE AND STABILITY Deposited 1991-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 3 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1L76 TOLERANCE OF T4 LYSOZYME TO PROLINE SUBSTITUTIONS WITHIN THE LONG INTERDOMAIN ALPHA-HELIX ILLUSTRATES THE ADAPTABILITY OF PROTEINS TO POTENTIALLY DESTABILIZING LESIONS Deposited 1991-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1L77 DESIGN AND STRUCTURAL ANALYSIS OF ALTERNATIVE HYDROPHOBIC CORE PACKING ARRANGEMENTS IN BACTERIOPHAGE T4 LYSOZYME Deposited 1991-11-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.05 Å |
| 1L79 DESIGN AND STRUCTURAL ANALYSIS OF ALTERNATIVE HYDROPHOBIC CORE PACKING ARRANGEMENTS IN BACTERIOPHAGE T4 LYSOZYME Deposited 1991-11-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1L80 DESIGN AND STRUCTURAL ANALYSIS OF ALTERNATIVE HYDROPHOBIC CORE PACKING ARRANGEMENTS IN BACTERIOPHAGE T4 LYSOZYME Deposited 1991-11-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1L81 DESIGN AND STRUCTURAL ANALYSIS OF ALTERNATIVE HYDROPHOBIC CORE PACKING ARRANGEMENTS IN BACTERIOPHAGE T4 LYSOZYME Deposited 1991-11-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 1L82 DESIGN AND STRUCTURAL ANALYSIS OF ALTERNATIVE HYDROPHOBIC CORE PACKING ARRANGEMENTS IN BACTERIOPHAGE T4 LYSOZYME Deposited 1991-11-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.10 Å |
| 1L83 A CAVITY-CONTAINING MUTANT OF T4 LYSOZYME IS STABILIZED BY BURIED BENZENE Deposited 1992-01-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 BNZ BENZENE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L84 A CAVITY-CONTAINING MUTANT OF T4 LYSOZYME IS STABILIZED BY BURIED BENZENE Deposited 1992-01-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 BNZ BENZENE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1L85 SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Deposited 1992-01-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 1L86 SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Deposited 1992-01-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1L87 SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Deposited 1992-01-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1L88 SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Deposited 1992-01-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 1L89 SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Deposited 1992-01-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1L90 SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Deposited 1992-01-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.75 Å |
| 1L91 SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Deposited 1992-01-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1L92 SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Deposited 1992-01-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1L93 SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Deposited 1992-01-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1L94 SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Deposited 1992-01-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1L95 SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Deposited 1992-01-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 1L96 STRUCTURE OF A HINGE-BENDING BACTERIOPHAGE T4 LYSOZYME MUTANT, ILE3-> PRO Deposited 1992-02-11 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 1L97 STRUCTURE OF A HINGE-BENDING BACTERIOPHAGE T4 LYSOZYME MUTANT, ILE3-> PRO Deposited 1992-02-11 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 1L97 STRUCTURE OF A HINGE-BENDING BACTERIOPHAGE T4 LYSOZYME MUTANT, ILE3-> PRO Deposited 1992-02-11 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 1L98 PERTURBATION OF TRP 138 IN T4 LYSOZYME BY MUTATIONS AT GLN 105 USED TO CORRELATE CHANGES IN STRUCTURE, STABILITY, SOLVATION, AND SPECTROSCOPIC PROPERTIES Deposited 1992-07-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1L99 PERTURBATION OF TRP 138 IN T4 LYSOZYME BY MUTATIONS AT GLN 105 USED TO CORRELATE CHANGES IN STRUCTURE, STABILITY, SOLVATION, AND SPECTROSCOPIC PROPERTIES Deposited 1992-07-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.95 Å |
| 1LGU T4 Lysozyme Mutant L99A/M102Q Deposited 2002-04-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A, M102Q | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 3 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1LGW T4 Lysozyme Mutant L99A/M102Q Bound by 2-fluoroaniline Deposited 2002-04-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A, M102Q | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 1AN 2-FLUOROANILINE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 1LGX T4 Lysozyme Mutant L99A/M102Q Bound by 3,5-difluoroaniline Deposited 2002-04-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A, M102Q | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 5AN 3,5-DIFLUOROANILINE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1LI2 T4 Lysozyme Mutant L99A/M102Q Bound by Phenol Deposited 2002-04-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A, M102Q | CL CHLORIDE ION × 2 IPH PHENOL × 1 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 1LI3 T4 lysozyme mutant L99A/M102Q bound by 3-chlorophenol Deposited 2002-04-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A, M102Q | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 3CH 3-CHLOROPHENOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 1LI6 T4 lysozyme mutant L99A/M102Q bound by 5-methylpyrrole Deposited 2002-04-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A, M102Q | CL CHLORIDE ION × 2 5MP 5-METHYLPYRROLE × 1 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 1LLH ARE CARBOXY TERMINII OF HELICES CODED BY THE LOCAL SEQUENCE OR BY TERTIARY STRUCTURE CONTACTS Deposited 2002-04-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, T157I | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.8；277 K；1.8M Phosphate, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å R-free 0.242 |
| 1LPY Multiple Methionine Substitutions in T4 Lysozyme Deposited 2002-05-08 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T,L84M,V87M,L91M,C97A,L99M,I100M,V103M,G110R,V111M,L118M,L121M,L133M Non-standard monomer：Yes (specific site not provided by mmCIF) | PO4 PHOSPHATE ION × 1 CL CHLORIDE ION × 1 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.65 Å |
| 1LW9 Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability Deposited 2002-05-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T,C97A | K POTASSIUM ION × 1 CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；pH 6.7
|
Resolution 1.45 Å R-free 0.254 |
| 1LWG Multiple Methionine Substitutions are Tolerated in T4 Lysozyme and have Coupled Effects on Folding and Stability Deposited 2002-05-31 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T,L84M,V87M,L91M,C97A,L99M,V111M,L118M,L121M,L133M | PO4 PHOSPHATE ION × 1 CL CHLORIDE ION × 3 K POTASSIUM ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
|
Resolution 1.70 Å |
| 1LWG Multiple Methionine Substitutions are Tolerated in T4 Lysozyme and have Coupled Effects on Folding and Stability Deposited 2002-05-31 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–164（164 aa）
|
Mutation：C54T,L84M,V87M,L91M,C97A,L99M,V111M,L118M,L121M,L133M | PO4 PHOSPHATE ION × 2 CL CHLORIDE ION × 6 K POTASSIUM ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
|
Resolution 1.70 Å |
| 1LWK Multiple Methionine Substitutions are Tolerated in T4 Lysozyme and have Coupled Effects on Folding and Stability Deposited 2002-05-31 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T,L84MSE,V87MSE,L91MSE,C97A,L99MSE,G110R,V111MSE,L118MSE,L121MSE,L133MSE,F153MSE Non-standard monomer：Yes (specific site not provided by mmCIF) | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
|
Resolution 2.10 Å |
| 1LYD CRYSTAL STRUCTURE OF T4-LYSOZYME GENERATED FROM SYNTHETIC CODING DNA EXPRESSED IN ESCHERICHIA COLI Deposited 1989-01-11 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 1LYE DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF SIX AMINO ACID SUBSTITUTIONS AT THR 59 Deposited 1992-08-10 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1LYF DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF SIX AMINO ACID SUBSTITUTIONS AT THR 59 Deposited 1992-08-10 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1LYG DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF SIX AMINO ACID SUBSTITUTIONS AT THR 59 Deposited 1992-08-10 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1LYH DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF SIX AMINO ACID SUBSTITUTIONS AT THR 59 Deposited 1992-08-10 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 1LYI DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF SIX AMINO ACID SUBSTITUTIONS AT THR 59 Deposited 1992-08-10 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 1LYJ DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF SIX AMINO ACID SUBSTITUTIONS AT THR 59 Deposited 1992-08-10 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1NHB Specificity of ligand binding in a buried non-polar cavity of t4 lysozyme: linkage of dynamics and structural plasticity Deposited 1995-02-24 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 PYJ PHENYLETHANE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1OV5 T4 Lysozyme Cavity Mutant L99a/M102Q Bound With 2-Allylphenol Deposited 2003-03-25 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A, M102Q | CL CHLORIDE ION × 2 2LP 2-ALLYLPHENOL × 1 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.10 Å |
| 1OV7 T4 Lysozyme Cavity Mutant L99A/M102Q Bound with 2-Allyl-6-Methyl-Phenol Deposited 2003-03-25 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A, M102Q | CL CHLORIDE ION × 2 LYL 2-ALLYL-6-METHYL-PHENOL × 1 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 1OVH T4 Lysozyme Cavity Mutant L99A/M102Q Bound With 2-Chloro-6-Methyl-Aniline Deposited 2003-03-26 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A, M102Q | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 3 2CM 2-CHLORO-6-METHYL-ANILINE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.95 Å |
| 1OVJ T4 Lysozyme Cavity Mutant L99A/M102Q Bound with 3-Fluoro-2-Methyl_Aniline Deposited 2003-03-26 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A, M102Q | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 3 FLM 3-FLUORO-2-METHYL-ANILINE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 1OVK T4 Lysozyme Cavity Mutant L99A/M102Q Bound with N-Allyl-Aniline Deposited 2003-03-26 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A, M102Q | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 3 NYL N-ALLYL-ANILINE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.10 Å |
| 1OWY T4 Lysozyme Cavity Mutant L99A/M102Q Bound With 2-Propyl-Aniline Deposited 2003-03-31 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A, M102Q | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 PRY 2-PROPYL-ANILINE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1OWZ T4 Lysozyme Cavity Mutant L99A/M102Q Bound With 4-FluoroPhenEthyl Alcohol Deposited 2003-03-31 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A, M102Q | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 3 4FA 4-FLUOROPHENETHYL ALCOHOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1OYU Long-Distance conformational changes in a protein engineered by modulated sequence duplication Deposited 2003-04-07 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；25% poly-ethylene glycol 4000, 50mM phosphate buffer, 0.2mM ammonium acetate, 20% isopropanol, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.50 Å R-free 0.324 |
| 1OYU Long-Distance conformational changes in a protein engineered by modulated sequence duplication Deposited 2003-04-07 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；25% poly-ethylene glycol 4000, 50mM phosphate buffer, 0.2mM ammonium acetate, 20% isopropanol, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.50 Å R-free 0.324 |
| 1P2L T4 Lysozyme Core Repacking Mutant V87I/TA Deposited 2003-04-15 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, V87I, C97A | PO4 PHOSPHATE ION × 1 K POTASSIUM ION × 1 CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；277 K；Potassium PHOSPHATE, Sodium Phosphate, NaCl, BME, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.58 Å R-free 0.217 |
| 1P2R T4 LYSOZYME CORE REPACKING MUTANT I78V/TA Deposited 2003-04-15 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, I78V, C97A | K POTASSIUM ION × 1 CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；277 K；Potassium Phosphate, Sodium phosphate, NaCl, BME, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.58 Å R-free 0.245 |
| 1P36 T4 LYOSZYME CORE REPACKING MUTANT I100V/TA Deposited 2003-04-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, I100V | K POTASSIUM ION × 1 CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；277 K；Potassium PHOSPHATE, Sodium Phosphate, NaCl, BME, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.45 Å R-free 0.226 |
| 1P37 T4 LYSOZYME CORE REPACKING BACK-REVERTANT L102M/CORE10 Deposited 2003-04-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, v87I, C97A, I100V, V103I, M106I, V111A, M120Y, L133F, V149I, T152V | K POTASSIUM ION × 1 CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；277 K；2M sodium/potassium phosphate, 40 mM BME, 550 mM NaCl, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.57 Å R-free 0.221 |
| 1P3N CORE REDESIGN BACK-REVERTANT I103V/CORE10 Deposited 2003-04-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, V87I, I100V, M102L, M106I, V111A, M120Y, L133F, V149I, T152V, C97A | PO4 PHOSPHATE ION × 1 K POTASSIUM ION × 1 CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；277 K；Potassium phosphate, sodium PHOSPHATE, NaCl, BME, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.55 Å R-free 0.247 |
| 1P46 T4 lysozyme core repacking mutant M106I/TA Deposited 2003-04-21 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, M106I | K POTASSIUM ION × 1 CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；277 K；Potassium/Sodium Phosphate, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.67 Å R-free 0.240 |
| 1P56 Duplication-extension of Helix A of T4 lysozyme Deposited 2003-04-25 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–163（163 aa）
|
Mutation：C54T, C97A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；35% PEG 4000, 50mM phosphate buffer, 5% isopropanol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.80 Å R-free 0.273 |
| 1P5C Circular permutation of Helix A in T4 lysozyme Deposited 2003-04-25 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
12–163（152 aa）
|
Mutation：C54T, C97A, G12M | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；298 K；30% PEG 3400, 50mM Phosphate buffer, 5% isopropanol, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.50 Å R-free 0.310 |
| 1P5C Circular permutation of Helix A in T4 lysozyme Deposited 2003-04-25 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
12–163（152 aa）
|
Mutation：C54T, C97A, G12M | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；298 K；30% PEG 3400, 50mM Phosphate buffer, 5% isopropanol, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.50 Å R-free 0.310 |
| 1P5C Circular permutation of Helix A in T4 lysozyme Deposited 2003-04-25 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
12–163（152 aa）
|
Mutation：C54T, C97A, G12M | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；298 K；30% PEG 3400, 50mM Phosphate buffer, 5% isopropanol, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.50 Å R-free 0.310 |
| 1P5C Circular permutation of Helix A in T4 lysozyme Deposited 2003-04-25 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
12–163（152 aa）
|
Mutation：C54T, C97A, G12M | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；298 K；30% PEG 3400, 50mM Phosphate buffer, 5% isopropanol, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.50 Å R-free 0.310 |
| 1P64 T4 LYSOZYME CORE REPACKING MUTANT L133F/TA Deposited 2003-04-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L133F | K POTASSIUM ION × 1 CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；277 K；K/Na Phosphate, NaCl, BME, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.62 Å R-free 0.251 |
| 1P6Y T4 LYSOZYME CORE REPACKING MUTANT M120Y/TA Deposited 2003-04-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, M120Y | PO4 PHOSPHATE ION × 1 K POTASSIUM ION × 1 CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；277 K；K/Na Phosphate, NaCl, BME, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.54 Å R-free 0.237 |
| 1P7S T4 LYSOZYME CORE REPACKING MUTANT V103I/TA Deposited 2003-05-05 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T/C97A/V103I | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；277 K；2M K/Na phosphate, NaCl, BME, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.50 Å R-free 0.266 |
| 1PQD T4 LYSOZYME CORE REPACKING MUTANT CORE10/TA Deposited 2003-06-18 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T/V87I/C97A/I100V/M102L/V103I/M106I/V111A/M120Y/L133F/V149I/T152V | K POTASSIUM ION × 1 CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；Potassium phosphate, sodium PHOSPHATE, NaCl, BME, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 100K
|
Resolution 1.65 Å |
| 1PQI T4 LYSOZYME CORE REPACKING MUTANT I118L/CORE7/TA Deposited 2003-06-18 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T/I78V/V87M/C97A/L118I/M120Y/L133F/V149I/T152V | K POTASSIUM ION × 1 CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；277 K；2 M Na/K Phosphate, 550 mM NaCl, 40 mM BME, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.70
|
Resolution 1.57 Å R-free 0.266 |
| 1PQJ T4 LYSOZYME CORE REPACKING MUTANT A111V/CORE10/TA Deposited 2003-06-18 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T/V87I/C97A/I100V/M102L/V103I/M106I/V111A/M120Y/L133F/V149I/T152V | K POTASSIUM ION × 1 CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；277 K；Potassium phosphate, Sodium PHOSPHATE, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.90 Å R-free 0.269 |
| 1PQK Repacking of the Core of T4 Lysozyme by Automated Design Deposited 2003-06-18 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, G77A, I78V, C97A, L118I, M120Y, L133F, V149I, T152V | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；277 K；Potassium phosphate, sodium PHOSPHATE, NaCl, BME, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.70
|
Resolution 2.00 Å R-free 0.277 |
| 1PQK Repacking of the Core of T4 Lysozyme by Automated Design Deposited 2003-06-18 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：C54T, G77A, I78V, C97A, L118I, M120Y, L133F, V149I, T152V | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；277 K；Potassium phosphate, sodium PHOSPHATE, NaCl, BME, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.70
|
Resolution 2.00 Å R-free 0.277 |
| 1PQK Repacking of the Core of T4 Lysozyme by Automated Design Deposited 2003-06-18 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
1–164（164 aa）
|
Mutation：C54T, G77A, I78V, C97A, L118I, M120Y, L133F, V149I, T152V | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；277 K；Potassium phosphate, sodium PHOSPHATE, NaCl, BME, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.70
|
Resolution 2.00 Å R-free 0.277 |
| 1PQM T4 Lysozyme Core Repacking Mutant V149I/T152V/TA Deposited 2003-06-18 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T/C97A/V149I/T152V | PO4 PHOSPHATE ION × 1 K POTASSIUM ION × 1 CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；277 K；Potassium phosphate, sodium PHOSPHATE, NaCl, BME, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.70
|
Resolution 1.52 Å R-free 0.219 |
| 1PQO T4 Lysozyme Core Repacking Mutant L118I/TA Deposited 2003-06-18 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T/C97A/L118I | K POTASSIUM ION × 1 CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；277 K；Potassium phosphate, sodium PHOSPHATE, NaCl, BME, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.70
|
Resolution 1.65 Å R-free 0.261 |
| 1QS5 THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME Deposited 1999-06-25 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T, C97A, A98L | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；POTASSIUM PHOSPHATE, SODIUM PHOSPHATE, BME, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.50 Å |
| 1QS9 THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME Deposited 1999-06-25 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T, C97A, A98V | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；POTASSIUM PHOSPHATE, SODIUM PHOSPHATE, BME, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.85 Å |
| 1QSB THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME Deposited 1999-06-20 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：A98C, C54T, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；pH 7.00
|
Resolution 1.80 Å |
| 1QSQ CAVITY CREATING MUTATION Deposited 1999-06-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, M106A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.6；277 K；NA2PO4, NACL, pH 6.6, VAPOR DIFFUSION, HANGING DROP
|
Resolution 1.90 Å |
| 1QT3 T26D MUTANT OF T4 LYSOZYME Deposited 1999-06-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T26D, C54T, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 1QT4 T26Q MUTANT OF T4 LYSOZYME Deposited 1999-06-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T26Q, C54T, C97A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.10 Å |
| 1QT5 D20E MUTANT STRUCTURE OF T4 LYSOZYME Deposited 1999-06-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：D20E, C54T, C97A | HED 2-HYDROXYETHYL DISULFIDE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1QT6 E11H Mutant of T4 Lysozyme Deposited 1999-06-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：E11H, C54T, C97A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1QT7 E11N Mutant of T4 Lysozyme Deposited 1999-06-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：E11N, C54T, C97A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 1QT8 T26H Mutant of T4 Lysozyme Deposited 1999-06-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T26H, C54T, C97A | HED 2-HYDROXYETHYL DISULFIDE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1QTB THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME Deposited 1999-06-26 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：A42V, C54T, C97A | HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；potassium phosphate, sodium phosphate, BME, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.90 Å |
| 1QTC THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME Deposited 1999-06-26 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T, C97A, A129F | CL CHLORIDE ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；POTASSIUM PHOSPHATE, SODIUM PHOSPHATE, BME, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.50 Å |
| 1QTD THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME Deposited 1999-06-27 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T, C97A, A129W | HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；potassium phosphate, sodium phosphate, BME, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.50 Å |
| 1QTH THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME Deposited 1999-06-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, A98M | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.4；277 K；PEG3.4K, magnesium chloride, Hepes, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.90 Å |
| 1QTH THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME Deposited 1999-06-28 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：C54T, C97A, A98M | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.4；277 K；PEG3.4K, magnesium chloride, Hepes, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.90 Å |
| 1QTV T26E APO STRUCTURE OF T4 LYSOZYME Deposited 1999-06-29 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T26E, C54T, C97A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.30 Å |
| 1QTZ D20C MUTANT OF T4 LYSOZYME Deposited 1999-06-29 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：D20C, C54T, C97A | BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 1QUD L99G MUTANT OF T4 LYSOZYME Deposited 1999-07-01 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T, C97A, L99G | CL CHLORIDE ION × 2 HEZ HEXANE-1,6-DIOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.75 Å |
| 1QUG E108V MUTANT OF T4 LYSOZYME Deposited 1999-07-01 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T, C97A, E108V | CL CHLORIDE ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1QUH L99G/E108V MUTANT OF T4 LYSOZYME Deposited 1999-07-01 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T, C97A, L99G, E108V | CL CHLORIDE ION × 2 HEZ HEXANE-1,6-DIOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 1QUO L99A/E108V MUTANT OF T4 LYSOZYME Deposited 1999-07-01 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T, C97A, L99A, E108V | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 1SSW Crystal structure of phage T4 lysozyme mutant Y24A/Y25A/T26A/I27A/C54T/C97A Deposited 2004-03-24 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：Y24A/Y25A/T26A/I27A/C54T/C97A | BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.13 Å R-free 0.215 |
| 1SSY Crystal structure of phage T4 lysozyme mutant G28A/I29A/G30A/C54T/C97A Deposited 2004-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：G28A/I29A/G30A/C54T/C97A | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.40 Å R-free 0.236 |
| 1SSY Crystal structure of phage T4 lysozyme mutant G28A/I29A/G30A/C54T/C97A Deposited 2004-03-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：G28A/I29A/G30A/C54T/C97A | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.40 Å R-free 0.236 |
| 1SWY Use of a Halide Binding Site to Bypass the 1000-atom Limit to Ab initio Structure Determination Deposited 2004-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：D72A, R96E | RB RUBIDIUM ION × 5 CL CHLORIDE ION × 5 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；277 K；sodium:potassium phosphate, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.70
|
Resolution 1.06 Å R-free 0.147 |
| 1SWZ Use of an ion-binding site to bypass the 1000-atom limit to ab initio structure determination by direct methods Deposited 2004-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：D72A, R96E | PO4 PHOSPHATE ION × 1 RB RUBIDIUM ION × 5 CL CHLORIDE ION × 4 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；sodium:potassium phosphate, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 100K, pH 6.70
|
Resolution 1.06 Å R-free 0.151 |
| 1SX2 Use of a Halide Binding Site to Bypass the 1000-atom Limit to Structure Determination by Direct Methods Deposited 2004-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：D72A, R96E | RB RUBIDIUM ION × 5 CL CHLORIDE ION × 5 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；sodium:potassium phosphate, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 100K, pH 6.70
|
Resolution 1.06 Å R-free 0.143 |
| 1SX7 Use of an ion-binding site to bypass the 1000-atom limit to ab initio structure determination by direct methods Deposited 2004-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：D72A, R96E | RB RUBIDIUM ION × 5 CL CHLORIDE ION × 4 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；sodium:potassium phosphate, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 100K, pH 6.70
|
Resolution 1.06 Å R-free 0.145 |
| 1T6H Crystal Structure T4 Lysozyme incorporating an unnatural amino acid p-iodo-L-phenylalanine at position 153 Deposited 2004-05-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：F153(PIL) Non-standard monomer：Yes (specific site not provided by mmCIF) | CL CHLORIDE ION × 3 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；0.25M NaCl. 2.0M Na/K phosphate buffer, 15mM hydroxyethyl disulfide, pH 6.7, VAPOR DIFFUSION, HANGING DROP
|
Resolution 2.01 Å R-free 0.210 |
| 1T8A USE OF SEQUENCE DUPLICATION TO ENGINEER A LIGAND-TRIGGERED LONG-DISTANCE MOLECULAR SWITCH IN T4 Lysozyme Deposited 2004-05-11 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L39I, R63A, C54T,C97A | CL CHLORIDE ION × 1 GAI GUANIDINE × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；1.8 M MIXED POTASSIUM AND SODIUM PHOSPHATE. 0.2 M GUANIDINIUM CHLORIDE, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.00 Å R-free 0.251 |
| 1T8F Crystal structure of phage T4 lysozyme mutant R14A/K16A/I17A/K19A/T21A/E22A/C54T/C97A Deposited 2004-05-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R14A,K16A,I17A,K19A,T21A,E22A,C54T,C97A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.15 Å R-free 0.275 |
| 1T8G Crystal structure of phage T4 lysozyme mutant L32A/L33A/T34A/C54T/C97A/E108V Deposited 2004-05-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L32A,L33A,T34A,E108V,C54T,C97A | PO4 PHOSPHATE ION × 1 CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å R-free 0.215 |
| 1T8G Crystal structure of phage T4 lysozyme mutant L32A/L33A/T34A/C54T/C97A/E108V Deposited 2004-05-12 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric |
Chain A
1–164（164 aa）
|
Mutation：L32A,L33A,T34A,E108V,C54T,C97A | PO4 PHOSPHATE ION × 8 CL CHLORIDE ION × 16 BME BETA-MERCAPTOETHANOL × 8 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å R-free 0.215 |
| 1T97 Use of sequence duplication to engineer a ligand-triggered long-distance molecular switch in T4 Lysozyme Deposited 2004-05-14 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；289 K；30% POLY-ETHYLENE GLYCOL 3400, 100MM HEPES BUFFER, 200MM AMMONIUM ACETATE, pH 7.50, VAPOR DIFFUSION, HANGING DROP, temperature 289K
|
Resolution 2.70 Å R-free 0.290 |
| 1T97 Use of sequence duplication to engineer a ligand-triggered long-distance molecular switch in T4 Lysozyme Deposited 2004-05-14 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；289 K；30% POLY-ETHYLENE GLYCOL 3400, 100MM HEPES BUFFER, 200MM AMMONIUM ACETATE, pH 7.50, VAPOR DIFFUSION, HANGING DROP, temperature 289K
|
Resolution 2.70 Å R-free 0.290 |
| 1TLA HYDROPHOBIC CORE REPACKING AND AROMATIC-AROMATIC INTERACTION IN THE THERMOSTABLE MUTANT OF T4 LYSOZYME SER 117 (RIGHT ARROW) PHE Deposited 1993-03-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | PO4 PHOSPHATE ION × 1 CL CHLORIDE ION × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 1XEP Catechol in complex with T4 lysozyme L99A/M102Q Deposited 2004-09-10 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A, M102Q | PO4 PHOSPHATE ION × 1 CAQ CATECHOL × 1 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277 K；phosphate, pH 6.8-7.3, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.55 Å R-free 0.219 |
| 1ZUR Crystal structure of spin labeled T4 Lysozyme (V131R1F) Deposited 2005-05-31 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, V131C | R1F S-[(1-oxyl-2,2,5,5-tetramethyl-4-phenyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 CL CHLORIDE ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；293 K；potassium phosphate, sodium phospahte, sodium choloride, sodium azide, oxidized beta-mercaptoehtanol, isopropanol, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 1.60 Å R-free 0.214 |
| 1ZWN Crystal structure of spin labeled T4 Lysozyme (V131R1B) Deposited 2005-06-03 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, V131C | R1B S-[(1-oxyl-2,2,4,5,5-pentamethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 AZI AZIDE ION × 2 CL CHLORIDE ION × 3 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.6；278 K；potassium phosphate, sodium phospahte, sodium choloride, sodium azide, oxidized beta-mercaptoehtanol, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 278K
|
Resolution 1.80 Å R-free 0.222 |
| 1ZYT Crystal structure of spin labeled T4 Lysozyme (A82R1) Deposited 2005-06-10 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T/C97A/A82C | MTN S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 AZI AZIDE ION × 1 CL CHLORIDE ION × 3 HED 2-HYDROXYETHYL DISULFIDE × 1 |
Experimental method not declared
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.8；293 K；potassium phosphate, sodium phospahte, sodium choloride, sodium azide, oxidized beta-mercaptoehtanol , pH 6.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K
|
Resolution 1.70 Å R-free 0.206 |
| 200L THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME Deposited 1995-11-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L121A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；pH 6.7
|
Resolution 1.95 Å |
| 201L HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME Deposited 1993-10-12 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 201L HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME Deposited 1993-10-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Not recorded | BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 205L HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME Deposited 1993-10-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.10 Å |
| 206L PHAGE T4 LYSOZYME Deposited 1996-03-19 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：A42S, C54T, C97A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；pH 6.7
|
Resolution 1.75 Å |
| 209L PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME Deposited 1996-09-23 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, INS(A73-AAA), C97A | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.70 Å |
| 210L PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME Deposited 1996-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, DEL(A73), C97A | HED 2-HYDROXYETHYL DISULFIDE × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.89 Å |
| 211L PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME Deposited 1996-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, INS(E108-A) | HED 2-HYDROXYETHYL DISULFIDE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 212L PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME Deposited 1996-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, INS(L164-AAAA) | HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
MUTANT CRYSTALLIZED FROM PEG IN CONTRAST TO L164AAAA WHICH WAS CRYSTALLIZED FROM PHOSPHATE.
|
Resolution 1.76 Å |
| 213L PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME Deposited 1996-09-23 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, INS(N140-A) | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.13 Å |
| 214L PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME Deposited 1996-09-23 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, INS(R119-A) | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.89 Å |
| 215L PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME Deposited 1996-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, INS(T115-A) | HED 2-HYDROXYETHYL DISULFIDE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.96 Å |
| 216L STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Deposited 1994-05-10 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.10 Å |
| 216L STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Deposited 1994-05-10 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.10 Å |
| 217L STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME Deposited 1993-04-27 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 1 BME BETA-MERCAPTOETHANOL × 3 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 218L PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME Deposited 1996-09-23 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, INS(V131-A) | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.05 Å |
| 219L PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME Deposited 1996-09-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, INS(L164-AAAA) | HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
MUTANT WAS CRYSTALLIZED FROM PHOSPHATE IN CONTRAST TO L1 64AAA_PEG WHICH WAS CRYSTALLIZED FROM PEG.
|
Resolution 1.66 Å |
| 220L GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS Deposited 1997-06-25 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, M102A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 BNZ BENZENE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；CRYSTALS GROWN IN HANGING DROPS AT 4 DEGREES C. PROTEIN 10-20 MG/ML IN A BUFFER CONTAINING 0.1M NA2PO4 PH 6.6, 0.55 M NACL WAS DILUTED 1/2 WITH A WELL SOLUTION CONTAINING 1.8-2.2M NA/KPO4 PH 6.3-7.1., pH 7.0, vapor diffusion - hanging drop, temperature 277K
|
Resolution 1.85 Å |
| 221L 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 Deposited 1993-05-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 222L GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS Deposited 1997-06-25 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, M102A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；CRYSTALS GROWN IN HANGING DROPS AT 4 DEGREES C. PROTEIN 10-20 MG/ML IN A BUFFER CONTAINING 0.1M NA2PO4 PH 6.6, 0.55 M NACL WAS DILUTED 1/2 WITH A WELL SOLUTION CONTAINING 1.8-2.2M NA/KPO4 PH 6.3-7.1., pH 7.0, vapor diffusion - hanging drop, temperature 277K
|
Resolution 1.90 Å |
| 223L GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS Deposited 1997-06-25 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L133G | CL CHLORIDE ION × 1 BME BETA-MERCAPTOETHANOL × 3 BNZ BENZENE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；CRYSTALS GROWN IN HANGING DROPS AT 4 DEGREES C. PROTEIN 10-20 MG/ML IN A BUFFER CONTAINING 0.1M NA2PO4 PH 6.6, 0.55 M NACL WAS DILUTED 1/2 WITH A WELL SOLUTION CONTAINING 1.8-2.2M NA/KPO4 PH 6.3-7.1 WITH OXIDIZED/REDUCED BME. CRYSTALS WERE EXPOSED TO BENZENE VAPOR IN A CAPILLARY FOR SEVERAL DAYS AT ROOM TEMPERATURE., pH 7.0, vapor diffusion - hanging drop, temperature 277K
|
Resolution 1.90 Å |
| 224L 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 Deposited 1993-09-27 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.85 Å |
| 225L GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS Deposited 1997-06-25 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L133G | PXY PARA-XYLENE × 1 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；CRYSTALS GROWN IN HANGING DROPS AT 4 DEGREES C. PROTEIN 10-20 MG/ML IN A BUFFER CONTAINING 0.1M NA2PO4 PH 6.6, 0.55 M NACL WAS DILUTED 1/2 WITH A WELL SOLUTION CONTAINING 1.8-2.2M NA/KPO4 PH 6.3-7.1 WITH OXIDIZED/REDUCED BME. CRYSTALS WERE EXPOSED TO P-XYLENE VAPOR IN A CAPILLARY FOR SEVERAL DAYS AT ROOM TEMPERATURE., pH 7.0, vapor diffusion - hanging drop, temperature 277K
|
Resolution 1.90 Å |
| 226L GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS Deposited 1997-06-25 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L133G | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；CRYSTALS GROWN IN HANGING DROPS AT 4 DEGREES C. PROTEIN 10-20 MG/ML IN A BUFFER CONTAINING 0.1M NA2PO4 PH 6.6, 0.55 M NACL WAS DILUTED 1/2 WITH A WELL SOLUTION CONTAINING 1.8-2.2M NA/KPO4 PH 6.3-7.1 WITH OXIDIZED/REDUCED BME., pH 7.0, vapor diffusion - hanging drop, temperature 277K
|
Resolution 1.80 Å |
| 227L GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS Deposited 1997-06-25 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, F104A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 BNZ BENZENE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；CRYSTALS GROWN IN HANGING DROPS AT 4 DEGREES C. PROTEIN 10-20 MG/ML IN A BUFFER CONTAINING 0.1M NA2PO4 PH 6.6, 0.55 M NACL WAS DILUTED 1/2 WITH A WELL SOLUTION CONTAINING 1.8-2.2M NA/KPO4 PH 6.3-7.1. CRYSTALS WERE EXPOSED TO BENZENE VAPOR IN A CAPILLARY FOR SEVERAL DAYS., pH 7.0, vapor diffusion - hanging drop, temperature 277K
|
Resolution 2.00 Å |
| 228L GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS Deposited 1997-06-25 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, F104A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；CRYSTALS GROWN IN HANGING DROPS AT 4 DEGREES C. PROTEIN 10-20 MG/ML IN A BUFFER CONTAINING 0.1M NA2PO4 PH 6.6, 0.55 M NACL WAS DILUTED 1/2 WITH A WELL SOLUTION CONTAINING 1.8-2.2M NA/KPO4 PH 6.3-7.1., pH 7.0, vapor diffusion - hanging drop, temperature 277K
|
Resolution 1.90 Å |
| 229L GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS Deposited 1997-06-26 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, R95A, C97A | CL CHLORIDE ION × 2 GAI GUANIDINE × 1 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；CRYSTALS GROWN IN HANGING DROPS AT 4 DEGREES C. PROTEIN 10-20 MG/ML IN A BUFFER CONTAINING 25 MM HEPES PH 7.5 WAS DILUTED 1/2 WITH A WELL SOLUTION CONTAINING 0.1 M NACL, 0.1 M KPO4,20% W/V PEG 3350,PH 7.1, 0.25 M GUAD-HCL (LIGAND)., pH 7.0, vapor diffusion - hanging drop, temperature 277K
|
Resolution 1.80 Å |
| 230L T4 LYSOZYME MUTANT M6L Deposited 1997-10-02 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：M6L, C54T, C97A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；M6L WAS AT 15MG/ML IN A BUFFER CONTAINING 0.1M NA2PO4 PH 6.6, 0.55 M NACL. IT WAS DILUTED BY 1/2 WITH A SOLUTION 1.8M IN NA/KPO4 PH 6.9. THIS WAS ALSO THE WELL SOLUTION. HANGING DROP METHODS WERE USED., pH 7.0, vapor diffusion - hanging drop
|
Resolution 1.90 Å |
| 231L T4 LYSOZYME MUTANT M106K Deposited 1997-10-03 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, M106K | CL CHLORIDE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；M106K WAS AT 19MG/ML IN A BUFFER CONTAINING 0.1M NA2PO4 PH 6.6, 0.55 M NACL. IT WAS DILUTED BY 1/2 WITH A SOLUTION 1.8M IN NA/KPO4 PH 6.9. THIS WAS ALSO THE WELL SOLUTION. HANGING DROP METHODS WERE USED., pH 7.0, vapor diffusion - hanging drop
|
Resolution 2.50 Å |
| 232L T4 LYSOZYME MUTANT M120K Deposited 1997-10-05 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, M120K | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；M120K WAS AT 32MG/ML IN A BUFFER CONTAINING 0.1M NA2PO4 PH 6.6, 0.55 M NACL. IT WAS DILUTED BY 1/2 WITH A SOLUTION 2.0M IN NA/KPO4 PH 7.1. THIS WAS ALSO THE WELL SOLUTION. HANGING DROP METHODS WERE USED., pH 7.0, vapor diffusion - hanging drop, temperature 277K
|
Resolution 1.73 Å |
| 233L T4 LYSOZYME MUTANT M120L Deposited 1997-10-07 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, M120L | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；pH 7.0
|
Resolution 1.90 Å |
| 234L T4 LYSOZYME MUTANT M106L Deposited 1997-10-07 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, M106L | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；pH 7.0
|
Resolution 1.90 Å |
| 235L THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT Deposited 1997-10-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, V111A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.8；pH 6.8
|
Resolution 1.90 Å |
| 236L THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT Deposited 1997-10-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, V87A, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.8；pH 6.8
|
Resolution 1.90 Å |
| 237L THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT Deposited 1997-10-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, V149A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.8；pH 6.8
|
Resolution 1.70 Å |
| 238L THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT Deposited 1997-10-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, V103A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 239L THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT Deposited 1997-10-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：I17A, C54T, C97A | CL CHLORIDE ION × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 240L THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT Deposited 1997-10-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：I27A, C54T, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.8；pH 6.8
|
Resolution 1.75 Å |
| 241L THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT Deposited 1997-10-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：I29A, C54T, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.8；pH 6.8
|
Resolution 1.70 Å |
| 242L THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT Deposited 1997-10-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：I50A, C54T, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.8；pH 6.8
|
Resolution 1.80 Å |
| 243L THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT Deposited 1997-10-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, I58A, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.8；pH 6.8
|
Resolution 1.75 Å |
| 244L THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT Deposited 1997-10-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, I100A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 245L THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT Deposited 1997-10-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：M6A, C54T, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.8；pH 6.8
|
Resolution 1.80 Å |
| 246L THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT Deposited 1997-10-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, F67A, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.8；pH 6.8
|
Resolution 1.80 Å |
| 247L THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT Deposited 1997-10-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, L84A, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.8；pH 6.8
|
Resolution 1.75 Å |
| 248L THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT Deposited 1997-10-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：I27A, I29A, C54T, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.8；pH 6.8
|
Resolution 1.90 Å |
| 249L THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT Deposited 1997-10-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：I27A, C54T, I58A, C97A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.8；pH 6.8
|
Resolution 1.90 Å |
| 250L THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT Deposited 1997-10-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：I29A, C54T, I58A, C97A, | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.8；pH 6.8
|
Resolution 1.80 Å |
| 251L THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT Deposited 1997-10-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L121A, L133A | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.8；pH 6.8
|
Resolution 2.60 Å |
| 252L GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS Deposited 1997-10-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, M102A, M106A | CL CHLORIDE ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；CRYSTALS GROWN IN HANGING DROPS AT 4 DEGREES C. PROTEIN 10-20 MG/ML IN A BUFFER CONTAINING 0.5 M NACL 0.1 M NAPO4 PH 6.5 WAS DILUTED 1/2 WITH A WELL SOLUTION CONTAINING MIXED K/NAPO4 PH 6.3-7.1,1.8-2.2 MOLAR., pH 7.0, vapor diffusion - hanging drop, temperature 277K
|
Resolution 2.10 Å |
| 253L LYSOZYME Deposited 1997-11-10 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：D20A, C54T, C97A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 254L LYSOZYME Deposited 1997-11-10 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：D20S, C54T, C97A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å |
| 255L HYDROLASE Deposited 1997-11-10 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：D20N, C54T, C97A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 256L BACTERIOPHAGE T4 LYSOZYME Deposited 1998-02-24 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：M6I | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 257L AN ADAPTABLE METAL-BINDING SITE ENGINEERED INTO T4 LYSOZYME Deposited 1999-01-05 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21H,C54T,C97A,T142H | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；CRYSTALS GROWN IN HANGING DROPS AT 4 DEGREES C. PROTEIN 10-20 MG/ML IN A
BUFFER CONTAINING SODIUM PHOSPHATE PH 5.4, 200 MM NACL, WAS DILUTED 1/2 WITH A
WELL SOLUTION CONTAINING 1.8-2.0 M NA/K PHOSPHATE, 200MM NACL, PH 6.5-7.5, AND
5MM OXIDIZED BME 10% V/V ISOPROPANOL,18% W/V PEG 8000, PH 7.5
|
Resolution 1.90 Å |
| 258L AN ADAPTABLE METAL-BINDING SITE ENGINEERED INTO T4 LYSOZYME Deposited 1999-01-05 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 ZN ZINC ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；pH 7.50
|
Resolution 1.80 Å |
| 259L AN ADAPTABLE METAL-BINDING SITE ENGINEERED INTO T4 LYSOZYME Deposited 1999-02-10 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T,C97A,T21H,T142H | CL CHLORIDE ION × 2 CO COBALT (II) ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.92 Å |
| 260L AN ADAPTABLE METAL-BINDING SITE ENGINEERED INTO T4 LYSOZYME Deposited 1999-03-01 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T,C97A,T21H,T142H | CL CHLORIDE ION × 2 NI NICKEL (II) ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å |
| 261L STRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDING Deposited 1999-05-11 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–50（50 aa）
Chain A
51–162（112 aa）
|
Mutation：L39I Mutation：L39I | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；CRYSTALS WERE GROWN FROM 20% POLYETHYLENE GLYCOL 6000, 20% ISOPROPANOL, 50MM
TRIS-HCL PH 7.5
|
Resolution 2.50 Å |
| 262L STRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDING Deposited 1999-05-11 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–50（50 aa）
Chain A
51–162（112 aa）
|
Mutation：L39I Mutation：L39I | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；CRYSTALS WERE GROWN FROM 20%
POLYETHYLENE GLYCOL 6000, 20% ISOPROPANOL,
50MM TRIS-HCL PH 7.5
|
Resolution 2.50 Å |
| 262L STRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDING Deposited 1999-05-11 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–50（50 aa）
Chain B
51–162（112 aa）
|
Mutation：L39I Mutation：L39I | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；CRYSTALS WERE GROWN FROM 20%
POLYETHYLENE GLYCOL 6000, 20% ISOPROPANOL,
50MM TRIS-HCL PH 7.5
|
Resolution 2.50 Å |
| 29AJ Crystal Structure of the human mARC1 M187K variant Deposited 2026-03-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
1–159（159 aa）
|
Mutation：M187K | MTE PHOSPHONIC ACIDMONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,7,8A,9,10,10A-HEXAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL)ESTER × 1 B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 MOO MOLYBDATE ION × 4 EFK oxidanyl(oxidanylidene)molybdenum × 1 CL CHLORIDE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；100 mM Bis-TRIS propane, 20 mM Na2MoO4, 10 mM TCEP, 27.5 % PEG3350
|
Resolution 1.63 Å R-free 0.215 |
| 2A4T Crystal structure of spin labeled T4 Lysozyme (V131R7) Deposited 2005-06-29 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T,C97A,V131C | R7A S-[(4-bromo-1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 AZI AZIDE ION × 1 CL CHLORIDE ION × 3 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；273 K；potassium phosphate, sodium phospahte, sodium choloride, sodium azide, oxidized beta-mercaptoehtanol, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 273K
|
Resolution 1.70 Å R-free 0.215 |
| 2B6T T4 Lysozyme mutant L99A at 200 MPa Deposited 2005-10-03 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T,C97A,L99A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；293 K；~2.0 Molar Na/K phosphates, 50 mM beta-mercaptoethanol, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 293, temperature 20K
|
Resolution 2.10 Å R-free 0.198 |
| 2B6W T4 Lysozyme mutant L99A at 200 MPa Deposited 2005-10-03 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T,C97A,L99A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；293 K；~2 M Na/K phosphate, 50 mM beta-mercaptoethanol, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.20 Å R-free 0.208 |
| 2B6X T4 Lysozyme mutant L99A at 200 MPa Deposited 2005-10-03 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T,C97A,L99A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；293 K；~ 2.0 M Na/K phosphate, 50 mM beta-mercaptoethanol, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.11 Å R-free 0.204 |
| 2B6Y T4 Lysozyme mutant L99A at ambient pressure Deposited 2005-10-03 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T,C97A,L99A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；293 K；~ 2.0 M Na/K phosphate, 50 mM beta-mercaptoethanol, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.40 Å R-free 0.212 |
| 2B6Z T4 Lysozyme mutant L99A at ambient pressure Deposited 2005-10-03 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T,C97A,L99A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；293 K；~2.0 M Na/K phosphate, 50 mM beta-mercaptoethanol, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.40 Å R-free 0.197 |
| 2B70 T4 Lysozyme mutant L99A at ambient pressure Deposited 2005-10-03 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T,C97A,L99A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；293 K；~ 2.0 M Na/K phosphate, 50 mM beta-mercaptoethanol, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.40 Å R-free 0.218 |
| 2B72 T4 Lysozyme mutant L99A at 100 MPa Deposited 2005-10-03 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T,C97A,L99A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；293 K；~ 2.0 M Na/K phosphate, 50 mM beta-mercaptoethanol, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.10 Å R-free 0.212 |
| 2B73 T4 Lysozyme mutant L99A at 100 MPa Deposited 2005-10-03 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T,C97A,L99A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；293 K；~ 2.0 M Na/K phosphate, 50 mM beta-mercaptoethanol, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.15 Å R-free 0.219 |
| 2B74 T4 Lysozyme mutant L99A at 100 MPa Deposited 2005-10-03 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T,C97A,L99A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；293 K；~ 2.0 M Na/K phosphate, 50 mM beta-mercaptoethanol, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.10 Å R-free 0.232 |
| 2B75 T4 Lysozyme mutant L99A at 150 MPa Deposited 2005-10-03 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：C54T,C97A,L99A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；293 K；~2.0 M Na/K phosphate, 50mM beta-mercaptoethanol, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.10 Å R-free 0.214 |
| 2B7X Sequential reorganization of beta-sheet topology by insertion of a single strand Deposited 2005-10-05 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, residues (YTIGIG) inserted after residue G30 | SO4 SULFATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；Polyehtylene glycol 4000, 50mM Ammonium sulfate, , pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 3.00 Å R-free 0.319 |
| 2B7X Sequential reorganization of beta-sheet topology by insertion of a single strand Deposited 2005-10-05 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：C54T, C97A, residues (YTIGIG) inserted after residue G30 | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；Polyehtylene glycol 4000, 50mM Ammonium sulfate, , pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 3.00 Å R-free 0.319 |
| 2B7X Sequential reorganization of beta-sheet topology by insertion of a single strand Deposited 2005-10-05 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
1–164（164 aa）
|
Mutation：C54T, C97A, residues (YTIGIG) inserted after residue G30 | SO4 SULFATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；Polyehtylene glycol 4000, 50mM Ammonium sulfate, , pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 3.00 Å R-free 0.319 |
| 2B7X Sequential reorganization of beta-sheet topology by insertion of a single strand Deposited 2005-10-05 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
1–164（164 aa）
|
Mutation：C54T, C97A, residues (YTIGIG) inserted after residue G30 | SO4 SULFATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；Polyehtylene glycol 4000, 50mM Ammonium sulfate, , pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 3.00 Å R-free 0.319 |
| 2CUU Crystal structure of spin labeled T4 Lysozyme (V131R1) Deposited 2005-05-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T/C97A/V131 | MTN S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 AZI AZIDE ION × 1 CL CHLORIDE ION × 3 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；278 K；potassium phosphate, sodium phospahte, sodium choloride, sodium azide, oxidized beta-mercaptoehtanol, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 278K
|
Resolution 1.75 Å R-free 0.224 |
| 2F2Q High resolution crystal structure of T4 lysozyme mutant L20R63/A liganded to guanidinium ion Deposited 2005-11-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：I39L, A63R, T65C, A108C | CL CHLORIDE ION × 1 GAI GUANIDINE × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.5；277 K；0.5 mM protein, 1.8 M MIXED POTASSIUM AND SODIUM PHOSPHATE, 0.2 M GUANIDINIUM CHLORIDE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, pH 6.50
|
Resolution 1.45 Å R-free 0.223 |
| 2F32 Xray crystal structure of lysozyme mutant L20/R63A liganded to ethylguanidinium Deposited 2005-11-18 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L39I, INS (NAAKSELDKAI -N62), R63A, C65T, C108A | BME BETA-MERCAPTOETHANOL × 1 EGD N-ETHYLGUANIDINE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；1.8 M MIXED POTASSIUM AND SODIUM PHOSPHATE. 0.2 M ETHYL GUANIDINIUM CHLORIDE, pH 6.50, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å R-free 0.245 |
| 2F47 Xray crystal structure of T4 lysozyme mutant L20/R63A liganded to methylguanidinium Deposited 2005-11-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L39I, INS (NAAKSELDKAI -N62), R63A, C65T, C108A | CL CHLORIDE ION × 1 MGX 1-METHYLGUANIDINE × 1 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；1.8 M MIXED POTASSIUM AND SODIUM PHOSPHATE. 0.2 M GUANIDINIUM CHLORIDE, pH 6.50, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.70 Å R-free 0.217 |
| 2HUK Crystal structure of T4 Lysozyme V131C synthetic dimer Deposited 2006-07-26 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–164（164 aa）
|
Mutation：V131C | SO4 SULFATE ION × 8 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.5；295 K；20% PEG 8000, 0.1M Na Cacodylate, pH 6.5, 0.2M Ammonium Acetate, VAPOR DIFFUSION, HANGING DROP, temperature 295K, pH 6.50
|
Resolution 2.00 Å R-free 0.240 |
| 2HUL Crystal structure of T4 Lysozyme S44C synthetic dimer Deposited 2006-07-26 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–164（164 aa）
|
Mutation：S44C | SO4 SULFATE ION × 8 GOL GLYCEROL × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；298 K；2.0 M Ammonium Sulfate, 0.1 M Cacodylate pH 6.7, 0.2 M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 6.70
|
Resolution 1.80 Å R-free 0.192 |
| 2HUL Crystal structure of T4 Lysozyme S44C synthetic dimer Deposited 2006-07-26 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：S44C | SO4 SULFATE ION × 4 GOL GLYCEROL × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；298 K；2.0 M Ammonium Sulfate, 0.1 M Cacodylate pH 6.7, 0.2 M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 6.70
|
Resolution 1.80 Å R-free 0.192 |
| 2HUM Crystal structure of T4 Lysozyme D72C synthetic dimer Deposited 2006-07-26 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–164（164 aa）
Chain B
1–164（164 aa）
|
Mutation：C54T, D72C, C97A Mutation：C54T, D72C, C97A | TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；0.2 M tri-Lithium Citrate, 20% PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.35 Å R-free 0.304 |
| 2IGC Structure of Spin labeled T4 Lysozyme Mutant T115R1A Deposited 2006-09-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A | MTN S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；296 K；1.8 M NaH2PO4, 1.8 M K2HPO4, 240 mM NaCl, 40 mM 2-hydroxyethyl disulfide, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 296K
|
Resolution 1.40 Å R-free 0.198 |
| 2L78 DESIGN AND STRUCTURAL ANALYSIS OF ALTERNATIVE HYDROPHOBIC CORE PACKING ARRANGEMENTS IN BACTERIOPHAGE T4 LYSOZYME Deposited 1992-01-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å |
| 2LC9 Solution Structure of a Minor and Transiently Formed State of a T4 Lysozyme Mutant Deposited 2011-04-26 | Different mutation/modification Different experimental conditions | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L99A, G113A, R119P | No recorded non-water small molecule |
SOLUTION NMR
NMR measurement conditions
pH 5.5；307 K；Ionic strength (raw mmCIF value) 85；Pressure ambient
NMR measurement conditions
pH 5.5；308 K；Ionic strength (raw mmCIF value) 85；Pressure ambient
NMR sample composition
1.5 mM [U-100% 13C; U-100% 15N] T4 L99A/G113A/R119P, 90% H2O/10% D2O | 90% H2O/10% D2O
|
Resolution not provided |
| 2LZM STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME REFINED AT 1.7 ANGSTROMS RESOLUTION Deposited 1986-08-18 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 2NTG Structure of Spin-labeled T4 Lysozyme Mutant T115R7 Deposited 2006-11-07 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, T115C | R7A S-[(4-bromo-1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.6；296 K；2.0 M Na/K Phosphate, 240 mM NaCl, 40 mM 2-hydroxyethyl disulfide, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 296K
|
Resolution 1.40 Å R-free 0.210 |
| 2NTH Structure of Spin-labeled T4 Lysozyme Mutant L118R1 Deposited 2006-11-07 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A | MTN S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；296 K；2.0 M Na/K Phosphate, 240 mM NaCl, 40 mM 2-hydroxyethyl disulfide, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 296K
|
Resolution 1.80 Å R-free 0.212 |
| 2O4W T4 lysozyme circular permutant Deposited 2006-12-05 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
13–164（152 aa）
Chain A
1–12（12 aa）
|
Mutation：C54T, C97A Mutation：C54T, C97A | CL CHLORIDE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；0.9 M K2HPO4, 1.1 M NaH2PO4, pH 6.9, 0.25 M NaCl, 49.0 mM oxidized B-mercaptoethanol, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.90 Å R-free 0.213 |
| 2O79 T4 lysozyme with C-terminal extension Deposited 2006-12-10 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A | PO4 PHOSPHATE ION × 1 CL CHLORIDE ION × 3 GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.6；277 K；0.9 M K2HPO4, 1.1 M NaH2PO4, pH 6.6, 0.25 M NaCl, 49.0 mM oxidized B mercaptoethanol, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å R-free 0.182 |
| 2O7A T4 lysozyme C-terminal fragment Deposited 2006-12-10 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
60–164（105 aa）
Chain A
1–12（12 aa）
|
Mutation：C97A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C97A Non-standard monomer：Yes (specific site not provided by mmCIF) | ACT ACETATE ION × 1 CL CHLORIDE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5；291 K；100 mM NaCacodylate pH 5.0, 200 mM NaAcetate, 26% PEG 8000, VAPOR DIFFUSION, HANGING DROP, temperature 291K
|
Resolution 0.84 Å R-free 0.108 |
| 2OE4 High Pressure Psuedo Wild Type T4 Lysozyme Deposited 2006-12-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain X
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；293 K；~2.0 M NA/K PHOSPHATES, 50 MM BETA-MERCAPTOETHANOL, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.10 Å R-free 0.222 |
| 2OE7 High-Pressure T4 Lysozyme Deposited 2006-12-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain X
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；293 K；~2.0 M NA/K PHOSPHATES, 50 MM BETA-MERCAPTOETHANOL, PH 7.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
|
Resolution 2.10 Å R-free 0.214 |
| 2OE9 High-pressure structure of pseudo-WT T4 Lysozyme Deposited 2006-12-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain X
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；293 K；~2.0 M NA/K PHOSPHATES, 50 MM BETA-MERCAPTOETHANOL, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.01 Å R-free 0.210 |
| 2OEA High-pressure structure of pseudo-WT T4 Lysozyme Deposited 2006-12-28 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain X
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；293 K；~2.0 M NA/K PHOSPHATES, 50 MM BETA-MERCAPTOETHANOL, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.01 Å R-free 0.213 |
| 2OTY 1,2-dichlorobenzene in complex with T4 Lysozyme L99A Deposited 2007-02-09 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain X
1–162（162 aa）
|
Not recorded | PO4 PHOSPHATE ION × 3 BME BETA-MERCAPTOETHANOL × 1 YAN 1,2-DICHLOROBENZENE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.83 Å R-free 0.235 |
| 2OTZ N-methylaniline in complex with T4 Lysozyme L99A Deposited 2007-02-09 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain X
1–162（162 aa）
|
Not recorded | PO4 PHOSPHATE ION × 2 1MR N-METHYLANILINE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.07 Å R-free 0.258 |
| 2OU0 1-methylpyrrole in complex with T4 Lysozyme L99A Deposited 2007-02-09 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain X
1–162（162 aa）
|
Not recorded | PO4 PHOSPHATE ION × 2 MR3 1-METHYL-1H-PYRROLE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.94 Å R-free 0.234 |
| 2OU8 Structure of Spin-labeled T4 Lysozyme Mutant T115R1 at Room Temperature Deposited 2007-02-09 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A | MTN S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 BME BETA-MERCAPTOETHANOL × 4 |
Experimental method not declared
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；296 K；1.8 M Na/K Phosphate, 240 mM NaCl, 40 mM 2-hydroxyethyl disulfide, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 296K
|
Resolution 1.80 Å R-free 0.238 |
| 2OU9 Structure of Spin-labeled T4 Lysozyme Mutant T115R1/R119A Deposited 2007-02-09 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, R119A | MTN S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION；pH 6.9；296 K；2.0 M Na/K Phosphate, 240 mM NaCl, 40 mM 2-hydroxyethyl disulfide, pH 6.9, VAPOR DIFFUSION, temperature 296K
|
Resolution 1.55 Å R-free 0.220 |
| 2Q9D Structure of spin-labeled T4 lysozyme mutant A41R1 Deposited 2007-06-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A | MTN S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 BME BETA-MERCAPTOETHANOL × 1 |
Experimental method not declared
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.6；294 K；2.0 M Na/K Phosphate, 240 mM NaCl, 40 mM 2-hydroxyethyl disulfide, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 294K
|
Resolution 1.40 Å R-free 0.202 |
| 2Q9E Structure of spin-labeled T4 lysozyme mutant S44R1 Deposited 2007-06-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, N55A | MTN S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 |
Experimental method not declared
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.6；294 K；2.0 M Na/K Phosphate, 240 mM NaCl, 40 mM 2-hydroxyethyl disulfide, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 294K
|
Resolution 2.10 Å R-free 0.250 |
| 2Q9E Structure of spin-labeled T4 lysozyme mutant S44R1 Deposited 2007-06-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：C54T, C97A, N55A | MTN S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 HED 2-HYDROXYETHYL DISULFIDE × 2 |
Experimental method not declared
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.6；294 K；2.0 M Na/K Phosphate, 240 mM NaCl, 40 mM 2-hydroxyethyl disulfide, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 294K
|
Resolution 2.10 Å R-free 0.250 |
| 2Q9E Structure of spin-labeled T4 lysozyme mutant S44R1 Deposited 2007-06-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
1–164（164 aa）
|
Mutation：C54T, C97A, N55A | MTN S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 |
Experimental method not declared
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.6；294 K；2.0 M Na/K Phosphate, 240 mM NaCl, 40 mM 2-hydroxyethyl disulfide, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 294K
|
Resolution 2.10 Å R-free 0.250 |
| 2QB0 Structure of the 2TEL crystallization module fused to T4 lysozyme with an Ala-Gly-Pro linker. Deposited 2007-06-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain D
2–162（161 aa）
|
Not recorded | MN MANGANESE (II) ION × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.56 Å R-free 0.252 |
| 2QB0 Structure of the 2TEL crystallization module fused to T4 lysozyme with an Ala-Gly-Pro linker. Deposited 2007-06-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain B
2–162（161 aa）
|
Not recorded | MN MANGANESE (II) ION × 3 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.56 Å R-free 0.252 |
| 2RAY beta-chlorophenetole in complex with T4 lysozyme L99A Deposited 2007-09-17 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain X
1–162（162 aa）
|
Mutation：L99A | PO4 PHOSPHATE ION × 1 258 (2-chloroethoxy)benzene × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
hanging drop；pH 7.1；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 7.1, hanging drop, temperature 277K
|
Resolution 1.80 Å R-free 0.212 |
| 2RAZ 4-(methylthio)nitrobenzene in complex with T4 lysozyme L99A Deposited 2007-09-17 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain X
1–162（162 aa）
|
Mutation：L99A | PO4 PHOSPHATE ION × 3 259 1-(methylsulfanyl)-4-nitrobenzene × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.64 Å R-free 0.221 |
| 2RB0 2,6-difluorobenzylbromide complex with T4 lysozyme L99A Deposited 2007-09-17 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain X
1–162（162 aa）
|
Mutation：L99A | PO4 PHOSPHATE ION × 2 260 2-(bromomethyl)-1,3-difluorobenzene × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 7.1, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.84 Å R-free 0.233 |
| 2RB1 2-ethoxyphenol in complex with T4 lysozyme L99A Deposited 2007-09-17 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain X
1–162（162 aa）
|
Mutation：L99A | PO4 PHOSPHATE ION × 1 261 2-ethoxyphenol × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 7.1, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.70 Å R-free 0.230 |
| 2RB2 3-methylbenzylazide in complex with T4 lysozyme L99A Deposited 2007-09-17 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain X
1–162（162 aa）
|
Mutation：L99A | PO4 PHOSPHATE ION × 3 263 1-(azidomethyl)-3-methylbenzene × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 7.1, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.46 Å R-free 0.213 |
| 2RBN N-phenylglycinonitrile in complex with T4 lysozyme L99A/M102Q Deposited 2007-09-19 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：L99A/M102Q | PO4 PHOSPHATE ION × 1 264 (phenylamino)acetonitrile × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 7.1, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.29 Å R-free 0.191 |
| 2RBO 2-nitrothiophene in complex with T4 lysozyme L99A/M102Q Deposited 2007-09-19 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：L99A/M102Q | PO4 PHOSPHATE ION × 1 265 2-nitrothiophene × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 7.1, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.29 Å R-free 0.193 |
| 2RBP 2-(n-propylthio)ethanol in complex with T4 lysozyme L99A/M102Q Deposited 2007-09-19 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：L99A/M102Q | PO4 PHOSPHATE ION × 1 266 2-(propylsulfanyl)ethanol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 7.1, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.47 Å R-free 0.206 |
| 2RBQ 3-methylbenzylazide in complex with T4 L99A/M102Q Deposited 2007-09-19 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：L99A/M102Q | PO4 PHOSPHATE ION × 1 263 1-(azidomethyl)-3-methylbenzene × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 7.1, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.63 Å R-free 0.240 |
| 2RBR 2-phenoxyethanol in complex with T4 lysozyme L99A/M102Q Deposited 2007-09-19 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：L99A/M102Q | PO4 PHOSPHATE ION × 1 268 2-phenoxyethanol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 7.1, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.43 Å R-free 0.200 |
| 2RBS (r)(+)-3-chloro-1-phenyl-1-propanol in complex with T4 lysozyme L99A/M102Q Deposited 2007-09-19 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：L99A/M102Q | PO4 PHOSPHATE ION × 2 269 (1R)-3-chloro-1-phenylpropan-1-ol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 7.1, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.56 Å R-free 0.205 |
| 2RH1 High resolution crystal structure of human B2-adrenergic G protein-coupled receptor. Deposited 2007-10-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：N187E, C54T, C97A | SO4 SULFATE ION × 6 CAU (2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol × 1 BU1 1,4-BUTANEDIOL × 2 ACM ACETAMIDE × 1 CLR CHOLESTEROL × 3 PLM PALMITIC ACID × 1 12P DODECAETHYLENE GLYCOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC MESOPHASE；pH 6.75；293 K；30-35% v/v PEG 400, 0.1-0.2 M Na2SO4, 0.1 M Bis-tris propane pH 6.5-7.0, 5-7% 1,4-Butanediol, 8-10% Cholesterol, 52-50% Monoolein, pH 6.75, LIPIDIC MESOPHASE, temperature 293K
|
Resolution 2.40 Å R-free 0.232 |
| 3C7W Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme Deposited 2008-02-08 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R96K | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；2 M NA/K PHOSPHATE PH 6.7, 550 MM NACL 50 MM REDUCED BME, 50 MM OXIDIZED BME , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K, pH 6.70
|
Resolution 1.77 Å R-free 0.187 |
| 3C7Y Mutant R96A OF T4 lysozyme in wildtype background at 298K Deposited 2008-02-08 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R96A | CL CHLORIDE ION × 1 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；277 K；2 M NA/K PHOSPHATE PH 6.7
550 mM NACL
50 MM REDUCED BME,
50 MM OXIDIZED BME
, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.95 Å |
| 3C7Z T4 lysozyme mutant D89A/R96H at room temperature Deposited 2008-02-08 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：D89A,R96H | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；2 M NA/K PHOSPHATE PH 6.7 550 MM NACL 50 MM REDUCED BME, 50 MM OXIDIZED BME , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K, pH 6.70
|
Resolution 1.67 Å |
| 3C80 T4 Lysozyme mutant R96Y at room temperature Deposited 2008-02-08 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；2 M NA/K PHOSPHATE PH 6.7 550 MM NACL 50 MM REDUCED BME, 50 MM OXIDIZED BME , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, pH 6.70
|
Resolution 1.99 Å |
| 3C81 Mutant K85A of T4 lysozyme in wildtype background at room temperature Deposited 2008-02-08 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：K85A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；2 M NA/K PHOSPHATE PH 6.7 550 MM NACL 50 MM REDUCED BME, 50 MM OXIDIZED BME , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, pH 6.70
|
Resolution 1.85 Å |
| 3C82 Bacteriophage lysozyme T4 lysozyme mutant K85A/R96H Deposited 2008-02-08 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：K85A,R96H | CL CHLORIDE ION × 1 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；2 M NA/K PHOSPHATE PH 6.7 550 MM NACL 50 MM REDUCED BME, 50 MM OXIDIZED BME , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, pH 6.70
|
Resolution 1.68 Å |
| 3C83 Bacteriophage T4 lysozyme mutant D89A in wildtype background at room temperature Deposited 2008-02-08 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：D89A | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；2 M NA/K PHOSPHATE PH 6.7 550 MM NACL 50 MM REDUCED BME, 50 MM OXIDIZED BME , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, pH 6.70
|
Resolution 1.84 Å |
| 3C8Q Contribution of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme Deposited 2008-02-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R96D | K POTASSIUM ION × 1 CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；2M NA/K PHOSPHATE PH 6.7, 50 MM OXIDIZED BME, 50 MM REDUCED BME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 276K, pH 6.70
|
Resolution 1.64 Å R-free 0.186 |
| 3C8R Contributions of all 20 amino acids at site 96 to stability and structure of T4 lysozyme Deposited 2008-02-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R96G | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；2M NA/K PHOSPHATE 50 MM REDUCED BME 50 MM OXIDIZED BME, PH 6.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 276K, PH 6.70
|
Resolution 1.80 Å R-free 0.172 |
| 3C8S Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme Deposited 2008-02-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R96E | CL CHLORIDE ION × 2 K POTASSIUM ION × 1 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；2 M NA/K PHOSPHATE PH 6.7 50 MM REDUCED BME 50 MM OXIDIZED BME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, pH 6.70
|
Resolution 1.68 Å R-free 0.204 |
| 3CDO Bacteriophage T4 lysozyme mutant R96V in wildtype background at low temperature Deposited 2008-02-27 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R96V | HEZ HEXANE-1,6-DIOL × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；100 MM MES, 200 MM LITHIUM SULFATE, 35% MPD, 50 MM 1,6-HEXANEDIOL, 12.5 MG/ML, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, pH 6.00
|
Resolution 1.87 Å R-free 0.231 |
| 3CDO Bacteriophage T4 lysozyme mutant R96V in wildtype background at low temperature Deposited 2008-02-27 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：R96V | SO4 SULFATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；100 MM MES, 200 MM LITHIUM SULFATE, 35% MPD, 50 MM 1,6-HEXANEDIOL, 12.5 MG/ML, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, pH 6.00
|
Resolution 1.87 Å R-free 0.231 |
| 3CDO Bacteriophage T4 lysozyme mutant R96V in wildtype background at low temperature Deposited 2008-02-27 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
1–164（164 aa）
|
Mutation：R96V | HEZ HEXANE-1,6-DIOL × 2 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；100 MM MES, 200 MM LITHIUM SULFATE, 35% MPD, 50 MM 1,6-HEXANEDIOL, 12.5 MG/ML, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, pH 6.00
|
Resolution 1.87 Å R-free 0.231 |
| 3CDO Bacteriophage T4 lysozyme mutant R96V in wildtype background at low temperature Deposited 2008-02-27 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
1–164（164 aa）
|
Mutation：R96V | HEZ HEXANE-1,6-DIOL × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 SO4 SULFATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；100 MM MES, 200 MM LITHIUM SULFATE, 35% MPD, 50 MM 1,6-HEXANEDIOL, 12.5 MG/ML, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, pH 6.00
|
Resolution 1.87 Å R-free 0.231 |
| 3CDQ Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme Deposited 2008-02-27 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R96S | CL CHLORIDE ION × 2 K POTASSIUM ION × 1 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；2 M NA/K PHOSPHATE PH 6.7 50 MM REDUCED BME 50 MM OXIDIZED BME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, pH 6.70
|
Resolution 1.68 Å R-free 0.196 |
| 3CDR R96Q Mutant of wildtype phage T4 lysozyme at 298 K Deposited 2008-02-27 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R96Q | CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；2 M NA/K PHOSPHATE PH 6.7, 550 MM NACL 50 MM REDUCED BME, 50 MM OXIDIZED BME , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, pH 6.70
|
Resolution 1.70 Å |
| 3CDT Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme Deposited 2008-02-27 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R96N | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；2 M NA/K PHOSPHATE PH 6.7, 550 MM NACL 50 MM REDUCED BME, 50 MM OXIDIZED BME , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, pH 6.70
|
Resolution 1.63 Å R-free 0.195 |
| 3CDV Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme Deposited 2008-02-27 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R96M | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.7；2 M NA/K PHOSPHATE PH 6.7, 550 MM NACL 50 MM REDUCED BME, 50 MM OXIDIZED BME , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, pH 6.70
|
Resolution 1.73 Å R-free 0.200 |
| 3D4S Cholesterol bound form of human beta2 adrenergic receptor. Deposited 2008-05-14 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：E122W, N187E, C1054T, C1097A | TIM (2S)-1-(tert-butylamino)-3-[(4-morpholin-4-yl-1,2,5-thiadiazol-3-yl)oxy]propan-2-ol × 1 CLR CHOLESTEROL × 2 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
MESOPHASE；pH 7；293 K；28% v/v PEG 400, 300mM K formate, 100mM Bis-tris propane pH 7.0, 2mM Timolol, MESOPHASE, temperature 293K
|
Resolution 2.80 Å R-free 0.273 |
| 3DKE Polar and non-polar cavities in phage T4 lysozyme Deposited 2008-06-24 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain X
1–164（164 aa）
|
Mutation：C54T, C97A, L99A, M102L Non-standard monomer：Yes (specific site not provided by mmCIF) | K POTASSIUM ION × 1 CL CHLORIDE ION × 2 AZI AZIDE ION × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 BME BETA-MERCAPTOETHANOL × 2 HED 2-HYDROXYETHYL DISULFIDE × 2 GOL GLYCEROL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；2.0-2.2 M NaH2PO4 and K2HPO4, pH 6.9, 5mM BME, 5mM oxidized BME, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.25 Å R-free 0.173 |
| 3DMV Free of ligand binding in the hydrophobic cavity of T4 lysozyme L99A mutant Deposited 2008-07-01 | Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L99A | PO4 PHOSPHATE ION × 1 CL CHLORIDE ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 3 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；2.0-2.2 M K/Na phosphate, pH 6.9, 5mM BME and 5mM oxidized BME. Complexes were made by soaking or gas-phase diffusion, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.65 Å R-free 0.210 |
| 3DMX Benzene binding in the hydrophobic cavity of T4 lysozyme L99A mutant Deposited 2008-07-01 | Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L99A | PO4 PHOSPHATE ION × 2 CL CHLORIDE ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 2 BNZ BENZENE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；2.0-2.2 M K/Na phosphate, pH 6.9, 5mM BME and 5mM oxidized BME. Complexes were prepared by soaking or vapor diffusion methods, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å R-free 0.208 |
| 3DMZ Hexafluorobenzene binding in the hydrophobic cavity of T4 lysozyme L99A mutant Deposited 2008-07-01 | Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L99A | PO4 PHOSPHATE ION × 2 CL CHLORIDE ION × 1 HFB hexafluorobenzene × 1 HED 2-HYDROXYETHYL DISULFIDE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6；277 K；2.0-2.2 M K/Na phosphate, pH 6.9, 5mM BME and 5mM oxidized BME. Complexes were prepared by soaking or vapor diffusion methods, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.00 Å R-free 0.214 |
| 3DN0 Pentafluorobenzene binding in the hydrophobic cavity of T4 lysozyme L99A mutant Deposited 2008-07-01 | Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L99A | PO4 PHOSPHATE ION × 2 CL CHLORIDE ION × 1 F5B 1,2,3,4,5-pentafluorobenzene × 1 HED 2-HYDROXYETHYL DISULFIDE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；2.0-2.2 M K/Na phosphate, pH 6.9, 5mM BME and 5mM oxidized BME
Complexes were prepared by soaking or vapor diffusion methods, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å R-free 0.222 |
| 3DN1 Chloropentafluorobenzene binding in the hydrophobic cavity of T4 lysozyme L99A mutant Deposited 2008-07-01 | Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L99A | PO4 PHOSPHATE ION × 2 CL CHLORIDE ION × 1 BCF 1-chloro-2,3,4,5,6-pentafluorobenzene × 1 HED 2-HYDROXYETHYL DISULFIDE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；2.0-2.2 M K/Na phosphate, pH 6.9, 5mM BME and 5mM oxidized BME. Complexes were prepared by soaking or vapor diffusion methods, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å R-free 0.220 |
| 3DN2 Bromopentafluorobenzene binding in the hydrophobic cavity of T4 lysozyme L99A mutant Deposited 2008-07-01 | Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L99A | PO4 PHOSPHATE ION × 2 BBF 1-bromo-2,3,4,5,6-pentafluorobenzene × 1 HED 2-HYDROXYETHYL DISULFIDE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；2.0-2.2 M K/Na phosphate, pH 6.9, 5mM BME and 5mM oxidized BME. Complexes were prepared by soaking or vapor diffusion methods, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å R-free 0.215 |
| 3DN3 Iodopentafluorobenzene binding in the hydrophobic cavity of T4 lysozyme L99A mutant Deposited 2008-07-01 | Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L99A | PO4 PHOSPHATE ION × 2 IBF 1,2,3,4,5-pentafluoro-6-iodobenzene × 1 HED 2-HYDROXYETHYL DISULFIDE × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；2.0-2.2 M K/Na phosphate, pH 6.9, 5mM BME and 5mM oxidized BME. Complexes were prepared by soaking or vapor diffusion methods, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å R-free 0.210 |
| 3DN4 Iodobenzene binding in the hydrophobic cavity of T4 lysozyme L99A mutant Deposited 2008-07-01 | Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L99A | PO4 PHOSPHATE ION × 2 PIH iodobenzene × 1 HED 2-HYDROXYETHYL DISULFIDE × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；2.0-2.2 M K/Na phosphate, pH 6.9, 5mM BME and 5mM oxidized BME. Complexes were prepared by soaking or vapor diffusion methods, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å R-free 0.223 |
| 3DN6 1,3,5-trifluoro-2,4,6-trichlorobenzene binding in the hydrophobic cavity of T4 lysozyme L99A mutant Deposited 2008-07-01 | Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L99A | PO4 PHOSPHATE ION × 2 F3B 1,3,5-trichloro-2,4,6-trifluorobenzene × 1 HED 2-HYDROXYETHYL DISULFIDE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；2.0-2.2 M K/Na phosphate, pH 6.9, 5mM BME and 5mM oxidized BME. Complexes were prepared by soaking or vapor diffusion methods, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.80 Å R-free 0.221 |
| 3DN8 Iodopentafluorobenzene binding in the hydrophobic cavity of T4 lysozyme L99A mutant (seleno version) Deposited 2008-07-01 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L99A, seleno version Non-standard monomer：Yes (specific site not provided by mmCIF) | PO4 PHOSPHATE ION × 1 CL CHLORIDE ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 3 BME BETA-MERCAPTOETHANOL × 1 IBF 1,2,3,4,5-pentafluoro-6-iodobenzene × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；2.0-2.2 M K/Na phosphate, pH 6.9, 5mM BME and 5mM oxidized BME. Complexes were prepared by soaking or vapor diffusion methods, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.70 Å R-free 0.223 |
| 3DNA Iodobenzene binding in the hydrophobic cavity of T4 lysozyme L99A mutant (seleno version) Deposited 2008-07-01 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L99A Non-standard monomer：Yes (specific site not provided by mmCIF) | PO4 PHOSPHATE ION × 1 CL CHLORIDE ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 3 BME BETA-MERCAPTOETHANOL × 1 PIH iodobenzene × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；2.0-2.2 M K/Na phosphate, pH 6.9, 5mM BME and 5mM oxidized BME. Complexes were prepared by soaking or vapor diffusion methods, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.70 Å R-free 0.217 |
| 3EML The 2.6 A Crystal Structure of a Human A2A Adenosine Receptor bound to ZM241385. Deposited 2008-09-24 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Not recorded | ZMA 4-{2-[(7-amino-2-furan-2-yl[1,2,4]triazolo[1,5-a][1,3,5]triazin-5-yl)amino]ethyl}phenol × 1 STE STEARIC ACID × 5 SO4 SULFATE ION × 7 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.5；293 K；PEG400 30%v/v, LiSO4 185mM, NaCitrate 100mM, pH 6.5, Lipidic mesophase, temperature 293K
|
Resolution 2.60 Å R-free 0.231 |
| 3F8V Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant Arg96-->His Deposited 2008-11-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R96H | HED 2-HYDROXYETHYL DISULFIDE × 1 PO4 PHOSPHATE ION × 1 CL CHLORIDE ION × 2 NA SODIUM ION × 1 K POTASSIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.3；277 K；2 M Na/K Phosphate, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.08 Å R-free 0.163 |
| 3F9L Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant Arg96-->His Deposited 2008-11-14 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：D72A | PO4 PHOSPHATE ION × 1 NA SODIUM ION × 1 CL CHLORIDE ION × 2 K POTASSIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；277 K；2M Na/K Phosphate, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.19 Å R-free 0.189 |
| 3FA0 Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant Arg96-->His Deposited 2008-11-14 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Not recorded | HED 2-HYDROXYETHYL DISULFIDE × 1 BME BETA-MERCAPTOETHANOL × 1 PO4 PHOSPHATE ION × 2 CL CHLORIDE ION × 2 K POTASSIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；277 K；2 M Na/K phosphate, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.09 Å R-free 0.188 |
| 3FAD Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant Arg96-->His Deposited 2008-11-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：D72A/R96H | PO4 PHOSPHATE ION × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；277 K；2 M Na/K Phospahte, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.20 Å R-free 0.174 |
| 3FAD Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant Arg96-->His Deposited 2008-11-17 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–164（164 aa）
|
Mutation：D72A/R96H | PO4 PHOSPHATE ION × 4 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；277 K；2 M Na/K Phospahte, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.20 Å R-free 0.174 |
| 3FI5 Crystal Structure of T4 Lysozyme Mutant R96W Deposited 2008-12-11 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R96W | CL CHLORIDE ION × 1 NA SODIUM ION × 1 IPA ISOPROPYL ALCOHOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.53 Å R-free 0.261 |
| 3FI5 Crystal Structure of T4 Lysozyme Mutant R96W Deposited 2008-12-11 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：R96W | CL CHLORIDE ION × 1 NA SODIUM ION × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.53 Å R-free 0.261 |
| 3FI5 Crystal Structure of T4 Lysozyme Mutant R96W Deposited 2008-12-11 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
1–164（164 aa）
|
Mutation：R96W | CL CHLORIDE ION × 1 NA SODIUM ION × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.53 Å R-free 0.261 |
| 3FI5 Crystal Structure of T4 Lysozyme Mutant R96W Deposited 2008-12-11 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
1–164（164 aa）
|
Mutation：R96W | CL CHLORIDE ION × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.53 Å R-free 0.261 |
| 3G3V Crystal structure of spin labeled T4 Lysozyme (V131R1) at 291 K Deposited 2009-02-02 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, V131C | MTN S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 AZI AZIDE ION × 1 CL CHLORIDE ION × 3 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；278 K；2.0M dibasic potassium phosphate and monobasic sodium phospahte, 0.25M sodium choloride, 0.04% sodium azide, 0.02M oxidized beta-mercaptoehtanol, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 278K
|
Resolution 2.10 Å R-free 0.199 |
| 3G3W Crystal structure of spin labeled T4 Lysozyme (T151R1) at 291 K Deposited 2009-02-02 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, T151C | MTN S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 CL CHLORIDE ION × 1 AZI AZIDE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；278 K；2.0M dibasic potassium phosphate and monobasic sodium phospahte, 0.25M sodium choloride, 0.04% sodium azide, 0.02M oxidized beta-mercaptoehtanol, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 278K
|
Resolution 2.30 Å R-free 0.216 |
| 3G3X Crystal structure of spin labeled T4 Lysozyme (T151R1) at 100 K Deposited 2009-02-02 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, T151R1 | MTN S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 AZI AZIDE ION × 2 CL CHLORIDE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；278 K；2.0M dibasic potassium phosphate and monobasic sodium phospahte, 0.25M sodium choloride, 0.04% sodium azide, 0.02M oxidized beta-mercaptoehtanol, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 278K
|
Resolution 1.80 Å R-free 0.224 |
| 3GUI T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--Apo structure Deposited 2009-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102E/E108V/S117V/T142C/N144D Non-standard monomer：Yes (specific site not provided by mmCIF) | BME BETA-MERCAPTOETHANOL × 1 CO3 CARBONATE ION × 1 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；30% PEG 8000, 0.20M ammonium sulfate, 0.10M Tris, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K
|
Resolution 1.45 Å R-free 0.206 |
| 3GUJ T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--Benzene binding Deposited 2009-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102E/E108V/S117V/T142C/N144D Non-standard monomer：Yes (specific site not provided by mmCIF) | BNZ BENZENE × 1 BME BETA-MERCAPTOETHANOL × 1 CO3 CARBONATE ION × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；30% PEG 8000, 0.2M ammounium sulfate, 0.1M Tris, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K
|
Resolution 1.60 Å R-free 0.239 |
| 3GUK T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--Toluene binding Deposited 2009-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102E/E108V/S117V/T142C/N144D Non-standard monomer：Yes (specific site not provided by mmCIF) | MBN TOLUENE × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；30% PEG 8000, 0.14M magnesium/calcium sulfate, 0.1M PIPES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K, VAPOR DIFFUSION, SITTING DROP
|
Resolution 1.85 Å R-free 0.273 |
| 3GUK T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--Toluene binding Deposited 2009-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102E/E108V/S117V/T142C/N144D Non-standard monomer：Yes (specific site not provided by mmCIF) | MBN TOLUENE × 1 CL CHLORIDE ION × 1 ACT ACETATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；30% PEG 8000, 0.14M magnesium/calcium sulfate, 0.1M PIPES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K, VAPOR DIFFUSION, SITTING DROP
|
Resolution 1.85 Å R-free 0.273 |
| 3GUL T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--ethylbenzene binding Deposited 2009-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102E/E108V/S117V/T142C/N144D Non-standard monomer：Yes (specific site not provided by mmCIF) | PYJ PHENYLETHANE × 1 ACT ACETATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；30% PEG 8000, 0.14M magnesium/calcium sulfate, 0.1M PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
|
Resolution 2.07 Å R-free 0.293 |
| 3GUL T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--ethylbenzene binding Deposited 2009-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102E/E108V/S117V/T142C/N144D Non-standard monomer：Yes (specific site not provided by mmCIF) | PYJ PHENYLETHANE × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；30% PEG 8000, 0.14M magnesium/calcium sulfate, 0.1M PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
|
Resolution 2.07 Å R-free 0.293 |
| 3GUM T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--p-xylene binding Deposited 2009-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102E/E108V/S117V/T142C/N144D Non-standard monomer：Yes (specific site not provided by mmCIF) | PXY PARA-XYLENE × 1 CL CHLORIDE ION × 1 ACT ACETATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；30% PEG 8000, 0.14M magnesium/calcium sulfate, 0.1M PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
|
Resolution 2.24 Å R-free 0.264 |
| 3GUM T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--p-xylene binding Deposited 2009-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102E/E108V/S117V/T142C/N144D Non-standard monomer：Yes (specific site not provided by mmCIF) | PXY PARA-XYLENE × 1 CL CHLORIDE ION × 2 ACT ACETATE ION × 1 CA CALCIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；30% PEG 8000, 0.14M magnesium/calcium sulfate, 0.1M PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
|
Resolution 2.24 Å R-free 0.264 |
| 3GUN T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--aniline binding Deposited 2009-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102E/E108V/S117V/T142C/N144D Non-standard monomer：Yes (specific site not provided by mmCIF) | ANL ANILINE × 2 CA CALCIUM ION × 1 CL CHLORIDE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；30% PEG 8000, 0.14M magnesium/calcium sulfate, 0.1M PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
|
Resolution 1.50 Å R-free 0.251 |
| 3GUN T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--aniline binding Deposited 2009-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102E/E108V/S117V/T142C/N144D Non-standard monomer：Yes (specific site not provided by mmCIF) | ANL ANILINE × 1 CL CHLORIDE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；30% PEG 8000, 0.14M magnesium/calcium sulfate, 0.1M PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
|
Resolution 1.50 Å R-free 0.251 |
| 3GUO T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--phenol binding Deposited 2009-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102E/E108V/S117V/T142C/N144D Non-standard monomer：Yes (specific site not provided by mmCIF) | IPH PHENOL × 1 CL CHLORIDE ION × 1 CA CALCIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；30% PEG 8000, 0.14M magnesium/calcium sulfate, 0.1M PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
|
Resolution 2.16 Å R-free 0.272 |
| 3GUO T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--phenol binding Deposited 2009-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102E/E108V/S117V/T142C/N144D Non-standard monomer：Yes (specific site not provided by mmCIF) | IPH PHENOL × 1 CL CHLORIDE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；30% PEG 8000, 0.14M magnesium/calcium sulfate, 0.1M PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
|
Resolution 2.16 Å R-free 0.272 |
| 3GUP T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--pyridine binding Deposited 2009-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102E/E108V/S117V/T142C/N144D Non-standard monomer：Yes (specific site not provided by mmCIF) | 0PY pyridine × 2 CO3 CARBONATE ION × 1 MG MAGNESIUM ION × 1 CL CHLORIDE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；30% PEG 8000, 0.14M magnesium/calcium sulfate, 0.1M PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
|
Resolution 1.50 Å R-free 0.253 |
| 3GUP T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--pyridine binding Deposited 2009-03-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102E/E108V/S117V/T142C/N144D Non-standard monomer：Yes (specific site not provided by mmCIF) | 0PY pyridine × 1 CO3 CARBONATE ION × 1 CL CHLORIDE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；30% PEG 8000, 0.14M magnesium/calcium sulfate, 0.1M PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
|
Resolution 1.50 Å R-free 0.253 |
| 3HH3 New azaborine compounds bind to the T4 lysozyme L99A cavity - 1,2-dihydro-1,2-azaborine Deposited 2009-05-14 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T,C97A,L99A | HED 2-HYDROXYETHYL DISULFIDE × 2 PO4 PHOSPHATE ION × 1 NA SODIUM ION × 1 B20 1,2-dihydro-1,2-azaborinine × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；2.0-2.2M K/Na phosphase, 50mM BME, 50mM HED (vapor-diffusion for complex preparation), pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.25 Å R-free 0.187 |
| 3HH4 New azaborine compounds bind to the T4 lysozyme L99A cavity - Benzene as control Deposited 2009-05-14 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T,C97A,L99A | HED 2-HYDROXYETHYL DISULFIDE × 2 PO4 PHOSPHATE ION × 1 BNZ BENZENE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；2.0-2.2M K/Na phosphase, 50mM BME, 50mM HED (vapor-diffusion for complex preparation), pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.25 Å R-free 0.192 |
| 3HH5 New azaborine compounds bind to the T4 lysozyme L99A cavity - 1-ethyl-2-hydro-1,2-azaborine Deposited 2009-05-14 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T/C97A/L99A | HED 2-HYDROXYETHYL DISULFIDE × 1 NA SODIUM ION × 1 PO4 PHOSPHATE ION × 1 B24 1-ethyl-1,2-dihydro-1,2-azaborinine × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；2.0-2.2M K/Na phosphase, 50mM BME, 50mM HED (vapor-diffusion for complex preparation), pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.25 Å R-free 0.182 |
| 3HH6 New azaborine compounds bind to the T4 lysozyme L99A cavity -ethylbenzene as control Deposited 2009-05-14 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T,C97A,L99A | HED 2-HYDROXYETHYL DISULFIDE × 2 PO4 PHOSPHATE ION × 1 PYJ PHENYLETHANE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277 K；2.0-2.2M K/Na phosphase, 50mM BME, 50mM HED (vapor-diffusion for complex preparation), pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.25 Å R-free 0.182 |
| 3HT6 2-methylphenol in complex with T4 lysozyme L99A/M102Q Deposited 2009-06-11 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：S38D,L99A, M102Q,N144D | PO4 PHOSPHATE ION × 2 JZ0 o-cresol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 6.5, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.59 Å R-free 0.220 |
| 3HT7 2-ethylphenol in complex with T4 lysozyme L99A/M102Q Deposited 2009-06-11 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：S38D,L99A,M102Q,N144D | PO4 PHOSPHATE ION × 2 JZ1 2-ethylphenol × 1 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 6.5, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.70 Å R-free 0.222 |
| 3HT8 5-chloro-2-methylphenol in complex with T4 lysozyme L99A/M102Q Deposited 2009-06-11 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：S38D,L99A,M102Q,N144D | PO4 PHOSPHATE ION × 2 JZ2 5-chloro-2-methylphenol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 6.5, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.60 Å R-free 0.214 |
| 3HT9 2-methoxyphenol in complex with T4 lysozyme L99A/M102Q Deposited 2009-06-11 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：S38D,L99A,M102Q,N144D | PO4 PHOSPHATE ION × 2 JZ3 Guaiacol × 1 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 6.5, vapor diffusion, hanging drop, temperature 277K
|
Resolution 2.02 Å R-free 0.219 |
| 3HTB 2-propylphenol in complex with T4 lysozyme L99A/M102Q Deposited 2009-06-11 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：S38D,L99A,M102Q,N144D | PO4 PHOSPHATE ION × 2 JZ4 2-propylphenol × 1 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 6.5, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.81 Å R-free 0.245 |
| 3HTD (Z)-Thiophene-2-carboxaldoxime in complex with T4 lysozyme L99A/M102Q Deposited 2009-06-11 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：S38D,L99A,M102Q,N144D | PO4 PHOSPHATE ION × 1 JZ5 (NZ)-N-(thiophen-2-ylmethylidene)hydroxylamine × 1 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 6.5, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.40 Å R-free 0.190 |
| 3HTF 4-chloro-1h-pyrazole in complex with T4 lysozyme L99A/M102Q Deposited 2009-06-11 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：S38D,L99A,M102Q,N144D | PO4 PHOSPHATE ION × 1 JZ6 4-chloro-1H-pyrazole × 2 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 6.5, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.85 Å R-free 0.208 |
| 3HTG 2-ethoxy-3,4-dihydro-2h-pyran in complex with T4 lysozyme L99A/M102Q Deposited 2009-06-11 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：S38D,L99A,M102Q,N144D | PO4 PHOSPHATE ION × 1 BME BETA-MERCAPTOETHANOL × 1 JZ7 (2S)-2-ethoxy-3,4-dihydro-2H-pyran × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 6.5, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.26 Å R-free 0.181 |
| 3HU8 2-ethoxyphenol in complex with T4 lysozyme L99A/M102Q Deposited 2009-06-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：S38D,L99A,M102Q,N144D | PO4 PHOSPHATE ION × 2 261 2-ethoxyphenol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 6.5, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.80 Å R-free 0.213 |
| 3HU9 Nitrosobenzene in complex with T4 lysozyme L99A/M102Q Deposited 2009-06-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：S38D,L99A,M102Q,N144D | PO4 PHOSPHATE ION × 1 NBE NITROSOBENZENE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 6.5, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.46 Å R-free 0.202 |
| 3HUA 4,5,6,7-tetrahydroindole in complex with T4 lysozyme L99A/M102Q Deposited 2009-06-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：S44D,L99A,M102Q,N144D | JZ9 4,5,6,7-tetrahydro-1H-indole × 1 BME BETA-MERCAPTOETHANOL × 2 PO4 PHOSPHATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 6.5, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.40 Å R-free 0.192 |
| 3HUK Benzylacetate in complex with T4 lysozyme L99A/M102Q Deposited 2009-06-14 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：S38D,L99A,M102Q,N144D | PO4 PHOSPHATE ION × 1 J0Z benzyl acetate × 1 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 6.5, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.29 Å R-free 0.185 |
| 3HUQ Thieno[3,2-b]thiophene in complex with T4 lysozyme L99A/M102Q Deposited 2009-06-15 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：S38D,L99A,M102Q,N144D | PO4 PHOSPHATE ION × 1 J1Z thieno[3,2-b]thiophene × 1 BME BETA-MERCAPTOETHANOL × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2M sodium-potassium phosphate, 0.05M beta-mercaptoethanol, 0.05M 2-hydroxyethyldisulfide, pH 6.5, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.45 Å R-free 0.189 |
| 3HWL Crystal Structure of T4 lysozyme with the unnatural amino acid p-Acetyl-L-Phenylalanine incorporated at position 131 Deposited 2009-06-17 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–164（164 aa）
|
Mutation：C54T,C97A,N68C,A93C,V131(4AF) Non-standard monomer：Yes (specific site not provided by mmCIF) | AZI AZIDE ION × 4 CL CHLORIDE ION × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；293 K；2.0M sodium/potassium phosphate, 0.2M sodium chloride, 0.04% sodium azide, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 1.80 Å R-free 0.227 |
| 3JR6 Sequential reorganization of beta-sheet topology by insertion of a single strand Deposited 2009-09-08 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, insertion of seuqence (gighll) after residue L33 | SO4 SULFATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；20% PEG 3400, 50 mM ammonium sulfate, Tris, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 3.00 Å R-free 0.320 |
| 3JR6 Sequential reorganization of beta-sheet topology by insertion of a single strand Deposited 2009-09-08 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：C54T, C97A, insertion of seuqence (gighll) after residue L33 | SO4 SULFATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；20% PEG 3400, 50 mM ammonium sulfate, Tris, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 3.00 Å R-free 0.320 |
| 3JR6 Sequential reorganization of beta-sheet topology by insertion of a single strand Deposited 2009-09-08 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
1–164（164 aa）
|
Mutation：C54T, C97A, insertion of seuqence (gighll) after residue L33 | SO4 SULFATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；20% PEG 3400, 50 mM ammonium sulfate, Tris, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 3.00 Å R-free 0.320 |
| 3JR6 Sequential reorganization of beta-sheet topology by insertion of a single strand Deposited 2009-09-08 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
1–164（164 aa）
|
Mutation：C54T, C97A, insertion of seuqence (gighll) after residue L33 | SO4 SULFATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；20% PEG 3400, 50 mM ammonium sulfate, Tris, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 3.00 Å R-free 0.320 |
| 3K2R Crystal Structure of Spin Labeled T4 Lysozyme Mutant K65V1/R76V1 Deposited 2009-09-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T,K65C,R76C,C97A | V1A S-(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-imidazol-4-yl) methanesulfonothioate × 2 HEZ HEXANE-1,6-DIOL × 2 CL CHLORIDE ION × 2 K POTASSIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；2.2M dibasic potassium phosphate and monobasic sodium phosphate, 0.15M sodium chloride, 100mM 1,6 hexanediol, pH 7.0, vapor diffusion, hanging drop, temperature 293K
|
Resolution 1.50 Å R-free 0.212 |
| 3L2X Crystal Structure of Spin Labeled T4 Lysozyme Mutant 115-119RX Deposited 2009-12-15 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, T115C, R119C | RXR [2,2,5,5-tetramethyl-3,4-bis(sulfanylmethyl)-2,5-dihydro-1H-pyrrol-1-yl]oxidanyl radical × 1 AZI AZIDE ION × 1 CL CHLORIDE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.4；277 K；2.0M dibasic potassium phosphate and monobasic sodium phosphate, 0.25M sodium chloride,
0.04% sodium azide, saturated with bis(2-hydroxyethyl) disulfide, pH 6.4, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.80 Å R-free 0.232 |
| 3L64 T4 Lysozyme S44E/WT* Deposited 2009-12-23 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：S44E, C54T, C97A | BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；10 Ul of protein solution (20 mg/ml) mixed with 10 Ul of well solution, typically 2.0 M-phosphate (pH 6.3 to 7.1), 0.25 M-NaCl and 6 Ul of 2-hydroxyethyl disulfide/ml (i.e. oxidized beta-mercaptoethanol). The drop was then equilibrated over 1 ml of well solution using a Limbro plate, VAPOR DIFFUSION, HANGING DROP
|
Resolution 1.90 Å |
| 3LZM STRUCTURAL STUDIES OF MUTANTS OF T4 LYSOZYME THAT ALTER HYDROPHOBIC STABILIZATION Deposited 1989-05-01 | Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 3NY8 Crystal structure of the human beta2 adrenergic receptor in complex with the inverse agonist ICI 118,551 Deposited 2010-07-14 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
Fragment：Chimeric protein of Beta-2 Adrenoreceptor 1-230, Lysozyme 2-161, Beta-2 adrenergic receptor 263-348
|
Mutation：E122W, N187E, C1054T, C1097A | CLR CHOLESTEROL × 2 JRZ (2S,3S)-1-[(7-methyl-2,3-dihydro-1H-inden-4-yl)oxy]-3-[(1-methylethyl)amino]butan-2-ol × 1 OLA OLEIC ACID × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2 PGE TRIETHYLENE GLYCOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
293 K；100 mM Tris/HCl pH 7.5-8.0, 200-500 mM Na-formate, 5% 1,4 butanediol, 27-32% PEG 400, Lipidic Cubic Phase (LCP) Crystallization, temperature 293-295K
|
Resolution 2.84 Å R-free 0.291 |
| 3NY9 Crystal structure of the human beta2 adrenergic receptor in complex with a novel inverse agonist Deposited 2010-07-14 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
Fragment：Chimeric protein of Beta-2 Adrenoreceptor 1-230, Lysozyme 2-161, Beta-2 adrenergic receptor 263-348
|
Mutation：E122W, N187E, C1054T, C1097A | CLR CHOLESTEROL × 2 JSZ ethyl 4-({(2S)-2-hydroxy-3-[(1-methylethyl)amino]propyl}oxy)-3-methyl-1-benzofuran-2-carboxylate × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
293 K；100 mM Tris/HCl pH 7.5-8, 5% 1,4 butanediol, 220 mM Na-formate, 27% PEG 400, Lipidic Cubic Phase (LCP) Crystallization, temperature 293-295K
|
Resolution 2.84 Å R-free 0.278 |
| 3NYA Crystal structure of the human beta2 adrenergic receptor in complex with the neutral antagonist alprenolol Deposited 2010-07-14 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
Fragment：Chimeric protein of Beta-2 Adrenoreceptor 1-230, Lysozyme 2-161, Beta-2 adrenergic receptor 263-348
|
Mutation：E122W, N187E, C1054T, C1097A | CLR CHOLESTEROL × 2 JTZ (2S)-1-[(1-methylethyl)amino]-3-(2-prop-2-en-1-ylphenoxy)propan-2-ol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
293 K；100 mM Bis-Tris Propane pH 6.6-6.8, 120 mM Na-tartrate, 3% 1,3 butanediol, 25-30% PEG 400, Lipidic Cubic Phase (LCP) Crystallization, temperature 293-295K
|
Resolution 3.16 Å R-free 0.290 |
| 3ODU The 2.5 A structure of the CXCR4 chemokine receptor in complex with small molecule antagonist IT1t Deposited 2010-08-11 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1002–1161（160 aa）
Fragment：CXCR4 residues 2-229, LYSOZYME residues 1002-1161, CXCR4 residues 230-319
Chain B
1002–1161（160 aa）
Fragment：CXCR4 residues 2-229, LYSOZYME residues 1002-1161, CXCR4 residues 230-319
|
Mutation：L125W, C1054T, C1097T Mutation：L125W, C1054T, C1097T | ITD (6,6-dimethyl-5,6-dihydroimidazo[2,1-b][1,3]thiazol-3-yl)methyl N,N'-dicyclohexylimidothiocarbamate × 2 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 5 OLA OLEIC ACID × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 5.5；293 K；Lipidic cubic phase made of monoolein and cholesterol, 20% PEG400, 0.3M Sodium malonate, 5mM Taurine, 0.1M Sodium citrate, pH 5.5, LIPIDIC CUBIC PHASE, temperature 293K
|
Resolution 2.50 Å R-free 0.282 |
| 3OE0 Crystal structure of the CXCR4 chemokine receptor in complex with a cyclic peptide antagonist CVX15 Deposited 2010-08-12 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain A
1002–1161（160 aa）
Fragment：CXCR4 residues 2-228, LYSOZYME residues 1002-1161, CXCR4 residues 231-319
|
Mutation：L125W, T240P, C1054T, C1097T | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 7；293 K；Lipidic cubic phase made of monoolein and cholesterol, 25% PEG400, 0.3M Potassium sodium tartrate, 0.1 M Tris pH 7.0, LIPIDIC CUBIC PHASE, temperature 293K
|
Resolution 2.90 Å R-free 0.267 |
| 3OE6 Crystal structure of the CXCR4 chemokine receptor in complex with a small molecule antagonist IT1t in I222 spacegroup Deposited 2010-08-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1002–1161（160 aa）
Fragment：CXCR4 residues 2-228, LYSOZYME residues 1002-1161, CXCR4 residues 231-325
|
Mutation：L125W, C1054T, C1097T | ITD (6,6-dimethyl-5,6-dihydroimidazo[2,1-b][1,3]thiazol-3-yl)methyl N,N'-dicyclohexylimidothiocarbamate × 2 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 6 GOL GLYCEROL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 5.5；293 K；Lipidic cubic phase made of monoolein and cholesterol, 20-26% PEG400, 0.3M Sodium malonate, 5mM Nickel chloride, 0.1M Sodium citrate pH 5.0-5.5, LIPIDIC CUBIC PHASE, temperature 293K
|
Resolution 3.20 Å R-free 0.306 |
| 3OE8 Crystal structure of the CXCR4 chemokine receptor in complex with a small molecule antagonist IT1t in P1 spacegroup Deposited 2010-08-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain B
1002–1161（160 aa）
Fragment：CXCR4 residues 2-229, LYSOZYME residues 1002-1161, CXCR4 residues 230-319
Chain C
1002–1161（160 aa）
Fragment：CXCR4 residues 2-229, LYSOZYME residues 1002-1161, CXCR4 residues 230-319
|
Mutation：L125W, C1054T, C1097T Mutation：L125W, C1054T, C1097T | ITD (6,6-dimethyl-5,6-dihydroimidazo[2,1-b][1,3]thiazol-3-yl)methyl N,N'-dicyclohexylimidothiocarbamate × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6；293 K；Lipidic cubic phase made of monoolein and cholesterol, 26% PEG400, 0.3M Sodium malonate, 5mM Strontium chloride, 0.1M MES pH 6.0, LIPIDIC CUBIC PHASE, temperature 293K
|
Resolution 3.10 Å R-free 0.295 |
| 3OE8 Crystal structure of the CXCR4 chemokine receptor in complex with a small molecule antagonist IT1t in P1 spacegroup Deposited 2010-08-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
1002–1161（160 aa）
Fragment：CXCR4 residues 2-229, LYSOZYME residues 1002-1161, CXCR4 residues 230-319
Chain B
1002–1161（160 aa）
Fragment：CXCR4 residues 2-229, LYSOZYME residues 1002-1161, CXCR4 residues 230-319
Chain C
1002–1161（160 aa）
Fragment：CXCR4 residues 2-229, LYSOZYME residues 1002-1161, CXCR4 residues 230-319
|
Mutation：L125W, C1054T, C1097T Mutation：L125W, C1054T, C1097T Mutation：L125W, C1054T, C1097T | ITD (6,6-dimethyl-5,6-dihydroimidazo[2,1-b][1,3]thiazol-3-yl)methyl N,N'-dicyclohexylimidothiocarbamate × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6；293 K；Lipidic cubic phase made of monoolein and cholesterol, 26% PEG400, 0.3M Sodium malonate, 5mM Strontium chloride, 0.1M MES pH 6.0, LIPIDIC CUBIC PHASE, temperature 293K
|
Resolution 3.10 Å R-free 0.295 |
| 3OE8 Crystal structure of the CXCR4 chemokine receptor in complex with a small molecule antagonist IT1t in P1 spacegroup Deposited 2010-08-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1002–1161（160 aa）
Fragment：CXCR4 residues 2-229, LYSOZYME residues 1002-1161, CXCR4 residues 230-319
|
Mutation：L125W, C1054T, C1097T | ITD (6,6-dimethyl-5,6-dihydroimidazo[2,1-b][1,3]thiazol-3-yl)methyl N,N'-dicyclohexylimidothiocarbamate × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6；293 K；Lipidic cubic phase made of monoolein and cholesterol, 26% PEG400, 0.3M Sodium malonate, 5mM Strontium chloride, 0.1M MES pH 6.0, LIPIDIC CUBIC PHASE, temperature 293K
|
Resolution 3.10 Å R-free 0.295 |
| 3OE9 Crystal structure of the chemokine CXCR4 receptor in complex with a small molecule antagonist IT1t in P1 spacegroup Deposited 2010-08-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1002–1161（160 aa）
Fragment：CXCR4 residues 2-228, LYSOZYME residues 1002-1161, CXCR4 residues 231-319
Chain B
1002–1161（160 aa）
Fragment：CXCR4 residues 2-228, LYSOZYME residues 1002-1161, CXCR4 residues 231-319
|
Mutation：L125W, T240P, C1054T, C1097T Mutation：L125W, T240P, C1054T, C1097T | ITD (6,6-dimethyl-5,6-dihydroimidazo[2,1-b][1,3]thiazol-3-yl)methyl N,N'-dicyclohexylimidothiocarbamate × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6；293 K；Lipidic cubic phase made of monoolein and cholesterol, 27-35% PEG400, 0.27-0.33M Sodium malonate, 5mM Hexamine cobalt chloride, 0.1M MES pH 6.0, LIPIDIC CUBIC PHASE, temperature 293K
|
Resolution 3.10 Å R-free 0.284 |
| 3P0G Structure of a nanobody-stabilized active state of the beta2 adrenoceptor Deposited 2010-09-28 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
Fragment：UNP P07550 residues 1-230, 263-365, UNP P00720 residues 2-161
|
Mutation：N187E | P0G 8-[(1R)-2-{[1,1-dimethyl-2-(2-methylphenyl)ethyl]amino}-1-hydroxyethyl]-5-hydroxy-2H-1,4-benzoxazin-3(4H)-one × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 8；293 K；36-44% PEG 400, 100 mM Tris pH 8.0, 4% DMSO, 1% 1,2,3-heptanetriol, twin-syringe mixing method, temperature 293K
|
Resolution 3.50 Å R-free 0.308 |
| 3PBL Structure of the human dopamine D3 receptor in complex with eticlopride Deposited 2010-10-20 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：L119W, C1054T, C1097A | ETQ 3-chloro-5-ethyl-N-{[(2S)-1-ethylpyrrolidin-2-yl]methyl}-6-hydroxy-2-methoxybenzamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 7.5；293 K；Lipidic cubic phase made of monoolein and 10% cholesterol, 30% PEG400, 300mM Ammonium acetate, 2% glucose, 100mM bis tris propane pH 7.5, 1mM eticlopride, LIPIDIC CUBIC PHASE, temperature 293K
|
Resolution 2.89 Å R-free 0.272 |
| 3PBL Structure of the human dopamine D3 receptor in complex with eticlopride Deposited 2010-10-20 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–161（160 aa）
|
Mutation：L119W, C1054T, C1097A | ETQ 3-chloro-5-ethyl-N-{[(2S)-1-ethylpyrrolidin-2-yl]methyl}-6-hydroxy-2-methoxybenzamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 7.5；293 K；Lipidic cubic phase made of monoolein and 10% cholesterol, 30% PEG400, 300mM Ammonium acetate, 2% glucose, 100mM bis tris propane pH 7.5, 1mM eticlopride, LIPIDIC CUBIC PHASE, temperature 293K
|
Resolution 2.89 Å R-free 0.272 |
| 3PDS Irreversible Agonist-Beta2 Adrenoceptor Complex Deposited 2010-10-24 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–162（161 aa）
|
Mutation：H93C,N187E,C265A | ERC 8-hydroxy-5-[(1R)-1-hydroxy-2-({2-[3-methoxy-4-(3-sulfanylpropoxy)phenyl]ethyl}amino)ethyl]quinolin-2(1H)-one × 1 CLR CHOLESTEROL × 1 SO4 SULFATE ION × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6.7；293 K；26 %(v/v) PEG 400, 200 mM Li2SO4, 4 %(v/v) DMSO, 3.5 %(v/v) 1,4-butandediol, 100 mM MES pH 6.7, Lipidic Cubic Phase, temperature 293K
|
Resolution 3.50 Å R-free 0.283 |
| 3QAK Agonist bound structure of the human adenosine A2a receptor Deposited 2011-01-11 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Not recorded | UKA 6-(2,2-diphenylethylamino)-9-[(2R,3R,4S,5S)-5-(ethylcarbamoyl)-3,4-dihydroxy-oxolan-2-yl]-N-[2-[(1-pyridin-2-ylpiperidin-4-yl)carbamoylamino]ethyl]purine-2-carboxamide × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 5；293 K；PEG400 30%v/v, MgCl2 200mM, pH 5.0, Lipidic cubic phase, temperature 293K
|
Resolution 2.71 Å R-free 0.273 |
| 3RUN New strategy to analyze structures of glycopeptide antibiotic-target complexes Deposited 2011-05-05 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, L164A Non-standard monomer：Yes (specific site not provided by mmCIF) | MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 2 PO4 PHOSPHATE ION × 1 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 CL CHLORIDE ION × 1 IPA ISOPROPYL ALCOHOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；291 K；0.2M ammonium phosphate, 0.1M Tris 8.5, 35% MPD, vapor diffusion, hanging drop, temperature 291K
|
Resolution 1.40 Å R-free 0.180 |
| 3RZE Structure of the human histamine H1 receptor in complex with doxepin Deposited 2011-05-11 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Not recorded | 5EH (3E)-3-(dibenzo[b,e]oxepin-11(6H)-ylidene)-N,N-dimethylpropan-1-amine × 1 D7V (3Z)-3-(dibenzo[b,e]oxepin-11(6H)-ylidene)-N,N-dimethylpropan-1-amine × 1 PO4 PHOSPHATE ION × 3 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 4.5；293 K；26-30% PEG400, 300mM ammonium phosphate, 10mM MgCl2, 100mM Na-citrate pH 4.5, 1mM doxepin, Lipidic cubic phase, 293K
|
Resolution 3.10 Å R-free 0.249 |
| 3SB5 Zn-mediated Trimer of T4 Lysozyme R125C/E128C by Synthetic Symmetrization Deposited 2011-06-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain B
1–162（162 aa）
|
Mutation：C54T, C97A, R125C, E128C | ZN ZINC ION × 6 CL CHLORIDE ION × 6 MG MAGNESIUM ION × 6 GOL GLYCEROL × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；290 K；0.2M Magnesium Chloride, 20% PEG 8000, 0.1M TRIS, pH 8.5, vapor diffusion, hanging drop, temperature 290K
|
Resolution 2.46 Å R-free 0.230 |
| 3SB5 Zn-mediated Trimer of T4 Lysozyme R125C/E128C by Synthetic Symmetrization Deposited 2011-06-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
1–162（162 aa）
|
Mutation：C54T, C97A, R125C, E128C | ZN ZINC ION × 6 CL CHLORIDE ION × 6 MG MAGNESIUM ION × 6 GOL GLYCEROL × 9 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；290 K；0.2M Magnesium Chloride, 20% PEG 8000, 0.1M TRIS, pH 8.5, vapor diffusion, hanging drop, temperature 290K
|
Resolution 2.46 Å R-free 0.230 |
| 3SB5 Zn-mediated Trimer of T4 Lysozyme R125C/E128C by Synthetic Symmetrization Deposited 2011-06-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain C
1–162（162 aa）
|
Mutation：C54T, C97A, R125C, E128C | ZN ZINC ION × 6 CL CHLORIDE ION × 6 GOL GLYCEROL × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；290 K；0.2M Magnesium Chloride, 20% PEG 8000, 0.1M TRIS, pH 8.5, vapor diffusion, hanging drop, temperature 290K
|
Resolution 2.46 Å R-free 0.230 |
| 3SB5 Zn-mediated Trimer of T4 Lysozyme R125C/E128C by Synthetic Symmetrization Deposited 2011-06-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain D
1–162（162 aa）
|
Mutation：C54T, C97A, R125C, E128C | ZN ZINC ION × 6 CL CHLORIDE ION × 6 MG MAGNESIUM ION × 6 GOL GLYCEROL × 9 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；290 K；0.2M Magnesium Chloride, 20% PEG 8000, 0.1M TRIS, pH 8.5, vapor diffusion, hanging drop, temperature 290K
|
Resolution 2.46 Å R-free 0.230 |
| 3SB6 Cu-mediated Dimer of T4 Lysozyme D61H/K65H/R76H/R80H by Synthetic Symmetrization Deposited 2011-06-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–162（162 aa）
Chain B
1–162（162 aa）
|
Mutation：C54T, D61H, K65H, R76H, R80H, C97A Mutation：C54T, D61H, K65H, R76H, R80H, C97A | CU COPPER (II) ION × 2 CL CHLORIDE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；290 K；0.2M Ammonium Nitrate, 20% PEG 3350, vapor diffusion, hanging drop, temperature 290K
|
Resolution 2.70 Å R-free 0.272 |
| 3SB7 Cu-mediated Trimer of T4 Lysozyme D61H/K65H/R76H/R80H by Synthetic Symmetrization Deposited 2011-06-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain B
1–162（162 aa）
|
Mutation：C54T, D61H, K65H, R76H, R80H, C97A | CU COPPER (II) ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；290 K；0.2M Potassium Thiocyanate, 25% PEG 3350, vapor diffusion, hanging drop, temperature 290K
|
Resolution 2.70 Å R-free 0.226 |
| 3SB7 Cu-mediated Trimer of T4 Lysozyme D61H/K65H/R76H/R80H by Synthetic Symmetrization Deposited 2011-06-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–162（162 aa）
Chain B
1–162（162 aa）
|
Mutation：C54T, D61H, K65H, R76H, R80H, C97A Mutation：C54T, D61H, K65H, R76H, R80H, C97A | GOL GLYCEROL × 1 CU COPPER (II) ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；290 K；0.2M Potassium Thiocyanate, 25% PEG 3350, vapor diffusion, hanging drop, temperature 290K
|
Resolution 2.70 Å R-free 0.226 |
| 3SB8 Cu-mediated Dimer of T4 Lysozyme D61H/K65H by Synthetic Symmetrization Deposited 2011-06-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–162（162 aa）
Chain B
1–162（162 aa）
|
Mutation：C54T, D61H, K65H, C97A Mutation：C54T, D61H, K65H, C97A | CU COPPER (II) ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；290 K；3.5M Sodium Formate, pH 7.0, vapor diffusion, hanging drop, temperature 290K
|
Resolution 2.65 Å R-free 0.273 |
| 3SB8 Cu-mediated Dimer of T4 Lysozyme D61H/K65H by Synthetic Symmetrization Deposited 2011-06-03 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
1–162（162 aa）
|
Mutation：C54T, D61H, K65H, C97A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；290 K；3.5M Sodium Formate, pH 7.0, vapor diffusion, hanging drop, temperature 290K
|
Resolution 2.65 Å R-free 0.273 |
| 3SB9 Cu-mediated Dimer of T4 Lysozyme R76H/R80H by Synthetic Symmetrization Deposited 2011-06-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–162（162 aa）
Chain B
1–162（162 aa）
|
Mutation：C54T, R76H, R80H, C97A Mutation：C54T, R76H, R80H, C97A | FMT FORMIC ACID × 2 CU COPPER (II) ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；290 K；3.5M Sodium Formate, pH 7.0, vapor diffusion, hanging drop, temperature 290K
|
Resolution 2.45 Å R-free 0.239 |
| 3SBA Zn-mediated Hexamer of T4 Lysozyme R76H/R80H by Synthetic Symmetrization Deposited 2011-06-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric |
Chain A
1–162（162 aa）
Chain B
1–162（162 aa）
Chain C
1–162（162 aa）
Chain D
1–162（162 aa）
Chain E
1–162（162 aa）
Chain F
1–162（162 aa）
|
Mutation：C54T, R76H, R80H, C97A Mutation：C54T, R76H, R80H, C97A Mutation：C54T, R76H, R80H, C97A Mutation：C54T, R76H, R80H, C97A Mutation：C54T, R76H, R80H, C97A Mutation：C54T, R76H, R80H, C97A | ZN ZINC ION × 3 CL CHLORIDE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；290 K；0.17M Ammonium Acetate, 0.085 Sodium Acetate Trihydrate, 25.5% PEG 4000, 15% Glycerol, pH 4.6, vapor diffusion, hanging drop, temperature 290K
|
Resolution 2.75 Å R-free 0.278 |
| 3SBB Disulphide-mediated Tetramer of T4 Lysozyme R76C/R80C by Synthetic Symmetrization Deposited 2011-06-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric |
Chain C
1–162（162 aa）
|
Mutation：C54T, R76C, R80C, C97A | CL CHLORIDE ION × 12 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；290 K；4.3M Sodium Chloride, 0.1M HEPES, pH 7.5, vapor diffusion, hanging drop, temperature 290K
|
Resolution 1.43 Å R-free 0.177 |
| 3SN6 Crystal structure of the beta2 adrenergic receptor-Gs protein complex Deposited 2011-06-28 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric |
Chain R
2–161（160 aa）
|
Mutation：C54T,C97A,M96T,M98T,N187E | P0G 8-[(1R)-2-{[1,1-dimethyl-2-(2-methylphenyl)ethyl]amino}-1-hydroxyethyl]-5-hydroxy-2H-1,4-benzoxazin-3(4H)-one × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6.5；293 K；350-450 mM potassium nitrate, 100 mM MES, 1 mM TCEP, 10 mM phosphonoformate, 0.01 mM BI167107, 18-22% PEG400. Crystals were grown in a 10:1 (w:w) MAG 7.7:cholesterol lipid mix. , pH 6.5, Lipidic cubic phase, temperature 293K
|
Resolution 3.20 Å R-free 0.277 |
| 3UON Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist Deposited 2011-11-16 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
Fragment：UNP RESIDUES 1-217, UNP RESIDUES 2-161, UNP RESIDUES 377-466
|
Mutation：N2D, N3D, N6D, N9D, C54T, C97A | QNB (3R)-1-azabicyclo[2.2.2]oct-3-yl hydroxy(diphenyl)acetate × 1 BGC beta-D-glucopyranose × 1 CL CHLORIDE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；293 K；25 to 35% PEG 300, 100 mM ammonium phosphate, 2% 2-Methyl-2,4-pentanediol, 100 mM HEPES, 10:1 monoolein:cholesterol lipid mix diluted 1.5:1 with protein in detergent buffer, Lipidic cubic phase, temperature 293K, pH 7.5
|
Resolution 3.00 Å R-free 0.276 |
| 3V2W Crystal Structure of a Lipid G protein-Coupled Receptor at 3.35A Deposited 2011-12-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：C1054T, C1097A | ML5 {(3R)-3-amino-4-[(3-hexylphenyl)amino]-4-oxobutyl}phosphonic acid × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
Lupuc cubic phase；287 K；0.1M Tricine, 34-36% PEG400, 80mM sodium citrate and 4% glycerol, Lupuc cubic phase, temperature 287K
|
Resolution 3.35 Å R-free 0.281 |
| 3V2Y Crystal Structure of a Lipid G protein-Coupled Receptor at 2.80A Deposited 2011-12-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：C1054T, C1097A | ML5 {(3R)-3-amino-4-[(3-hexylphenyl)amino]-4-oxobutyl}phosphonic acid × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
Lipid cubic phase；287 K；0.1M Tricine, 34-36% PEG400, 80mM sodium citrate and 4% glycerol, Lipid cubic phase, temperature 287K
|
Resolution 2.80 Å R-free 0.272 |
| 3VW7 Crystal structure of human protease-activated receptor 1 (PAR1) bound with antagonist vorapaxar at 2.2 angstrom Deposited 2012-08-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：N250G, N259S, D1020N, C1054T, C1097A | VPX ethyl [(1R,3aR,4aR,6R,8aR,9S,9aS)-9-{(E)-2-[5-(3-fluorophenyl)pyridin-2-yl]ethenyl}-1-methyl-3-oxododecahydronaphtho[2,3-c]fur an-6-yl]carbamate × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 9 CL CHLORIDE ION × 1 NA SODIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
293 K；0.1-0.2M sodium chloride, 100mM sodium phosphate pH 6.0-6.5, 25%-35% PEG 300, Lipidic cubic phase (in meso phase), temperature 293K
|
Resolution 2.20 Å R-free 0.235 |
| 4ARJ Crystal structure of a pesticin (translocation and receptor binding domain) from Y. pestis and T4-lysozyme chimera Deposited 2012-04-24 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–164（163 aa）
Fragment：N-TERMINAL DOMAIN OF PESTICIN, RESIDUES 1-167
|
Mutation：YES | SO4 SULFATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；20% PEG 3350 0.15 M K2(SO4), pH 7
|
Resolution 2.59 Å R-free 0.237 |
| 4ARJ Crystal structure of a pesticin (translocation and receptor binding domain) from Y. pestis and T4-lysozyme chimera Deposited 2012-04-24 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–164（163 aa）
Fragment：N-TERMINAL DOMAIN OF PESTICIN, RESIDUES 1-167
|
Mutation：YES | SO4 SULFATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；20% PEG 3350 0.15 M K2(SO4), pH 7
|
Resolution 2.59 Å R-free 0.237 |
| 4DAJ Structure of the M3 Muscarinic Acetylcholine Receptor Deposited 2012-01-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–161（161 aa）
Fragment：P08483 residues 57-259, 482-589, P00720 residues 1-161
|
Mutation：C1054T, C1097A | 0HK (1R,2R,4S,5S,7S)-7-{[hydroxy(dithiophen-2-yl)acetyl]oxy}-9,9-dimethyl-3-oxa-9-azoniatricyclo[3.3.1.0~2,4~]nonane × 1 PO4 PHOSPHATE ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；293 K；27-38% PEG 300, 100 mM HEPES pH 7.5, 1% (w/w) 1,2,3-heptanetriol, and 100 mM ammonium phosphate. Protein was reconstituted in cubic phase using a 10:1 monolein:cholesterol mix by weight, Lipidic cubic phase, temperature 293K
|
Resolution 3.40 Å R-free 0.303 |
| 4DAJ Structure of the M3 Muscarinic Acetylcholine Receptor Deposited 2012-01-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–161（161 aa）
Fragment：P08483 residues 57-259, 482-589, P00720 residues 1-161
|
Mutation：C1054T, C1097A | 0HK (1R,2R,4S,5S,7S)-7-{[hydroxy(dithiophen-2-yl)acetyl]oxy}-9,9-dimethyl-3-oxa-9-azoniatricyclo[3.3.1.0~2,4~]nonane × 1 PO4 PHOSPHATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；293 K；27-38% PEG 300, 100 mM HEPES pH 7.5, 1% (w/w) 1,2,3-heptanetriol, and 100 mM ammonium phosphate. Protein was reconstituted in cubic phase using a 10:1 monolein:cholesterol mix by weight, Lipidic cubic phase, temperature 293K
|
Resolution 3.40 Å R-free 0.303 |
| 4DAJ Structure of the M3 Muscarinic Acetylcholine Receptor Deposited 2012-01-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
1–161（161 aa）
Fragment：P08483 residues 57-259, 482-589, P00720 residues 1-161
|
Mutation：C1054T, C1097A | 0HK (1R,2R,4S,5S,7S)-7-{[hydroxy(dithiophen-2-yl)acetyl]oxy}-9,9-dimethyl-3-oxa-9-azoniatricyclo[3.3.1.0~2,4~]nonane × 1 PO4 PHOSPHATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；293 K；27-38% PEG 300, 100 mM HEPES pH 7.5, 1% (w/w) 1,2,3-heptanetriol, and 100 mM ammonium phosphate. Protein was reconstituted in cubic phase using a 10:1 monolein:cholesterol mix by weight, Lipidic cubic phase, temperature 293K
|
Resolution 3.40 Å R-free 0.303 |
| 4DAJ Structure of the M3 Muscarinic Acetylcholine Receptor Deposited 2012-01-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
1–161（161 aa）
Fragment：P08483 residues 57-259, 482-589, P00720 residues 1-161
|
Mutation：C1054T, C1097A | 0HK (1R,2R,4S,5S,7S)-7-{[hydroxy(dithiophen-2-yl)acetyl]oxy}-9,9-dimethyl-3-oxa-9-azoniatricyclo[3.3.1.0~2,4~]nonane × 1 PO4 PHOSPHATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；293 K；27-38% PEG 300, 100 mM HEPES pH 7.5, 1% (w/w) 1,2,3-heptanetriol, and 100 mM ammonium phosphate. Protein was reconstituted in cubic phase using a 10:1 monolein:cholesterol mix by weight, Lipidic cubic phase, temperature 293K
|
Resolution 3.40 Å R-free 0.303 |
| 4DAJ Structure of the M3 Muscarinic Acetylcholine Receptor Deposited 2012-01-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 5 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–161（161 aa）
Fragment：P08483 residues 57-259, 482-589, P00720 residues 1-161
Chain B
1–161（161 aa）
Fragment：P08483 residues 57-259, 482-589, P00720 residues 1-161
|
Mutation：C1054T, C1097A Mutation：C1054T, C1097A | 0HK (1R,2R,4S,5S,7S)-7-{[hydroxy(dithiophen-2-yl)acetyl]oxy}-9,9-dimethyl-3-oxa-9-azoniatricyclo[3.3.1.0~2,4~]nonane × 2 PO4 PHOSPHATE ION × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；293 K；27-38% PEG 300, 100 mM HEPES pH 7.5, 1% (w/w) 1,2,3-heptanetriol, and 100 mM ammonium phosphate. Protein was reconstituted in cubic phase using a 10:1 monolein:cholesterol mix by weight, Lipidic cubic phase, temperature 293K
|
Resolution 3.40 Å R-free 0.303 |
| 4DAJ Structure of the M3 Muscarinic Acetylcholine Receptor Deposited 2012-01-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 6 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain C
1–161（161 aa）
Fragment：P08483 residues 57-259, 482-589, P00720 residues 1-161
Chain D
1–161（161 aa）
Fragment：P08483 residues 57-259, 482-589, P00720 residues 1-161
|
Mutation：C1054T, C1097A Mutation：C1054T, C1097A | 0HK (1R,2R,4S,5S,7S)-7-{[hydroxy(dithiophen-2-yl)acetyl]oxy}-9,9-dimethyl-3-oxa-9-azoniatricyclo[3.3.1.0~2,4~]nonane × 2 PO4 PHOSPHATE ION × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；293 K；27-38% PEG 300, 100 mM HEPES pH 7.5, 1% (w/w) 1,2,3-heptanetriol, and 100 mM ammonium phosphate. Protein was reconstituted in cubic phase using a 10:1 monolein:cholesterol mix by weight, Lipidic cubic phase, temperature 293K
|
Resolution 3.40 Å R-free 0.303 |
| 4DJH Structure of the human kappa opioid receptor in complex with JDTic Deposited 2012-02-01 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
Fragment：UNP P41145 residues 43-261, UNP P00720 residues 2-161, UNP P41145 residues 362-358
Chain B
2–161（160 aa）
Fragment：UNP P41145 residues 43-261, UNP P00720 residues 2-161, UNP P41145 residues 362-358
|
Mutation：I135L, C54T, C97A Mutation：I135L, C54T, C97A | JDC (3R)-7-hydroxy-N-{(2S)-1-[(3R,4R)-4-(3-hydroxyphenyl)-3,4-dimethylpiperidin-1-yl]-3-methylbutan-2-yl}-1,2,3,4-tetrahydroisoquinoline-3-carboxamide × 2 CIT CITRIC ACID × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2 PEG DI(HYDROXYETHYL)ETHER × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6；293 K；100 mM sodium citrate pH 6.0, 30% (v/v) PEG400, 400 mM potassium nitrate, lipidic cubic phase, temperature 293K
|
Resolution 2.90 Å R-free 0.265 |
| 4DJH Structure of the human kappa opioid receptor in complex with JDTic Deposited 2012-02-01 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
Fragment：UNP P41145 residues 43-261, UNP P00720 residues 2-161, UNP P41145 residues 362-358
Chain B
2–161（160 aa）
Fragment：UNP P41145 residues 43-261, UNP P00720 residues 2-161, UNP P41145 residues 362-358
|
Mutation：I135L, C54T, C97A Mutation：I135L, C54T, C97A | JDC (3R)-7-hydroxy-N-{(2S)-1-[(3R,4R)-4-(3-hydroxyphenyl)-3,4-dimethylpiperidin-1-yl]-3-methylbutan-2-yl}-1,2,3,4-tetrahydroisoquinoline-3-carboxamide × 2 CIT CITRIC ACID × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2 PEG DI(HYDROXYETHYL)ETHER × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6；293 K；100 mM sodium citrate pH 6.0, 30% (v/v) PEG400, 400 mM potassium nitrate, lipidic cubic phase, temperature 293K
|
Resolution 2.90 Å R-free 0.265 |
| 4DKL Crystal structure of the mu-opioid receptor bound to a morphinan antagonist Deposited 2012-02-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
Fragment：SEE REMARK 999
|
Mutation：D1020N, C1054T, C1097A | BF0 methyl 4-{[(5beta,6alpha)-17-(cyclopropylmethyl)-3,14-dihydroxy-4,5-epoxymorphinan-6-yl]amino}-4-oxobutanoate × 2 SO4 SULFATE ION × 24 CLR CHOLESTEROL × 2 MPG [(Z)-octadec-9-enyl] (2R)-2,3-bis(oxidanyl)propanoate × 4 1PE PENTAETHYLENE GLYCOL × 2 CL CHLORIDE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 7；293 K；100 mM HEPES, pH 7.0, 300 mM lithium sulfate, 7.5% DMSO, 30-38% PEG400 in monoolein:cholesterol mixed in a 10:1 ratio, LIPIDIC CUBIC PHASE, temperature 293K
|
Resolution 2.80 Å R-free 0.275 |
| 4E97 T4 Lysozyme L99A/M102H with 2-Mercaptoethanol Bound Deposited 2012-03-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 5 SO4 SULFATE ION × 3 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.30 Å R-free 0.166 |
| 4E97 T4 Lysozyme L99A/M102H with 2-Mercaptoethanol Bound Deposited 2012-03-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 3 SO4 SULFATE ION × 2 ACT ACETATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.30 Å R-free 0.166 |
| 4EJ4 Structure of the delta opioid receptor bound to naltrindole Deposited 2012-04-06 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
Fragment：P32300 residues 36-244, 251-342
|
Mutation：D1020N, C1054T, C1097A | EJ4 (4bS,8R,8aS,14bR)-7-(cyclopropylmethyl)-5,6,7,8,14,14b-hexahydro-4,8-methano[1]benzofuro[2,3-a]pyrido[4,3-b]carbazole-1,8a(9H)-diol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；293 K；29-33% PEG 400, 100 mM HEPES pH 7.5, 120-180 mM sodium citrate, 350 mM Magnesium chloride. Protein was mixed 1:1.5 (w:w) with 91% monoolein 9% cholesterol mixture by weight, Lipidic cubic phase, temperature 293K
|
Resolution 3.40 Å R-free 0.282 |
| 4EKP T4 Lysozyme L99A/M102H with Nitrobenzene Bound Deposited 2012-04-09 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102H/E108V/S117V/T142C/N144D | BME BETA-MERCAPTOETHANOL × 2 NBZ NITROBENZENE × 1 SO4 SULFATE ION × 3 ACT ACETATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.64 Å R-free 0.196 |
| 4EKP T4 Lysozyme L99A/M102H with Nitrobenzene Bound Deposited 2012-04-09 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102H/E108V/S117V/T142C/N144D | BME BETA-MERCAPTOETHANOL × 2 NBZ NITROBENZENE × 1 SO4 SULFATE ION × 2 ACT ACETATE ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.64 Å R-free 0.196 |
| 4EKP T4 Lysozyme L99A/M102H with Nitrobenzene Bound Deposited 2012-04-09 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–164（164 aa）
Chain B
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102H/E108V/S117V/T142C/N144D Mutation：T21C/S38D/L99A/M102H/E108V/S117V/T142C/N144D | BME BETA-MERCAPTOETHANOL × 4 NBZ NITROBENZENE × 2 SO4 SULFATE ION × 5 ACT ACETATE ION × 3 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.64 Å R-free 0.196 |
| 4EKQ T4 Lysozyme L99A/M102H with 4-Nitrophenol Bound Deposited 2012-04-09 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102H/E108V/S117V/T142C/N144D | BME BETA-MERCAPTOETHANOL × 1 NPO P-NITROPHENOL × 2 SO4 SULFATE ION × 3 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.54 Å R-free 0.204 |
| 4EKQ T4 Lysozyme L99A/M102H with 4-Nitrophenol Bound Deposited 2012-04-09 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102H/E108V/S117V/T142C/N144D | BME BETA-MERCAPTOETHANOL × 1 NPO P-NITROPHENOL × 1 SO4 SULFATE ION × 2 ACT ACETATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.54 Å R-free 0.204 |
| 4EKR T4 Lysozyme L99A/M102H with 2-Cyanophenol Bound Deposited 2012-04-09 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102H/E108V/S117V/T142C/N144D | BME BETA-MERCAPTOETHANOL × 2 0R0 2-hydroxybenzonitrile × 2 SO4 SULFATE ION × 2 ACT ACETATE ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.49 Å R-free 0.206 |
| 4EKR T4 Lysozyme L99A/M102H with 2-Cyanophenol Bound Deposited 2012-04-09 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102H/E108V/S117V/T142C/N144D | BME BETA-MERCAPTOETHANOL × 1 0R0 2-hydroxybenzonitrile × 1 SO4 SULFATE ION × 2 ACT ACETATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.49 Å R-free 0.206 |
| 4EKR T4 Lysozyme L99A/M102H with 2-Cyanophenol Bound Deposited 2012-04-09 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–164（164 aa）
Chain B
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102H/E108V/S117V/T142C/N144D Mutation：T21C/S38D/L99A/M102H/E108V/S117V/T142C/N144D | BME BETA-MERCAPTOETHANOL × 3 0R0 2-hydroxybenzonitrile × 3 SO4 SULFATE ION × 4 ACT ACETATE ION × 4 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.49 Å R-free 0.206 |
| 4EKS T4 Lysozyme L99A/M102H with Isoxazole Bound Deposited 2012-04-09 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102H/E108V/S117V/T142C/N144D | BME BETA-MERCAPTOETHANOL × 2 0R1 1,2-benzisoxazole × 1 SO4 SULFATE ION × 3 ACT ACETATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.64 Å R-free 0.198 |
| 4EKS T4 Lysozyme L99A/M102H with Isoxazole Bound Deposited 2012-04-09 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102H/E108V/S117V/T142C/N144D | BME BETA-MERCAPTOETHANOL × 2 0R1 1,2-benzisoxazole × 1 SO4 SULFATE ION × 2 ACT ACETATE ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.64 Å R-free 0.198 |
| 4EKS T4 Lysozyme L99A/M102H with Isoxazole Bound Deposited 2012-04-09 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–164（164 aa）
Chain B
1–164（164 aa）
|
Mutation：T21C/S38D/L99A/M102H/E108V/S117V/T142C/N144D Mutation：T21C/S38D/L99A/M102H/E108V/S117V/T142C/N144D | BME BETA-MERCAPTOETHANOL × 4 0R1 1,2-benzisoxazole × 2 SO4 SULFATE ION × 5 ACT ACETATE ION × 3 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.64 Å R-free 0.198 |
| 4EPI The crystal structure of pesticin-T4 lysozyme hybrid stabilized by engineered disulfide bonds Deposited 2012-04-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
4–165（162 aa）
Fragment：SEE REMARK 999
|
Mutation：I168C,I174C,C219T,L329C | SO4 SULFATE ION × 2 NA SODIUM ION × 8 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；20% w/v PEG3350, 0.25 M calcium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 1.74 Å R-free 0.200 |
| 4EXM The crystal structure of an engineered phage lysin containing the binding domain of pesticin and the killing domain of T4-lysozyme Deposited 2012-04-30 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
4–165（162 aa）
Fragment：SEE REMARK 999
Chain D
4–165（162 aa）
Fragment：SEE REMARK 999
|
Mutation：G182R,C267T,C267A,R307I Mutation：G182R,C267T,C267A,R307I | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；20% w/v PEG3350, 0.25 M calcium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K
|
Resolution 2.60 Å R-free 0.251 |
| 4EXM The crystal structure of an engineered phage lysin containing the binding domain of pesticin and the killing domain of T4-lysozyme Deposited 2012-04-30 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain B
4–165（162 aa）
Fragment：SEE REMARK 999
Chain C
4–165（162 aa）
Fragment：SEE REMARK 999
|
Mutation：G182R,C267T,C267A,R307I Mutation：G182R,C267T,C267A,R307I | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；20% w/v PEG3350, 0.25 M calcium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K
|
Resolution 2.60 Å R-free 0.251 |
| 4GBR N-Terminal T4 Lysozyme Fusion Facilitates Crystallization of a G Protein Coupled Receptor Deposited 2012-07-27 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain B
2–161（160 aa）
Fragment：UNP RESIDUES 2-161
|
Not recorded | CAU (2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.5；293 K；PEG300 37%
Bis-Tris propane 0.1M
Ammonium phosphate, dibasic, 0.1M, pH 6.5, lipidic cubic phase, temperature 293K
|
Resolution 3.99 Å R-free 0.282 |
| 4GRV The crystal structure of the neurotensin receptor NTS1 in complex with neurotensin (8-13) Deposited 2012-08-27 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
Fragment：see remark 999
|
Mutation：A86L, E166A, G215A, L310A, F358A, V360A | EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
Lipid cubic phase (LCP)；pH 7.4；298 K；80 mM HEPES pH 7.0, 2 mM TCEP, 43 mM NaK tartrate, 20.8% PEG400, Lipid cubic phase (LCP), temperature 298K
|
Resolution 2.80 Å R-free 0.282 |
| 4HTT Crystal Structure of Twin Arginine Translocase Receptor- TatC in DDM Deposited 2012-11-01 | Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.6；293 K；35% (v/v) PEG 400, ADA pH 6.6 and 0.1 M Potassium phosphate monobasic., VAPOR DIFFUSION, SITTING DROP, temperature 293K
|
Resolution 6.80 Å R-free 0.418 |
| 4HTT Crystal Structure of Twin Arginine Translocase Receptor- TatC in DDM Deposited 2012-11-01 | Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.6；293 K；35% (v/v) PEG 400, ADA pH 6.6 and 0.1 M Potassium phosphate monobasic., VAPOR DIFFUSION, SITTING DROP, temperature 293K
|
Resolution 6.80 Å R-free 0.418 |
| 4I7J T4 Lysozyme L99A/M102H with benzene bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 4 BNZ BENZENE × 1 SO4 SULFATE ION × 3 ACT ACETATE ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.67 Å R-free 0.239 |
| 4I7J T4 Lysozyme L99A/M102H with benzene bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 3 BNZ BENZENE × 1 SO4 SULFATE ION × 2 ACT ACETATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.67 Å R-free 0.239 |
| 4I7K T4 Lysozyme L99A/M102H with toluene bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 2 MBN TOLUENE × 1 SO4 SULFATE ION × 3 ACT ACETATE ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.72 Å R-free 0.201 |
| 4I7K T4 Lysozyme L99A/M102H with toluene bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 4 MBN TOLUENE × 1 SO4 SULFATE ION × 2 ACT ACETATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.72 Å R-free 0.201 |
| 4I7L T4 Lysozyme L99A/M102H with phenol bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 3 IPH PHENOL × 1 SO4 SULFATE ION × 3 ACT ACETATE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.52 Å R-free 0.181 |
| 4I7L T4 Lysozyme L99A/M102H with phenol bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 2 IPH PHENOL × 1 SO4 SULFATE ION × 2 ACT ACETATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.52 Å R-free 0.181 |
| 4I7M T4 Lysozyme L99A/M102H with 2-allylphenol bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 2 2LP 2-ALLYLPHENOL × 1 SO4 SULFATE ION × 2 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.48 Å R-free 0.198 |
| 4I7M T4 Lysozyme L99A/M102H with 2-allylphenol bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 2 2LP 2-ALLYLPHENOL × 1 SO4 SULFATE ION × 4 ACT ACETATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.48 Å R-free 0.198 |
| 4I7N T4 Lysozyme L99A/M102H with 1-phenyl-2-propyn-1-ol bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 3 1DJ (1R)-1-phenylprop-2-yn-1-ol × 1 SO4 SULFATE ION × 4 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.58 Å R-free 0.202 |
| 4I7N T4 Lysozyme L99A/M102H with 1-phenyl-2-propyn-1-ol bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 2 1DJ (1R)-1-phenylprop-2-yn-1-ol × 1 SO4 SULFATE ION × 2 ACT ACETATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.58 Å R-free 0.202 |
| 4I7O T4 Lysozyme L99A/M102H with 2-amino-5-chlorothiazole bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 3 1DH 5-chloro-1,3-thiazol-2-amine × 1 SO4 SULFATE ION × 5 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.73 Å R-free 0.194 |
| 4I7O T4 Lysozyme L99A/M102H with 2-amino-5-chlorothiazole bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 2 1DH 5-chloro-1,3-thiazol-2-amine × 1 SO4 SULFATE ION × 3 ACT ACETATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.73 Å R-free 0.194 |
| 4I7P T4 Lysozyme L99A/M102H with 4-bromoimidazole bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 2 ES3 4-bromo-1H-imidazole × 1 SO4 SULFATE ION × 6 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.60 Å R-free 0.204 |
| 4I7P T4 Lysozyme L99A/M102H with 4-bromoimidazole bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 1 ES3 4-bromo-1H-imidazole × 1 SO4 SULFATE ION × 3 ACT ACETATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.60 Å R-free 0.204 |
| 4I7Q T4 Lysozyme L99A/M102H with 4-trifluoromethylimidazole bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 3 1DQ 5-(trifluoromethyl)-1H-imidazole × 1 SO4 SULFATE ION × 6 ACT ACETATE ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.58 Å R-free 0.213 |
| 4I7Q T4 Lysozyme L99A/M102H with 4-trifluoromethylimidazole bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 2 1DQ 5-(trifluoromethyl)-1H-imidazole × 1 SO4 SULFATE ION × 2 ACT ACETATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.58 Å R-free 0.213 |
| 4I7R T4 Lysozyme L99A/M102H with 2-(pyrazolo-1-yl) ethanol bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 3 1DU 2-(1H-pyrazol-1-yl)ethanol × 1 SO4 SULFATE ION × 4 ACT ACETATE ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.52 Å R-free 0.190 |
| 4I7R T4 Lysozyme L99A/M102H with 2-(pyrazolo-1-yl) ethanol bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 3 1DU 2-(1H-pyrazol-1-yl)ethanol × 1 SO4 SULFATE ION × 2 ACT ACETATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.52 Å R-free 0.190 |
| 4I7S T4 Lysozyme L99A/M102H with 3-trifluoromethyl-5-methyl pyrazole bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 1 1DV 5-methyl-3-(trifluoromethyl)-1H-pyrazole × 1 SO4 SULFATE ION × 4 ACT ACETATE ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.69 Å R-free 0.196 |
| 4I7S T4 Lysozyme L99A/M102H with 3-trifluoromethyl-5-methyl pyrazole bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 1 1DV 5-methyl-3-(trifluoromethyl)-1H-pyrazole × 1 SO4 SULFATE ION × 3 ACT ACETATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.69 Å R-free 0.196 |
| 4I7T T4 Lysozyme L99A/M102H with 2-bromo-5-hydroxybenzaldehyde bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 2 1DW 2-bromo-5-hydroxybenzaldehyde × 1 SO4 SULFATE ION × 3 ACT ACETATE ION × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.55 Å R-free 0.199 |
| 4I7T T4 Lysozyme L99A/M102H with 2-bromo-5-hydroxybenzaldehyde bound Deposited 2012-11-30 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Mutation：T21C, S38D, L99A, M102H, E108V, S117V, T142C, N144D | BME BETA-MERCAPTOETHANOL × 2 1DW 2-bromo-5-hydroxybenzaldehyde × 1 SO4 SULFATE ION × 2 ACT ACETATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, vapor diffusion, hanging drop, temperature 277K
|
Resolution 1.55 Å R-free 0.199 |
| 4IAP Crystal structure of PH domain of Osh3 from Saccharomyces cerevisiae Deposited 2012-12-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
Fragment：PH domain (UNP residues 221-317), T4 Lysozyme (UNP residues 2-161),PH domain (UNP residues 237-315)
|
Mutation：D1020N, C1054T, C1097A | SO4 SULFATE ION × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；0.1M Tris-HCl, 15% PEG8000, 0.2 M
Li2SO4, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 2.30 Å R-free 0.274 |
| 4IAP Crystal structure of PH domain of Osh3 from Saccharomyces cerevisiae Deposited 2012-12-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–161（160 aa）
Fragment：PH domain (UNP residues 221-317), T4 Lysozyme (UNP residues 2-161),PH domain (UNP residues 237-315)
|
Mutation：D1020N, C1054T, C1097A | SO4 SULFATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；0.1M Tris-HCl, 15% PEG8000, 0.2 M
Li2SO4, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 2.30 Å R-free 0.274 |
| 4IAP Crystal structure of PH domain of Osh3 from Saccharomyces cerevisiae Deposited 2012-12-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
Fragment：PH domain (UNP residues 221-317), T4 Lysozyme (UNP residues 2-161),PH domain (UNP residues 237-315)
Chain B
2–161（160 aa）
Fragment：PH domain (UNP residues 221-317), T4 Lysozyme (UNP residues 2-161),PH domain (UNP residues 237-315)
|
Mutation：D1020N, C1054T, C1097A Mutation：D1020N, C1054T, C1097A | SO4 SULFATE ION × 8 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；0.1M Tris-HCl, 15% PEG8000, 0.2 M
Li2SO4, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 2.30 Å R-free 0.274 |
| 4K5Y Crystal structure of human corticotropin-releasing factor receptor 1 (CRF1R) in complex with the antagonist CP-376395 Deposited 2013-04-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
Fragment：UNP P34998 RESIDUES 104-220, UNP P00720 RESIDUES 2-161, UNP P34998 RESIDUES 224-373
|
Mutation：v120a, l144a, w156a, s160a, n40s, a41v, c54s, c97s, t151a, k228a, f260a, i277a, y309a, f330a, s349a, y363a | 1Q5 3,6-dimethyl-N-(pentan-3-yl)-2-(2,4,6-trimethylphenoxy)pyridin-4-amine × 1 OLA OLEIC ACID × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 5.5；295.6 K；30% (v/v) PEG 400, 0.2M lithium sulphate, 0.1M sodium citrate 5.5, Lipidic Cubic Phase, temperature 295.6K
|
Resolution 2.98 Å R-free 0.265 |
| 4K5Y Crystal structure of human corticotropin-releasing factor receptor 1 (CRF1R) in complex with the antagonist CP-376395 Deposited 2013-04-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–161（160 aa）
Fragment：UNP P34998 RESIDUES 104-220, UNP P00720 RESIDUES 2-161, UNP P34998 RESIDUES 224-373
|
Mutation：v120a, l144a, w156a, s160a, n40s, a41v, c54s, c97s, t151a, k228a, f260a, i277a, y309a, f330a, s349a, y363a | 1Q5 3,6-dimethyl-N-(pentan-3-yl)-2-(2,4,6-trimethylphenoxy)pyridin-4-amine × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 1 SO4 SULFATE ION × 3 PGW (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate × 3 1PE PENTAETHYLENE GLYCOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 5.5；295.6 K；30% (v/v) PEG 400, 0.2M lithium sulphate, 0.1M sodium citrate 5.5, Lipidic Cubic Phase, temperature 295.6K
|
Resolution 2.98 Å R-free 0.265 |
| 4K5Y Crystal structure of human corticotropin-releasing factor receptor 1 (CRF1R) in complex with the antagonist CP-376395 Deposited 2013-04-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
2–161（160 aa）
Fragment：UNP P34998 RESIDUES 104-220, UNP P00720 RESIDUES 2-161, UNP P34998 RESIDUES 224-373
|
Mutation：v120a, l144a, w156a, s160a, n40s, a41v, c54s, c97s, t151a, k228a, f260a, i277a, y309a, f330a, s349a, y363a | 1Q5 3,6-dimethyl-N-(pentan-3-yl)-2-(2,4,6-trimethylphenoxy)pyridin-4-amine × 1 OLA OLEIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 5.5；295.6 K；30% (v/v) PEG 400, 0.2M lithium sulphate, 0.1M sodium citrate 5.5, Lipidic Cubic Phase, temperature 295.6K
|
Resolution 2.98 Å R-free 0.265 |
| 4LDE Structure of beta2 adrenoceptor bound to BI167107 and an engineered nanobody Deposited 2013-06-24 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
Fragment：UNP residues 29-348 with a deletion of residues 235-263
|
Mutation：C918T, C962A, M1096T, M1098T, N1157E, C1265A | P0G 8-[(1R)-2-{[1,1-dimethyl-2-(2-methylphenyl)ethyl]amino}-1-hydroxyethyl]-5-hydroxy-2H-1,4-benzoxazin-3(4H)-one × 1 NA SODIUM ION × 1 1WV (2S)-2,3-dihydroxypropyl (7Z)-tetradec-7-enoate × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6.5；293 K；100 mM MES pH 6.2-6.7, 40-100 mM ammonium phosphate dibasic, 18-24% PEG400, LIPIDIC CUBIC PHASE, temperature 293K
|
Resolution 2.79 Å R-free 0.256 |
| 4LDL Structure of beta2 adrenoceptor bound to hydroxybenzylisoproterenol and an engineered nanobody Deposited 2013-06-24 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
|
Mutation：C918T, C962A, M1096T, M1098T, N1157E, C1265A | XQC 4-[(1R)-1-hydroxy-2-{[1-(4-hydroxyphenyl)-2-methylpropan-2-yl]amino}ethyl]benzene-1,2-diol × 1 NA SODIUM ION × 1 1WV (2S)-2,3-dihydroxypropyl (7Z)-tetradec-7-enoate × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6.5；293 K；100 mM MES pH 6.2-6.7, 40-100 mM ammonium phosphate dibasic, 18-24% PEG400, LIPIDIC CUBIC PHASE, temperature 293K
|
Resolution 3.10 Å R-free 0.254 |
| 4LDO Structure of beta2 adrenoceptor bound to adrenaline and an engineered nanobody Deposited 2013-06-24 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
|
Mutation：C918T, C962A, M1096T, M1098T, N1157E, C1265A | 1WV (2S)-2,3-dihydroxypropyl (7Z)-tetradec-7-enoate × 1 ALE L-EPINEPHRINE × 1 NA SODIUM ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6.5；293 K；100 mM MES pH 6.2-6.7, 40-100 mM ammonium phosphate dibasic, 18-24% PEG400, LIPIDIC CUBIC PHASE, temperature 293K
|
Resolution 3.20 Å R-free 0.254 |
| 4LZM COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS Deposited 1991-01-25 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å |
| 4N9N Crystal Structure of Saccharomyces cerevisiae Upc2 Transcription Factor fused with T4 Lysozyme Deposited 2013-10-21 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
Fragment：residues 598-714 and 726-878 of Q12151, residues 2-161 of P00720
Chain B
2–161（160 aa）
Fragment：residues 598-714 and 726-878 of Q12151, residues 2-161 of P00720
|
Mutation：C1054T, C1097A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C1054T, C1097A Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；0.1M HEPES, 12.5% PEG 8000, 0.2M sodium citrate, 7.5% glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 2.90 Å R-free 0.272 |
| 4OO9 Structure of the human class C GPCR metabotropic glutamate receptor 5 transmembrane domain in complex with the negative allosteric modulator mavoglurant Deposited 2014-01-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–162（161 aa）
Fragment：SEE REMARK 999
|
Mutation：yes Non-standard monomer：Yes (specific site not provided by mmCIF) | OLA OLEIC ACID × 4 2U8 Mavoglurant × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6.8；293.1 K；24-34% v/v PEG400, 0.2 M ammonium phosphate dibasic, 0.1 M MES, pH 6.8, LIPIDIC CUBIC PHASE, temperature 293.1K
|
Resolution 2.60 Å R-free 0.275 |
| 4PHU Crystal structure of Human GPR40 bound to allosteric agonist TAK-875 Deposited 2014-05-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
Fragment：UNP O14842 residues 2-213, UNP P00720 residues 2-161, UNP O14842 residues 214-300
|
Mutation：L42A,F88A,G103A,Y202F,S211G,G212S,C1154T,C1197A | 2YB [(3S)-6-({2',6'-dimethyl-4'-[3-(methylsulfonyl)propoxy]biphenyl-3-yl}methoxy)-2,3-dihydro-1-benzofuran-3-yl]acetic acid × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 5 1PE PENTAETHYLENE GLYCOL × 1 DMS DIMETHYL SULFOXIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 8；294 K；29-31% Peg 400,100 mM Tris pH 8.0. 0.2 M Na Malonate,200 uM TAK-875
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 7.2；294 K；39.8 % Peg 400, 100 mM Bis-Tris-Propane pH 7.2, 0.1 Ammonium Phosphate (monobasic), 200 uM TAK-875
|
Resolution 2.33 Å R-free 0.233 |
| 4RWS Crystal structure of CXCR4 and viral chemokine antagonist vMIP-II complex (PSI Community Target) Deposited 2014-12-05 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
1002–1161（160 aa）
Fragment：CXCR4 residues 2-228, LYSOZYME residues 1002-1161, CXCR4 residues 231-319
|
Mutation：L125W, T240P, D187C, C1054T, C1097T | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 5.5；293 K；100 mM sodium citrate pH 5.5, 28% PEG 400, 120 mM ammonium phosphate dibasic, 2-6% polypropylene P400, Lipidic cubic phase, temperature 293K
|
Resolution 3.10 Å R-free 0.274 |
| 4TN3 Structure of the BBox-Coiled-coil region of Rhesus Trim5alpha Deposited 2014-06-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–164（164 aa）
Chain B
1–164（164 aa）
|
Not recorded | ZN ZINC ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；291 K；10% PEG4000, 20% Glycerol, 0.2M monosaccharides, 0.1M Bis/Tris pH 8.5
|
Resolution 3.20 Å R-free 0.316 |
| 4U14 Structure of the M3 muscarinic acetylcholine receptor bound to the antagonist tiotropium crystallized with disulfide-stabilized T4 lysozyme (dsT4L) Deposited 2014-07-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–161（161 aa）
Fragment：UNP P08483 residues 57-259, 482-563, P00720 residues 1-161
|
Not recorded | 0HK (1R,2R,4S,5S,7S)-7-{[hydroxy(dithiophen-2-yl)acetyl]oxy}-9,9-dimethyl-3-oxa-9-azoniatricyclo[3.3.1.0~2,4~]nonane × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 8.1；298 K；45% PEG 300, 110 mM ammonium sulfate, 113.5 mM lithium citrate, 100 mM Tris
|
Resolution 3.57 Å R-free 0.325 |
| 4U14 Structure of the M3 muscarinic acetylcholine receptor bound to the antagonist tiotropium crystallized with disulfide-stabilized T4 lysozyme (dsT4L) Deposited 2014-07-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–161（161 aa）
Fragment：UNP P08483 residues 57-259, 482-563, P00720 residues 1-161
|
Not recorded | 0HK (1R,2R,4S,5S,7S)-7-{[hydroxy(dithiophen-2-yl)acetyl]oxy}-9,9-dimethyl-3-oxa-9-azoniatricyclo[3.3.1.0~2,4~]nonane × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 8.1；298 K；45% PEG 300, 110 mM ammonium sulfate, 113.5 mM lithium citrate, 100 mM Tris
|
Resolution 3.57 Å R-free 0.325 |
| 4W51 T4 Lysozyme L99A with No Ligand Bound Deposited 2014-08-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A | EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；20% (w/v) PEGF-4000, 10% 2-propanol, 0.1 M HEPES, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.45 Å R-free 0.192 |
| 4W52 T4 Lysozyme L99A with Benzene Bound Deposited 2014-08-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A | BNZ BENZENE × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；20% (w/v) PEGF-4000, 10% 2-propanol, 0.1 M HEPES, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.50 Å R-free 0.182 |
| 4W53 T4 Lysozyme L99A with Toluene Bound Deposited 2014-08-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A | MBN TOLUENE × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；20% (w/v) PEGF-4000, 10% 2-propanol, 0.1 M HEPES, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.56 Å R-free 0.205 |
| 4W54 T4 Lysozyme L99A with Ethylbenzene Bound Deposited 2014-08-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A | PYJ PHENYLETHANE × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；20% (w/v) PEGF-4000, 10% 2-propanol, 0.1 M HEPES, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.79 Å R-free 0.198 |
| 4W55 T4 Lysozyme L99A with n-Propylbenzene Bound Deposited 2014-08-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A | 3H0 propylbenzene × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；20% (w/v) PEGF-4000, 10% 2-propanol, 0.1 M HEPES, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.64 Å R-free 0.187 |
| 4W56 T4 Lysozyme L99A with sec-Butylbenzene Bound Deposited 2014-08-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A | 3GY (2R)-butan-2-ylbenzene × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；20% (w/v) PEGF-4000, 10% 2-propanol, 0.1 M HEPES, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.63 Å R-free 0.188 |
| 4W57 T4 Lysozyme L99A with n-Butylbenzene Bound Deposited 2014-08-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A | N4B N-BUTYLBENZENE × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；20% (w/v) PEGF-4000, 10% 2-propanol, 0.1 M HEPES, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.68 Å R-free 0.185 |
| 4W58 T4 Lysozyme L99A with n-Pentylbenzene Bound Deposited 2014-08-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A | 3H2 pentylbenzene × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；20% (w/v) PEGF-4000, 10% 2-propanol, 0.1 M HEPES, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.80 Å R-free 0.184 |
| 4W59 T4 Lysozyme L99A with n-Hexylbenzene Bound Deposited 2014-08-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：L99A | 3GZ hexylbenzene × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；20% (w/v) PEGF-4000, 10% 2-propanol, 0.1 M HEPES, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.39 Å R-free 0.187 |
| 4W8F Crystal structure of the dynein motor domain in the AMPPNP-bound state Deposited 2014-08-24 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：E1849Q | ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；295 K；4-10% PEG 3350 and 200-300 mM NaAc
|
Resolution 3.54 Å R-free 0.262 |
| 4W8F Crystal structure of the dynein motor domain in the AMPPNP-bound state Deposited 2014-08-24 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–161（160 aa）
|
Mutation：E1849Q | ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；295 K；4-10% PEG 3350 and 200-300 mM NaAc
|
Resolution 3.54 Å R-free 0.262 |
| 4W8F Crystal structure of the dynein motor domain in the AMPPNP-bound state Deposited 2014-08-24 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
Chain B
2–161（160 aa）
|
Mutation：E1849Q Mutation：E1849Q | ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 8 MG MAGNESIUM ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；295 K；4-10% PEG 3350 and 200-300 mM NaAc
|
Resolution 3.54 Å R-free 0.262 |
| 4WTV Crystal structure of the phosphatidylinositol 4-kinase IIbeta Deposited 2014-10-30 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–164（163 aa）
Fragment：;UNP residues 90-165,UNP residues 2-164,UNP residues 176-450,UNP residues 90-165,UNP residues 2-164,UNP residues 176-450,UNP residues 90-165,UNP residues 2-164,UNP residues 176-450
;
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；100 mM MES/Imidazole pH = 6.5, 10% w/v PEG 4000, 20% v/v glycerol, 20 mM 1,6-hexanediol, 20 mM 1-butanol, 20 mM 1,2-propanediol, 20 mM 2-propanol, 20 mM 1,4-butanediol, 20 mM 1,3-propanediol
|
Resolution 1.90 Å R-free 0.240 |
| 4WTV Crystal structure of the phosphatidylinositol 4-kinase IIbeta Deposited 2014-10-30 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–164（163 aa）
Fragment：;UNP residues 90-165,UNP residues 2-164,UNP residues 176-450,UNP residues 90-165,UNP residues 2-164,UNP residues 176-450,UNP residues 90-165,UNP residues 2-164,UNP residues 176-450
;
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；100 mM MES/Imidazole pH = 6.5, 10% w/v PEG 4000, 20% v/v glycerol, 20 mM 1,6-hexanediol, 20 mM 1-butanol, 20 mM 1,2-propanediol, 20 mM 2-propanol, 20 mM 1,4-butanediol, 20 mM 1,3-propanediol
|
Resolution 1.90 Å R-free 0.240 |
| 4XEE Structure of active-like neurotensin receptor Deposited 2014-12-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
Fragment：UNP residues 43-396 (P20789), residues 2-161 (P00720)
|
Mutation：A86L, G215A, V360A | 1PE PENTAETHYLENE GLYCOL × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 FLC CITRATE ANION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；16-24% PEG400, 75 mM HEPES, pH 7.0-8.0, 1.7 mM TCEP, 32 mM lithium citrate, 0.9 mM Neurotensin (8-13)
|
Resolution 2.90 Å R-free 0.281 |
| 4XES Structure of active-like neurotensin receptor Deposited 2014-12-24 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
Fragment：UNP residues 43-396 (P20789), residues 2-161 (P00720)
|
Mutation：A86L, E166A, G215A, V360A | CIT CITRIC ACID × 1 PEG DI(HYDROXYETHYL)ETHER × 5 GOL GLYCEROL × 3 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；19.8-23.4% PEG400, 80 mM HEPES, 50 mM lithium citrate, 2 mM TCEP
|
Resolution 2.60 Å R-free 0.280 |
| 4YX7 Complex of SpaO(SPOA1,2) and OrgB(APAR)::T4lysozyme fusion protein Deposited 2015-03-22 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric |
Chain C
2–164（163 aa）
Fragment：UNP Residues 1-30,UNP Residues 1-30
|
Mutation：D20N,C54T,C97A,D20N,C54T,C97A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；SpaO(145-213) + SpaO (232-297) + OrgB(1-30)::T4 lysozyme was concentrated to 18.5mg/mL and crystallized with 25% PEG3350, 200mM ammonium formate, 100mM sodium acetate pH=5.0. Microseeding was employed to enhance crystal uniformity and diffraction. Briefly, crystals to be seeded were harvested in precipitant solution and vortexed in a microfuge tube with a small stir bar for ~60 seconds. The slurry of microseeds was serially dilluted (5-10-fold steps) in precipitant solution and 5 selected microseed-precipitant mixtures were mixed with fresh protein as in a normal hanging drop experiment. Crystals were cryoprotected in 30% PEG3350, 10% glycerol, 200mM ammonium acetate, 100mM sodium acetate pH=5.0.
|
Resolution 2.00 Å R-free 0.210 |
| 4YX7 Complex of SpaO(SPOA1,2) and OrgB(APAR)::T4lysozyme fusion protein Deposited 2015-03-22 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric |
Chain F
2–164（163 aa）
Fragment：UNP Residues 1-30,UNP Residues 1-30
|
Mutation：D20N,C54T,C97A,D20N,C54T,C97A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；SpaO(145-213) + SpaO (232-297) + OrgB(1-30)::T4 lysozyme was concentrated to 18.5mg/mL and crystallized with 25% PEG3350, 200mM ammonium formate, 100mM sodium acetate pH=5.0. Microseeding was employed to enhance crystal uniformity and diffraction. Briefly, crystals to be seeded were harvested in precipitant solution and vortexed in a microfuge tube with a small stir bar for ~60 seconds. The slurry of microseeds was serially dilluted (5-10-fold steps) in precipitant solution and 5 selected microseed-precipitant mixtures were mixed with fresh protein as in a normal hanging drop experiment. Crystals were cryoprotected in 30% PEG3350, 10% glycerol, 200mM ammonium acetate, 100mM sodium acetate pH=5.0.
|
Resolution 2.00 Å R-free 0.210 |
| 4YXA Complex of SpaO(SPOA1,2 SeMet) and OrgB(APAR)::T4lysozyme fusion protein Deposited 2015-03-22 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric |
Chain C
2–164（163 aa）
Fragment：UNP Residues 1-30,UNP Residues 1-30
|
Mutation：D20N, C54T, C97A,D20N, C54T, C97A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；SpaO(145-213, SeMet) + SpaO (232-297, SeMet) + OrgB(1-30)::T4 lysozyme (native) was concentrated to 18mg/mL, supplemented with 50mM maltose, and crystallized with 25% PEG3350, 200mM ammonium formate, 100mM sodium acetate pH=5.0. Microseeding was employed to enhance crystal uniformity and diffraction. Briefly, crystals to be seeded were harvested in precipitant solution and vortexed in a microfuge tube with a small stir bar for ~60 seconds. The slurry of microseeds was serially dilluted (5-10-fold steps) in precipitant solution and 5 selected microseed-precipitant mixtures were mixed with fresh protein as in a normal hanging drop experiment. Crystals were cryoprotected in 25% PEG3350, 10% ethylene glycol, 200mM ammonium formate, 100mM sodium acetate pH=5.0, 50mM maltose.
|
Resolution 2.35 Å R-free 0.262 |
| 4YXA Complex of SpaO(SPOA1,2 SeMet) and OrgB(APAR)::T4lysozyme fusion protein Deposited 2015-03-22 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric |
Chain F
2–164（163 aa）
Fragment：UNP Residues 1-30,UNP Residues 1-30
|
Mutation：D20N, C54T, C97A,D20N, C54T, C97A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；SpaO(145-213, SeMet) + SpaO (232-297, SeMet) + OrgB(1-30)::T4 lysozyme (native) was concentrated to 18mg/mL, supplemented with 50mM maltose, and crystallized with 25% PEG3350, 200mM ammonium formate, 100mM sodium acetate pH=5.0. Microseeding was employed to enhance crystal uniformity and diffraction. Briefly, crystals to be seeded were harvested in precipitant solution and vortexed in a microfuge tube with a small stir bar for ~60 seconds. The slurry of microseeds was serially dilluted (5-10-fold steps) in precipitant solution and 5 selected microseed-precipitant mixtures were mixed with fresh protein as in a normal hanging drop experiment. Crystals were cryoprotected in 25% PEG3350, 10% ethylene glycol, 200mM ammonium formate, 100mM sodium acetate pH=5.0, 50mM maltose.
|
Resolution 2.35 Å R-free 0.262 |
| 4YXC Complex of FliM(SPOA)::FliN fusion protein and FliH(APAR)::T4lysozyme fusion protein Deposited 2015-03-23 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
Fragment：UNP Residues 1-18
|
Mutation：D20N, C54T, C97A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；FliM(245-334)::FliN(5-137) + FliH(1-18)::T4 lysozyme was concentrated to 17mg/mL and crystallized with 11% PEG400, 100mM sodium potassium phosphate pH=6.5. Crystals were cryoprotected with 40% PEG400, 200mM sodium potassium phosphate pH=6.5.
|
Resolution 2.30 Å R-free 0.262 |
| 4ZWJ Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser Deposited 2015-05-19 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：R12G, C54T, C97A , I137R,N2C, E113Q, M257Y, N282C,L374A, V375A, F376A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 5；293 K；PEG400, sodium acetate, magnesium acetate
|
Resolution 3.30 Å R-free 0.293 |
| 4ZWJ Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser Deposited 2015-05-19 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–161（160 aa）
|
Mutation：R12G, C54T, C97A , I137R,N2C, E113Q, M257Y, N282C,L374A, V375A, F376A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 5；293 K；PEG400, sodium acetate, magnesium acetate
|
Resolution 3.30 Å R-free 0.293 |
| 4ZWJ Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser Deposited 2015-05-19 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
2–161（160 aa）
|
Mutation：R12G, C54T, C97A , I137R,N2C, E113Q, M257Y, N282C,L374A, V375A, F376A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 5；293 K；PEG400, sodium acetate, magnesium acetate
|
Resolution 3.30 Å R-free 0.293 |
| 4ZWJ Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser Deposited 2015-05-19 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
2–161（160 aa）
|
Mutation：R12G, C54T, C97A , I137R,N2C, E113Q, M257Y, N282C,L374A, V375A, F376A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 5；293 K；PEG400, sodium acetate, magnesium acetate
|
Resolution 3.30 Å R-free 0.293 |
| 5B2G Crystal structure of human claudin-4 in complex with C-terminal fragment of Clostridium perfringens enterotoxin Deposited 2016-01-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
2–162（161 aa）
Fragment：UNP residues 2-162,UNP residues 1-183
|
Mutation：R1012G, C1054T, C1097A, I1137R | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；288 K；75mM MES-NaOH, 20% PEG3350, 7-10% 1,6-hexanediol, 0.002% NaN3, 0.0005% 2,6-di-t-butyl-p-cresol, 150mM NaCl
|
Resolution 3.50 Å R-free 0.309 |
| 5B2G Crystal structure of human claudin-4 in complex with C-terminal fragment of Clostridium perfringens enterotoxin Deposited 2016-01-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain C
2–162（161 aa）
Fragment：UNP residues 2-162,UNP residues 1-183
|
Mutation：R1012G, C1054T, C1097A, I1137R | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；288 K；75mM MES-NaOH, 20% PEG3350, 7-10% 1,6-hexanediol, 0.002% NaN3, 0.0005% 2,6-di-t-butyl-p-cresol, 150mM NaCl
|
Resolution 3.50 Å R-free 0.309 |
| 5B2G Crystal structure of human claudin-4 in complex with C-terminal fragment of Clostridium perfringens enterotoxin Deposited 2016-01-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain E
2–162（161 aa）
Fragment：UNP residues 2-162,UNP residues 1-183
|
Mutation：R1012G, C1054T, C1097A, I1137R | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；288 K；75mM MES-NaOH, 20% PEG3350, 7-10% 1,6-hexanediol, 0.002% NaN3, 0.0005% 2,6-di-t-butyl-p-cresol, 150mM NaCl
|
Resolution 3.50 Å R-free 0.309 |
| 5B2G Crystal structure of human claudin-4 in complex with C-terminal fragment of Clostridium perfringens enterotoxin Deposited 2016-01-15 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain G
2–162（161 aa）
Fragment：UNP residues 2-162,UNP residues 1-183
|
Mutation：R1012G, C1054T, C1097A, I1137R | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；288 K；75mM MES-NaOH, 20% PEG3350, 7-10% 1,6-hexanediol, 0.002% NaN3, 0.0005% 2,6-di-t-butyl-p-cresol, 150mM NaCl
|
Resolution 3.50 Å R-free 0.309 |
| 5CGC Structure of the human class C GPCR metabotropic glutamate receptor 5 transmembrane domain in complex with the negative allosteric modulator 3-chloro-4-fluoro-5-[6-(1H-pyrazol-1-yl)pyrimidin-4-yl]benzonitrile Deposited 2015-07-09 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：;E579A N667Y I669A G675M C1054T C1097A T742A S753A,E579A N667Y I669A G675M C1054T C1097A T742A S753A,E579A N667Y I669A G675M C1054T C1097A T742A S753A ; | OLA OLEIC ACID × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 51D 3-chloro-4-fluoro-5-[6-(1H-pyrazol-1-yl)pyrimidin-4-yl]benzonitrile × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6.8；293.1 K；24-34% V/V PEG400, 0.2 M AMMONIUM PHOSPHATE DIBASIC, 0.1 M MES, PH 6.8,
|
Resolution 3.10 Å R-free 0.287 |
| 5CGD 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) Deposited 2015-07-09 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：;E579A N667Y I669A G675M C1054T C1097A T742A S753A,E579A N667Y I669A G675M C1054T C1097A T742A S753A,E579A N667Y I669A G675M C1054T C1097A T742A S753A ; | OLA OLEIC ACID × 4 51E 3-chloro-5-[6-(5-fluoropyridin-2-yl)pyrimidin-4-yl]benzonitrile × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6.8；293.1 K；24-34% V/V PEG400, 0.2 M AMMONIUM PHOSPHATE DIBASIC, 0.1 M MES, PH 6.8,
|
Resolution 2.60 Å R-free 0.285 |
| 5CXV Structure of the human M1 muscarinic acetylcholine receptor bound to antagonist Tiotropium Deposited 2015-07-29 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
|
Mutation：N110Q, C1052T, C1095A,N110Q, C1052T, C1095A,N110Q, C1052T, C1095A | 0HK (1R,2R,4S,5S,7S)-7-{[hydroxy(dithiophen-2-yl)acetyl]oxy}-9,9-dimethyl-3-oxa-9-azoniatricyclo[3.3.1.0~2,4~]nonane × 1 Y01 CHOLESTEROL HEMISUCCINATE × 1 EDO 1,2-ETHANEDIOL × 3 PGE TRIETHYLENE GLYCOL × 1 GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；33% PEG 300, 100 mM sodium acetate, and 100 mM Bis-Tris Propane (pH 8.0)
|
Resolution 2.70 Å R-free 0.282 |
| 5D5A In meso in situ serial X-ray crystallography structure of the Beta2-adrenergic receptor at 100 K Deposited 2015-08-10 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：;N187E, C54T, C97A,N187E, C54T, C97A,N187E, C54T, C97A,N187E, C54T, C97A,N187E, C54T, C97A,N187E, C54T, C97A,N187E, C54T, C97A,N187E, C54T, C97A,N187E, C54T, C97A ; | CAU (2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol × 1 BU1 1,4-BUTANEDIOL × 2 ACM ACETAMIDE × 1 CLR CHOLESTEROL × 3 PLM PALMITIC ACID × 1 12P DODECAETHYLENE GLYCOL × 1 SO4 SULFATE ION × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；30-35 %(v/v) PEG 400, 0.1-0.2 M Na2SO4, 0.1 M bis-tris propane pH 6.5-7.0 and 5-7 %(v/v) 1,4-butanediol
|
Resolution 2.48 Å R-free 0.262 |
| 5D5B In meso X-ray crystallography structure of the Beta2-adrenergic receptor at 100 K Deposited 2015-08-10 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：;N187E, C54T, C97A,N187E, C54T, C97A,N187E, C54T, C97A,N187E, C54T, C97A,N187E, C54T, C97A,N187E, C54T, C97A,N187E, C54T, C97A,N187E, C54T, C97A,N187E, C54T, C97A ; | CAU (2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol × 1 BU1 1,4-BUTANEDIOL × 1 ACM ACETAMIDE × 1 CLR CHOLESTEROL × 3 PLM PALMITIC ACID × 1 SO4 SULFATE ION × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；30-35 %(v/v) PEG 400, 0.1-0.2 M Na2SO4, 0.1 M bis-tris propane pH 6.5-7.0 and 5-7 %(v/v) 1,4-butanediol
|
Resolution 3.80 Å R-free 0.274 |
| 5D6L beta2AR-T4L - CIM Deposited 2015-08-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–162（162 aa）
|
Mutation：N187E, C54T, C97A,N187E, C54T, C97A,N187E, C54T, C97A | SO4 SULFATE ION × 6 CAU (2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol × 1 BU1 1,4-BUTANEDIOL × 2 ACM ACETAMIDE × 1 CLR CHOLESTEROL × 3 PLM PALMITIC ACID × 1 12P DODECAETHYLENE GLYCOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；30 - 35 % Peg 400, 5 -10 % butanediol, 0.1 - 0.35 mM Na sulphate, 0.1 M Bis-Tris pH 7.0.
|
Resolution 3.20 Å R-free 0.260 |
| 5DGY Crystal structure of rhodopsin bound to visual arrestin Deposited 2015-08-28 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
Chain C
2–161（160 aa）
|
Mutation：R12G, C54T, C97A , I137R,N2C, E113Q, M257Y, N282C,L374A, V375A, F376A Mutation：R12G, C54T, C97A , I137R,N2C, E113Q, M257Y, N282C,L374A, V375A, F376A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 5；293 K；PEG400
|
Resolution 7.70 Å R-free 0.335 |
| 5DGY Crystal structure of rhodopsin bound to visual arrestin Deposited 2015-08-28 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain B
2–161（160 aa）
Chain D
2–161（160 aa）
|
Mutation：R12G, C54T, C97A , I137R,N2C, E113Q, M257Y, N282C,L374A, V375A, F376A Mutation：R12G, C54T, C97A , I137R,N2C, E113Q, M257Y, N282C,L374A, V375A, F376A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 5；293 K；PEG400
|
Resolution 7.70 Å R-free 0.335 |
| 5DSG Structure of the M4 muscarinic acetylcholine receptor (M4-mT4L) bound to tiotropium Deposited 2015-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–11（10 aa）
Chain A
61–161（101 aa）
|
Not recorded | 0HK (1R,2R,4S,5S,7S)-7-{[hydroxy(dithiophen-2-yl)acetyl]oxy}-9,9-dimethyl-3-oxa-9-azoniatricyclo[3.3.1.0~2,4~]nonane × 1 OLA OLEIC ACID × 3 EDT {[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC ACID × 1 P6G HEXAETHYLENE GLYCOL × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；Reconstituted in 10:1 monoolein:cholesterol mix. Precipitant solution: 20 - 40% PEG300, 100 mM MES, pH 5.5 - 7.5, and 10 - 150 mM EDTA, pH 8.0
|
Resolution 2.60 Å R-free 0.240 |
| 5DSG Structure of the M4 muscarinic acetylcholine receptor (M4-mT4L) bound to tiotropium Deposited 2015-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–11（10 aa）
Chain B
61–161（101 aa）
|
Not recorded | 0HK (1R,2R,4S,5S,7S)-7-{[hydroxy(dithiophen-2-yl)acetyl]oxy}-9,9-dimethyl-3-oxa-9-azoniatricyclo[3.3.1.0~2,4~]nonane × 1 OLA OLEIC ACID × 2 P6G HEXAETHYLENE GLYCOL × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2 PG6 1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；Reconstituted in 10:1 monoolein:cholesterol mix. Precipitant solution: 20 - 40% PEG300, 100 mM MES, pH 5.5 - 7.5, and 10 - 150 mM EDTA, pH 8.0
|
Resolution 2.60 Å R-free 0.240 |
| 5DSG Structure of the M4 muscarinic acetylcholine receptor (M4-mT4L) bound to tiotropium Deposited 2015-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
2–11（10 aa）
Chain A
61–161（101 aa）
Chain B
2–11（10 aa）
Chain B
61–161（101 aa）
|
Not recorded | 0HK (1R,2R,4S,5S,7S)-7-{[hydroxy(dithiophen-2-yl)acetyl]oxy}-9,9-dimethyl-3-oxa-9-azoniatricyclo[3.3.1.0~2,4~]nonane × 2 OLA OLEIC ACID × 5 EDT {[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC ACID × 1 P6G HEXAETHYLENE GLYCOL × 2 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 5 PG6 1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；Reconstituted in 10:1 monoolein:cholesterol mix. Precipitant solution: 20 - 40% PEG300, 100 mM MES, pH 5.5 - 7.5, and 10 - 150 mM EDTA, pH 8.0
|
Resolution 2.60 Å R-free 0.240 |
| 5EE7 Crystal structure of the human glucagon receptor (GCGR) in complex with the antagonist MK-0893 Deposited 2015-10-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–160（160 aa）
|
Mutation：;G154A R173A A182L S190A G223A M276A E362F G207E K344A F387A V193F,G154A R173A A182L S190A G223A M276A E362F G207E K344A F387A V193F,G154A R173A A182L S190A G223A M276A E362F G207E K344A F387A V193F ; | 5MV 3-[[4-[(1~{S})-1-[3-[3,5-bis(chloranyl)phenyl]-5-(6-methoxynaphthalen-2-yl)pyrazol-1-yl]ethyl]phenyl]carbonylamino]propanoic acid × 1 OLA OLEIC ACID × 14 PE5 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL × 1 TLA L(+)-TARTARIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6；293.15 K；ADA BUFFER, SODIUM POTASSIUM TARTRATE, PEG 400
|
Resolution 2.50 Å R-free 0.263 |
| 5EUT Crystal structure of phosphatidyl inositol 4-kinase II alpha in the apo state Deposited 2015-11-19 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–163（162 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；291 K；12.5% w/v PEG 1000, 12.5% w/v PEG 3350, 12.5% v/v MPD, 0.1 M bicine/Trizma base pH 8.5
|
Resolution 2.80 Å R-free 0.289 |
| 5EWX Fusion protein of T4 lysozyme and B4 domain of protein A from staphylococcal aureus with chemical cross-linker EY-CBS Deposited 2015-11-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–35（35 aa）
Fragment：UNP RESIDUES 1-35, 219-266, 38-164
Chain A
38–164（127 aa）
Fragment：UNP RESIDUES 1-35, 219-266, 38-164
|
Mutation：A1212V, G1240A, E1258C, K1261A, L1262A, N40C, C54T, C97A, K162A Mutation：A1212V, G1240A, E1258C, K1261A, L1262A, N40C, C54T, C97A, K162A | EYC 2,2'-ethyne-1,2-diylbis{5-[(chloroacetyl)amino]benzenesulfonic acid} × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
EVAPORATION；pH 7.5；277 K；1.84M Na/K Phosphate, pH 7.5
|
Resolution 2.60 Å R-free 0.253 |
| 5EWX Fusion protein of T4 lysozyme and B4 domain of protein A from staphylococcal aureus with chemical cross-linker EY-CBS Deposited 2015-11-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–35（35 aa）
Fragment：UNP RESIDUES 1-35, 219-266, 38-164
Chain B
38–164（127 aa）
Fragment：UNP RESIDUES 1-35, 219-266, 38-164
|
Mutation：A1212V, G1240A, E1258C, K1261A, L1262A, N40C, C54T, C97A, K162A Mutation：A1212V, G1240A, E1258C, K1261A, L1262A, N40C, C54T, C97A, K162A | EYC 2,2'-ethyne-1,2-diylbis{5-[(chloroacetyl)amino]benzenesulfonic acid} × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
EVAPORATION；pH 7.5；277 K；1.84M Na/K Phosphate, pH 7.5
|
Resolution 2.60 Å R-free 0.253 |
| 5G27 Structure of Spin-labelled T4 lysozyme mutant L118C-R1 at Room Temperature Deposited 2016-04-07 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | MTN S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 CL CHLORIDE ION × 1 NA SODIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
PROTEIN WAS CRYSTALLIZED FROM 2.0 M K2HPO4/NAH2PO4, 250 MM NACL, 0.04 % AZIDE, 20 MM DITHIODIETHANOL, PH 7.2
|
Resolution 1.61 Å R-free 0.169 |
| 5JDT Structure of Spin-labelled T4 lysozyme mutant L118C-R1 at 100K Deposited 2016-04-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | MTN S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate × 1 CL CHLORIDE ION × 3 BME BETA-MERCAPTOETHANOL × 1 AZI AZIDE ION × 2 K POTASSIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；291 K；2.0 M NA/K PHOSPHATE, 240 mM NACL, 40 mM 2-HYDROXYETHYL DISULFIDE, PH 6.8
|
Resolution 1.00 Å R-free 0.130 |
| 5JEA Structure of a cytoplasmic 11-subunit RNA exosome complex including Ski7, bound to RNA Deposited 2016-04-18 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 11 PDB declaration: dodecameric |
Chain K
1–164（164 aa）
|
Not recorded | MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 7 NA SODIUM ION × 4 ZN ZINC ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6；293.15 K；27 % 2-Methyl-2,4-pentanediol (MPD), 0.1 M 2-(N-morpholino)ethanesulfonic acid (MES) pH 6 and 10 mM CaCl2.
|
Resolution 2.65 Å R-free 0.259 |
| 5JGN Spin-Labeled T4 Lysozyme Construct I9V1 Deposited 2016-04-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：I9C, C54T, C97A | CL CHLORIDE ION × 4 K POTASSIUM ION × 1 V1A S-(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-imidazol-4-yl) methanesulfonothioate × 1 PO4 PHOSPHATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；297 K；sodium/potassium phosphate, sodium chloride, hexane-1,6-diol, 2-propanol
|
Resolution 1.53 Å R-free 0.172 |
| 5JGR Spin-Labeled T4 Lysozyme Construct K43V1 Deposited 2016-04-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：K43C, C54T, C97A | V1A S-(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-imidazol-4-yl) methanesulfonothioate × 1 CL CHLORIDE ION × 3 PO4 PHOSPHATE ION × 1 K POTASSIUM ION × 1 HEZ HEXANE-1,6-DIOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.2；297 K；sodium/potassium phosphate, sodium chloride, hexane-1,6-diol, 2-propanol
|
Resolution 1.46 Å R-free 0.193 |
| 5JGU Spin-Labeled T4 Lysozyme Construct R119V1 Deposited 2016-04-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, R119C | PO4 PHOSPHATE ION × 1 CL CHLORIDE ION × 3 K POTASSIUM ION × 1 V1A S-(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-imidazol-4-yl) methanesulfonothioate × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；297 K；sodium/potassium phosphate, sodium chloride, hexane-1,6-diol, 2-propanol
|
Resolution 1.47 Å R-free 0.175 |
| 5JGV Spin-Labeled T4 Lysozyme Construct A73V1 Deposited 2016-04-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, A73C, C97A | CL CHLORIDE ION × 5 K POTASSIUM ION × 1 V1A S-(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-imidazol-4-yl) methanesulfonothioate × 1 HEZ HEXANE-1,6-DIOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；sodium/potassium phosphate, sodium chloride, hexane-1,6-diol, 2-propanol
|
Resolution 1.73 Å R-free 0.189 |
| 5JGX Spin-Labeled T4 Lysozyme Construct V131V1 Deposited 2016-04-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, V131C | CL CHLORIDE ION × 3 K POTASSIUM ION × 1 V1A S-(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-imidazol-4-yl) methanesulfonothioate × 1 PO4 PHOSPHATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；293 K；sodium/potassium phosphate, sodium chloride, hexane-1,6-diol, 2-propanol
|
Resolution 1.53 Å R-free 0.189 |
| 5JGZ Spin-Labeled T4 Lysozyme Construct T151V1 Deposited 2016-04-20 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T, C97A, T151C | CL CHLORIDE ION × 1 K POTASSIUM ION × 1 V1A S-(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-imidazol-4-yl) methanesulfonothioate × 1 PO4 PHOSPHATE ION × 1 HEZ HEXANE-1,6-DIOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；sodium/potassium phosphate, sodium chloride, hexane-1,6-diol, 2-propanol
|
Resolution 1.53 Å R-free 0.195 |
| 5JQH Structure of beta2 adrenoceptor bound to carazolol and inactive-state stabilizing nanobody, Nb60 Deposited 2016-05-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
Fragment：UNP RESIDUES 2-161, UNP RESIDEUS 30-348
|
Mutation：C919T, C962A, M1096T, M1098T, N1187E, C1265A,C919T, C962A, M1096T, M1098T, N1187E, C1265A | CAU (2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol × 1 CLR CHOLESTEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 7.5；293 K；100 mM HEPES pH 7.5, 20 mM EDTA, and 19-23% PEG300
|
Resolution 3.20 Å R-free 0.290 |
| 5JQH Structure of beta2 adrenoceptor bound to carazolol and inactive-state stabilizing nanobody, Nb60 Deposited 2016-05-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain B
2–161（160 aa）
Fragment：UNP RESIDUES 2-161, UNP RESIDEUS 30-348
|
Mutation：C919T, C962A, M1096T, M1098T, N1187E, C1265A,C919T, C962A, M1096T, M1098T, N1187E, C1265A | CAU (2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol × 1 CLR CHOLESTEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 7.5；293 K；100 mM HEPES pH 7.5, 20 mM EDTA, and 19-23% PEG300
|
Resolution 3.20 Å R-free 0.290 |
| 5JWS T4 Lysozyme L99A with 1-Hydro-2-ethyl-1,2-azaborine Bound Deposited 2016-05-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | 6OQ 2-ethyl-1,2-dihydro-1,2-azaborinine × 1 CL CHLORIDE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7；277.15 K；2.2 M sodium/potassium phosphate, pH 7.0, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.65 Å R-free 0.233 |
| 5JWT T4 Lysozyme L99A/M102Q with Benzene Bound Deposited 2016-05-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | BNZ BENZENE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；277.15 K；2.2 M sodium/potassium phosphate, pH 6.9, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.41 Å R-free 0.243 |
| 5JWU T4 Lysozyme L99A/M102Q with 1,2-Dihydro-1,2-azaborine Bound Deposited 2016-05-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | B20 1,2-dihydro-1,2-azaborinine × 1 CL CHLORIDE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277.15 K；2.1 M sodium/potassium phosphate, pH 7.0, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.70 Å R-free 0.251 |
| 5JWV T4 Lysozyme L99A/M102Q with Ethylbenzene Bound Deposited 2016-05-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | PYJ PHENYLETHANE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.1；277.15 K；2.2 M sodium/potassium phosphate, pH 7.1, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.30 Å R-free 0.203 |
| 5JWW T4 Lysozyme L99A/M102Q with 1-Hydro-2-ethyl-1,2-azaborine Bound Deposited 2016-05-12 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 1 6OQ 2-ethyl-1,2-dihydro-1,2-azaborinine × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；277.15 K；2.1 M sodium/potassium phosphate, pH 6.8, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.47 Å R-free 0.249 |
| 5KGR Spin-Labeled T4 Lysozyme Construct I9V1/V131V1 (30 days) Deposited 2016-06-13 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：I9C, C54T, C97A, V131C | V1A S-(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-imidazol-4-yl) methanesulfonothioate × 2 HEZ HEXANE-1,6-DIOL × 1 CL CHLORIDE ION × 3 K POTASSIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；2 M sodium/potassium phosphate, 150 mM sodium chloride, 100 mM 1,2-hexanediol, 3% 2-propanol
|
Resolution 1.47 Å R-free 0.189 |
| 5KHZ PSEUDO T4 LYSOZYME Deposited 2016-06-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；291.15 K；2.0M KPO4, 50MM 2-HYDROXYETHYLDISULFIDE, 50MM 2-MERCAPTOETHANOL, PH 6.9
|
Resolution 1.49 Å R-free 0.201 |
| 5KI1 PSEUDO T4 LYSOZYME MUTANT - Y18F Deposited 2016-06-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；291.15 K；2.4M KPO4, 50MM 2-HYDROXYETHYLDISULFIDE, 50MM 2-MERCAPTOETHANOL, PH 6.7
|
Resolution 1.46 Å R-free 0.207 |
| 5KI2 PSEUDO T4 LYSOZYME MUTANT - Y18PHE-METHYL Deposited 2016-06-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；291.15 K；2.2M KPO4, 50MM 2-HYDROXYETHYLDISULFIDE, 50MM 2-MERCAPTOETHANOL, PH 6.8
|
Resolution 1.50 Å R-free 0.221 |
| 5KI3 PSEUDO T4 LYSOZYME MUTANT - Y18PHE-BR Deposited 2016-06-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；291.15 K；2.0M KPO4, 50MM 2-HYDROXYETHYLDISULFIDE, 50MM 2-MERCAPTOETHANOL, PH 6.7
|
Resolution 1.65 Å R-free 0.250 |
| 5KI8 PSEUDO T4 LYSOZYME MUTANT - Y88PHE-BR Deposited 2016-06-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；291.15 K；2.4M KPO4, 50MM 2-HYDROXYETHYLDISULFIDE, 50MM 2-MERCAPTOETHANOL, PH 6.9
|
Resolution 1.55 Å R-free 0.210 |
| 5KIG PSEUDO T4 LYSOZYME MUTANT - Y88F Deposited 2016-06-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES | HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；291.15 K；2.0M KPO4, 50MM 2-HYDROXYETHYLDISULFIDE, 50MM 2-MERCAPTOETHANOL, PH6.9
|
Resolution 1.50 Å R-free 0.196 |
| 5KII PSEUDO T4 LYSOZYME MUTANT - Y88PHE-METHYL Deposited 2016-06-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | HED 2-HYDROXYETHYL DISULFIDE × 1 PO4 PHOSPHATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；291.15 K；2.0M KP04, 50mM 2-HYDROXYETHYLDISULFIDE, 50mM 2-MERCAPTOETHANOL, PH 6.9
|
Resolution 1.56 Å R-free 0.223 |
| 5KIM PSEUDO T4 LYSOZYME MUTANT - Y88PHE-I Deposited 2016-06-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | HED 2-HYDROXYETHYL DISULFIDE × 1 NA SODIUM ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.9；291.15 K；2.0M KPO4, 50mM 2-HYDROXYETHYLDISULFID, 50mM 2-MERCAPTOETHANOL, PH6.9
|
Resolution 1.50 Å R-free 0.184 |
| 5KIO PSEUDO T4 LYSOZYME MUTANT - Y18PHE-I Deposited 2016-06-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.7；291.15 K；2.0M KPO4, 50MM 2-HYDROXYETHYLDISULFIDE, 50MM 2-MERCAPTOETHANOL, PH 6.7
|
Resolution 1.63 Å R-free 0.237 |
| 5LWO Structure of Spin-labelled T4 lysozyme mutant L115C-R119C-R1 at 100K Deposited 2016-09-18 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：C54T C97A L118C T115C R119C | RXR [2,2,5,5-tetramethyl-3,4-bis(sulfanylmethyl)-2,5-dihydro-1H-pyrrol-1-yl]oxidanyl radical × 1 CL CHLORIDE ION × 4 HED 2-HYDROXYETHYL DISULFIDE × 1 PO4 PHOSPHATE ION × 1 BME BETA-MERCAPTOETHANOL × 1 K POTASSIUM ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.8；293 K；2.0 M NA/K PHOSPHATE, 240 mM NACL, 40 mM 2-HYDROXYETHYL DISULFIDE, PH 6.8
|
Resolution 1.18 Å R-free 0.164 |
| 5LZM COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS Deposited 1991-01-25 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 3 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 5T04 STRUCTURE OF CONSTITUTIVELY ACTIVE NEUROTENSIN RECEPTOR Deposited 2016-08-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
Fragment：unp residues 43-268; 2-161; 297-396,unp residues 43-268; 2-161; 297-396,unp residues 43-268; 2-161; 297-396
|
Mutation：;A86L, G215A, F358A, V360A, R12G, C54T, C97A, Q122N, Q123N, I137R,A86L, G215A, F358A, V360A, R12G, C54T, C97A, Q122N, Q123N, I137R,A86L, G215A, F358A, V360A, R12G, C54T, C97A, Q122N, Q123N, I137R ; | TCE 3,3',3''-phosphanetriyltripropanoic acid × 1 GOL GLYCEROL × 1 PEG DI(HYDROXYETHYL)ETHER × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；13-16% (v/v) PEG 400,
80 mM TrisHCl pH 8.5-9.0,
1.9 mM TCEP,
68-91 mM lithium acetate,
0.9 mM Neurotensin
|
Resolution 3.30 Å R-free 0.283 |
| 5TZR GPR40 in complex with partial agonist MK-8666 Deposited 2016-11-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：L42A, F88A, G103A, Y202F, R1012G, C1054T, C1097A, I1137R | NA SODIUM ION × 1 MK6 (5aR,6S,6aS)-3-({2',6'-dimethyl-4'-[3-(methylsulfonyl)propoxy][1,1'-biphenyl]-3-yl}methoxy)-5,5a,6,6a-tetrahydrocyclopropa[4,5]cyclopenta[1,2-c]pyridine-6-carboxylic acid × 1 MLI MALONATE ION × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 1PE PENTAETHYLENE GLYCOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 7.7；293 K；25-28%PEG 400, 0.2M sodium malonate, 0.1M Tris pH7.7
|
Resolution 2.20 Å R-free 0.228 |
| 5TZY GPR40 in complex with AgoPAM AP8 and partial agonist MK-8666 Deposited 2016-11-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：;L42A, G103A, Y202F, R1012G, C1054T, C1097A, I1137R,L42A, G103A, Y202F, R1012G, C1054T, C1097A, I1137R,L42A, G103A, Y202F, R1012G, C1054T, C1097A, I1137R ; | OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 1 MK6 (5aR,6S,6aS)-3-({2',6'-dimethyl-4'-[3-(methylsulfonyl)propoxy][1,1'-biphenyl]-3-yl}methoxy)-5,5a,6,6a-tetrahydrocyclopropa[4,5]cyclopenta[1,2-c]pyridine-6-carboxylic acid × 1 7OS (2S,3R)-3-cyclopropyl-3-[(2R)-2-(1-{(1S)-1-[5-fluoro-2-(trifluoromethoxy)phenyl]ethyl}piperidin-4-yl)-3,4-dihydro-2H-1-benzopyran-7-yl]-2-methylpropanoic acid × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6.5；293 K；22% PEG 400, 0.37M potassium nitrate, 0.1M MES pH6.5
|
Resolution 3.22 Å R-free 0.287 |
| 5VEW Structure of the human GLP-1 receptor complex with PF-06372222 Deposited 2017-04-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) | 97Y N-{4-[(R)-(3,3-dimethylcyclobutyl)({6-[4-(trifluoromethyl)-1H-imidazol-1-yl]pyridin-3-yl}amino)methyl]benzene-1-carbonyl}-beta-alanine × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2 OLA OLEIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；0.4-0.45 M ammonium acetate, 0.1 M sodium cacodylate, pH 6.2-6.6, 35-38% PEG400, 3% w/v aminohexanoic acid
|
Resolution 2.70 Å R-free 0.246 |
| 5VEW Structure of the human GLP-1 receptor complex with PF-06372222 Deposited 2017-04-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–161（160 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) | 97Y N-{4-[(R)-(3,3-dimethylcyclobutyl)({6-[4-(trifluoromethyl)-1H-imidazol-1-yl]pyridin-3-yl}amino)methyl]benzene-1-carbonyl}-beta-alanine × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；0.4-0.45 M ammonium acetate, 0.1 M sodium cacodylate, pH 6.2-6.6, 35-38% PEG400, 3% w/v aminohexanoic acid
|
Resolution 2.70 Å R-free 0.246 |
| 5VEX Structure of the human GLP-1 receptor complex with NNC0640 Deposited 2017-04-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) | 97V 4-{[(4-cyclohexylphenyl){[3-(methylsulfonyl)phenyl]carbamoyl}amino]methyl}-N-(1H-tetrazol-5-yl)benzamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；0.4-0.45 M ammonium acetate, 0.1 M sodium acetate, pH 5.0-5.8, 38-40% PEG400
|
Resolution 3.00 Å R-free 0.256 |
| 5VEX Structure of the human GLP-1 receptor complex with NNC0640 Deposited 2017-04-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–161（160 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) | 97V 4-{[(4-cyclohexylphenyl){[3-(methylsulfonyl)phenyl]carbamoyl}amino]methyl}-N-(1H-tetrazol-5-yl)benzamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；0.4-0.45 M ammonium acetate, 0.1 M sodium acetate, pH 5.0-5.8, 38-40% PEG400
|
Resolution 3.00 Å R-free 0.256 |
| 5WF5 Agonist bound human A2a adenosine receptor with D52N mutation at 2.60 A resolution Deposited 2017-07-11 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：R1012G C1054T C1097A I1137R | UKA 6-(2,2-diphenylethylamino)-9-[(2R,3R,4S,5S)-5-(ethylcarbamoyl)-3,4-dihydroxy-oxolan-2-yl]-N-[2-[(1-pyridin-2-ylpiperidin-4-yl)carbamoylamino]ethyl]purine-2-carboxamide × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；296 K；100 mM sodium citrate pH 5, 24-27% (v/v)
polyethylene glycol (PEG) 400, 30-80 mM MgCl 2 , 5% (v/v) Jeffamine M-600 pH 7 (Hampton)
|
Resolution 2.60 Å R-free 0.251 |
| 5WF6 Agonist bound human A2a adenosine receptor with S91A mutation at 2.90 A resolution Deposited 2017-07-11 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：R1012G, C1054T, C1097A, I1137R | UKA 6-(2,2-diphenylethylamino)-9-[(2R,3R,4S,5S)-5-(ethylcarbamoyl)-3,4-dihydroxy-oxolan-2-yl]-N-[2-[(1-pyridin-2-ylpiperidin-4-yl)carbamoylamino]ethyl]purine-2-carboxamide × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；100 mM sodium citrate pH 5, 24-27% (v/v)
polyethylene glycol (PEG) 400, 30-80 mM MgCl 2 , 5% (v/v) Jeffamine M-600 pH 7 (Hampton)
|
Resolution 2.90 Å R-free 0.288 |
| 5X93 Human endothelin receptor type-B in complex with antagonist K-8794 Deposited 2017-03-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
61–161（101 aa）
|
Mutation：R124Y,D154A,K270A,C1054A,I1094R,S342A,I381A,C396A,C400A,C405A | K87 3-[6-[(4-tert-butylphenyl)sulfonylamino]-5-(2-methoxyphenoxy)-2-pyrimidin-2-yl-pyrimidin-4-yl]oxy-N-(2,6-dimethylphenyl)propanamide × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 11 CLR CHOLESTEROL × 1 SO4 SULFATE ION × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6；293 K；PEG 500 DME, (NH4)2SO4, MOPS
|
Resolution 2.20 Å R-free 0.239 |
| 5XPR Human endothelin receptor type-B in complex with antagonist bosentan Deposited 2017-06-04 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
61–161（101 aa）
|
Mutation：R124Y,K270A,C1054A,I1094R,S342A,I381A,C396A,C400A,C405A | K86 4-tert-butyl-N-[6-(2-hydroxyethyloxy)-5-(2-methoxyphenoxy)-2-pyrimidin-2-yl-pyrimidin-4-yl]benzenesulfonamide × 1 SO4 SULFATE ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6；293 K；PEG 500 DME, Na2SO4, MOPS
|
Resolution 3.60 Å R-free 0.297 |
| 5XSZ Crystal structure of zebrafish lysophosphatidic acid receptor LPA6 Deposited 2017-06-16 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：E1011N,R1012G,D1020N,C1054T,C1097A,I1137R | OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6；298 K；MES, PEG 400, NaH2PO4, 1,4-butanediol
|
Resolution 3.20 Å R-free 0.263 |
| 5YQR Crystal structure of the PH-like domain of Lam6 Deposited 2017-11-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：R12G,D20N, C54T, C97A, I137R | 2PE NONAETHYLENE GLYCOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；0.1M HEPES-HCl pH 7.0, 10% PEG8000, 0.1M Na3Citrate
|
Resolution 2.40 Å R-free 0.266 |
| 5ZKQ Crystal structure of the human platelet-activating factor receptor in complex with ABT-491 Deposited 2018-03-25 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
2–11（10 aa）
Chain A
61–161（101 aa）
Chain B
2–11（10 aa）
Chain B
61–161（101 aa）
|
Mutation：F116Y, N169D, A230D,C97A, I137R, A230D, V234A, D289N Mutation：F116Y, N169D, A230D,C97A, I137R, A230D, V234A, D289N Mutation：F116Y, N169D, A230D,C97A, I137R, A230D, V234A, D289N Mutation：F116Y, N169D, A230D,C97A, I137R, A230D, V234A, D289N | 9EU 4-ethynyl-3-{3-fluoro-4-[(2-methyl-1H-imidazo[4,5-c]pyridin-1-yl)methyl]benzene-1-carbonyl}-N,N-dimethyl-1H-indole-1-carboxamide × 2 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 7 ZN ZINC ION × 2 SO4 SULFATE ION × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；HEPES, PEG 400, MgSO4
|
Resolution 2.90 Å R-free 0.235 |
| 6BG3 Structure of (3S,4S)-1-benzyl-4-(3-(3-(trifluoromethyl)phenyl)ureido)piperidin-3-yl acetate bound to DCN1 Deposited 2017-10-27 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
Fragment：PONY
|
Not recorded | DOJ N-{(3S,4S)-1-benzyl-3-[(1S)-1-hydroxyethoxy]piperidin-4-yl}-N'-[3-(trifluoromethyl)phenyl]urea × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
EVAPORATION；277 K；6% PEG3350, 0.2M NH4Br
|
Resolution 1.05 Å R-free 0.173 |
| 6BG5 Structure of 1-(benzo[d][1,3]dioxol-5-ylmethyl)-1-(1-propylpiperidin-4-yl)-3-(3-(trifluoromethyl)phenyl)urea bound to DCN1 Deposited 2017-10-27 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
Fragment：PONY
|
Not recorded | DQD N-[(2H-1,3-benzodioxol-5-yl)methyl]-N-(1-propylpiperidin-4-yl)-N'-[3-(trifluoromethyl)phenyl]urea × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
EVAPORATION；277 K；6% PEG3350, 0.2M NH4Br
|
Resolution 1.10 Å R-free 0.172 |
| 6FFH Crystal Structure of mGluR5 in complex with Fenobam at 2.65 A Deposited 2018-01-08 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
Fragment：MGLUR5
|
Mutation：C54T C97A E579A N667Y I669A G675M T742A S753A Non-standard monomer：Yes (specific site not provided by mmCIF) | OLA OLEIC ACID × 5 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 D7W 1-(3-chlorophenyl)-3-(3-methyl-5-oxidanylidene-4~{H}-imidazol-2-yl)urea × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6.8；293.1 K；24-34% V/V PEG400, 0.2 M AMMONIUM PHOSPHATE DIBASIC, 0.1 M MES, PH 6.8
|
Resolution 2.65 Å R-free 0.267 |
| 6FFI Crystal Structure of mGluR5 in complex with MMPEP at 2.2 A Deposited 2018-01-08 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–162（161 aa）
Fragment：MGLUR5,MGLUR5,MGLUR5,MGLUR5,MGLUR5,MGLUR5,MGLUR5,MGLUR5,MGLUR5
|
Mutation：;E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A ; Non-standard monomer：Yes (specific site not provided by mmCIF) | OLA OLEIC ACID × 7 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 D8B 2-[2-(3-methoxyphenyl)ethynyl]-6-methyl-pyridine × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 6.8；293.1 K；24-34% V/V PEG400, 0.2 M AMMONIUM PHOSPHATE DIBASIC, 0.1 M MES, PH 6.8
|
Resolution 2.20 Å R-free 0.269 |
| 6IIH crystal structure of mitochondrial calcium uptake 2(MICU2) Deposited 2018-10-06 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–161（161 aa）
Chain B
1–161（161 aa）
|
Mutation：C54T, C97A Mutation：C54T, C97A | CA CALCIUM ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5.16；293 K；100 mM Sodium phosphate monobasic , 100 mM potassium phosphate monobasic , 100 mM MES, 6.0 and 1M sodium chloride
|
Resolution 1.96 Å R-free 0.227 |
| 6K1Q Human endothelin receptor type-B in complex with inverse agonist IRL2500 Deposited 2019-05-11 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
61–161（101 aa）
|
Mutation：;R124Y, K270A,C97A, I137R,S342A, I381A, C396A, C400A, C405A,R124Y, K270A,C97A, I137R,S342A, I381A, C396A, C400A, C405A,R124Y, K270A,C97A, I137R,S342A, I381A, C396A, C400A, C405A ; | D2U (2~{S})-2-[[(2~{R})-2-[(3,5-dimethylphenyl)carbonyl-methyl-amino]-3-(4-phenylphenyl)propanoyl]amino]-3-(1~{H}-indol-3-yl)propanoic acid × 1 PO4 PHOSPHATE ION × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 7.5；293 K；30% PEG300, 150 mM NaH2PO4,10 mM TCEP, 100 mM Bis-tris
|
Resolution 2.70 Å R-free 0.265 |
| 6KJV Structure of thermal-stabilised(M9) human GLP-1 receptor transmembrane domain Deposited 2019-07-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：S193C,I196F,S225A,S271A,I317C,G318I,K346A,C347F,G361C,205-214deletion,R1011G,C1053T,C1096A,I1136R | 97Y N-{4-[(R)-(3,3-dimethylcyclobutyl)({6-[4-(trifluoromethyl)-1H-imidazol-1-yl]pyridin-3-yl}amino)methyl]benzene-1-carbonyl}-beta-alanine × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；0.4-0.45 M ammonium acetate, 0.1 M sodium cacodylate, pH 6.2-6.6, 35-38% PEG400, 3% w/v aminohexanoic acid
|
Resolution 2.80 Å R-free 0.280 |
| 6KJV Structure of thermal-stabilised(M9) human GLP-1 receptor transmembrane domain Deposited 2019-07-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–161（160 aa）
|
Mutation：S193C,I196F,S225A,S271A,I317C,G318I,K346A,C347F,G361C,205-214deletion,R1011G,C1053T,C1096A,I1136R | 97Y N-{4-[(R)-(3,3-dimethylcyclobutyl)({6-[4-(trifluoromethyl)-1H-imidazol-1-yl]pyridin-3-yl}amino)methyl]benzene-1-carbonyl}-beta-alanine × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；0.4-0.45 M ammonium acetate, 0.1 M sodium cacodylate, pH 6.2-6.6, 35-38% PEG400, 3% w/v aminohexanoic acid
|
Resolution 2.80 Å R-free 0.280 |
| 6KK1 Structure of thermal-stabilised(M8) human GLP-1 receptor transmembrane domain Deposited 2019-07-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：;I196F,S225A,S271A,I317C,G318I,K346A,C347F,G361C,205-214deletion,R1011G,C1053T,C1096A,I1136R,I196F,S225A,S271A,I317C,G318I,K346A,C347F,G361C,205-214deletion ; | 97Y N-{4-[(R)-(3,3-dimethylcyclobutyl)({6-[4-(trifluoromethyl)-1H-imidazol-1-yl]pyridin-3-yl}amino)methyl]benzene-1-carbonyl}-beta-alanine × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；0.4-0.45 M ammonium acetate, 0.1 M sodium cacodylate, pH 6.2-6.6, 35-38% PEG400, 3% w/v aminohexanoic acid
|
Resolution 2.80 Å R-free 0.290 |
| 6KK1 Structure of thermal-stabilised(M8) human GLP-1 receptor transmembrane domain Deposited 2019-07-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–161（160 aa）
|
Mutation：;I196F,S225A,S271A,I317C,G318I,K346A,C347F,G361C,205-214deletion,R1011G,C1053T,C1096A,I1136R,I196F,S225A,S271A,I317C,G318I,K346A,C347F,G361C,205-214deletion ; | 97Y N-{4-[(R)-(3,3-dimethylcyclobutyl)({6-[4-(trifluoromethyl)-1H-imidazol-1-yl]pyridin-3-yl}amino)methyl]benzene-1-carbonyl}-beta-alanine × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；0.4-0.45 M ammonium acetate, 0.1 M sodium cacodylate, pH 6.2-6.6, 35-38% PEG400, 3% w/v aminohexanoic acid
|
Resolution 2.80 Å R-free 0.290 |
| 6KK7 Structure of thermal-stabilised(M6) human GLP-1 receptor transmembrane domain Deposited 2019-07-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：S225A,I317C,G318I,K346A,C347F,G361C,205-214deletion,R1011G,C1053T,C1096A,I1136R | 97Y N-{4-[(R)-(3,3-dimethylcyclobutyl)({6-[4-(trifluoromethyl)-1H-imidazol-1-yl]pyridin-3-yl}amino)methyl]benzene-1-carbonyl}-beta-alanine × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；0.4-0.45 M ammonium acetate, 0.1 M sodium cacodylate, pH 6.2-6.6, 35-38% PEG400, 3% w/v aminohexanoic acid
|
Resolution 3.10 Å R-free 0.303 |
| 6KK7 Structure of thermal-stabilised(M6) human GLP-1 receptor transmembrane domain Deposited 2019-07-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–161（160 aa）
|
Mutation：S225A,I317C,G318I,K346A,C347F,G361C,205-214deletion,R1011G,C1053T,C1096A,I1136R | 97Y N-{4-[(R)-(3,3-dimethylcyclobutyl)({6-[4-(trifluoromethyl)-1H-imidazol-1-yl]pyridin-3-yl}amino)methyl]benzene-1-carbonyl}-beta-alanine × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；0.4-0.45 M ammonium acetate, 0.1 M sodium cacodylate, pH 6.2-6.6, 35-38% PEG400, 3% w/v aminohexanoic acid
|
Resolution 3.10 Å R-free 0.303 |
| 6LZM COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS Deposited 1991-01-25 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 BME BETA-MERCAPTOETHANOL × 3 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 6M9T Crystal structure of EP3 receptor bound to misoprostol-FA Deposited 2018-08-24 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
Fragment：EP3 UNP residues 2-259,273-353 with intervening lysozyme
|
Not recorded | J9P (11alpha,12alpha,13E,16S)-11,16-dihydroxy-16-methyl-9-oxoprost-13-en-1-oic acid × 1 SO4 SULFATE ION × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 1 OLA OLEIC ACID × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；100 mM sodium citrate, pH 3.8-4.2, 10-35 mM magnesium sulfate, 20-23% v/v PEG400, 2.5% Jeffamine M-600
|
Resolution 2.50 Å R-free 0.242 |
| 6QAJ Structure of the tripartite motif of KAP1/TRIM28 Deposited 2018-12-19 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
Chain B
2–161（160 aa）
|
Not recorded | ZN ZINC ION × 8 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；15% (w/v) PEG 3350, 75 mM MgCl2, 0.1 M HEPES pH 7.5
|
Resolution 2.90 Å R-free 0.291 |
| 6WSK Crystal Structure of the Cannabinoid Receptor 1 Interacting Protein 1a (CRIP1a) Deposited 2020-05-01 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–161（161 aa）
|
Mutation：E11Q, D20N, C54T, C97A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；30 mg/mL, 0.1 M sodium citrate (pH 4-5.5), and 0.3-0.6 ammonium sulfate
|
Resolution 1.55 Å R-free 0.225 |
| 6XYR Structure of the T4Lnano fusion protein Deposited 2020-01-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–164（163 aa）
|
Not recorded | CA CALCIUM ION × 5 GOL GLYCEROL × 5 CL CHLORIDE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293.15 K；8% PEG 8000, 200 mM LiCl2, 100 mM Tris pH 8.0, 15% Glycerol
|
Resolution 2.08 Å R-free 0.236 |
| 6ZFZ Structure of M1-StaR-T4L in complex with 77-LH-28-1 at 2.17A Deposited 2020-06-18 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：F27A,T32A,V46L,L64A,T95A,W101A,S112A,A143L,A196T,K362A,A364L,S411A | QJT 1-[3-(4-butylpiperidin-1-yl)propyl]-3,4-dihydroquinolin-2-one × 1 OLA OLEIC ACID × 8 PO4 PHOSPHATE ION × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 PGE TRIETHYLENE GLYCOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；0.1M NaHEPES pH 7.4-7.8, 0.1M di-ammonium hydrogenphosphate, 30-38% PEG300
|
Resolution 2.17 Å R-free 0.242 |
| 6ZG4 Structure of M1-StaR-T4L in complex with HTL0009936 at 2.35A Deposited 2020-06-18 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：F27A,T32A,V46L,L64A,T95A,W101A,S112A,A143L,A196T,K362A,A364L,S411A | QK8 ethyl (4~{S})-4-[4-[(1-methylcyclobutyl)carbamoyl]piperidin-1-yl]azepane-1-carboxylate × 1 OLA OLEIC ACID × 11 PGE TRIETHYLENE GLYCOL × 1 PO4 PHOSPHATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；0.1M NaHEPES pH 7.4-7.8, 0.1M di-Ammonium hydrogenphosphate, 30-38% PEG300
|
Resolution 2.33 Å R-free 0.234 |
| 6ZG9 Structure of M1-StaR-T4L in complex with GSK1034702 at 2.5A Deposited 2020-06-18 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：F27A,T32A,V46L,L64A,T95A,W101A,S112A,A143L,A196T,K362A,A364L,S411A | QK2 7-fluoranyl-5-methyl-3-[1-(oxan-4-yl)piperidin-4-yl]-1~{H}-benzimidazol-2-one × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 OLA OLEIC ACID × 6 PO4 PHOSPHATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；0.1 NaHEPES pH 7.4-7.8, 0.1M di-ammonium hydrogenohosphate, 30-38% PEG300
|
Resolution 2.50 Å R-free 0.242 |
| 6ZX9 Crystal structure of SIV Vpr,fused to T4 lysozyme, isolated from moustached monkey, bound to human DDB1 and human DCAF1 (amino acid residues 1046-1396) Deposited 2020-07-29 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric |
Chain C
2–164（163 aa）
|
Not recorded | GOL GLYCEROL × 8 ZN ZINC ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；277.15 K；8-10% PEG 4000 (w/v), 200 mM MgCl2, 100 mM HEPES-NaOH, pH 7.0-8.2.
|
Resolution 2.52 Å R-free 0.260 |
| 7F8U Crystal structure of the cholecystokinin receptor CCKAR in complex with lintitript Deposited 2021-07-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Not recorded | 1OE 2-[2-[[4-(2-chlorophenyl)-1,3-thiazol-2-yl]carbamoyl]indol-1-yl]ethanoic acid × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；0.1 M HEPES, pH7.5, 25% PEG400, 250 mM sodium tartrate ,1% 1,2 -butanediol
|
Resolution 2.80 Å R-free 0.253 |
| 7F8X Crystal structure of the cholecystokinin receptor CCKAR in complex with NN9056 Deposited 2021-07-02 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
|
Mutation：F130W,C1251G,C1336A,C1293T,I1376R | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；100 mM HEPES,7.5, 10 (v/v) PPG400 and 100 mM ammonium acetate
|
Resolution 3.00 Å R-free 0.261 |
| 7F8Y Crystal structure of the cholecystokinin receptor CCKAR in complex with devazepide Deposited 2021-07-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：D87N,F130W,R1251G,G1293T,C1336A,I385R | 1OZ N-[(3S)-1-methyl-2-oxidanylidene-5-phenyl-3H-1,4-benzodiazepin-3-yl]-1H-indole-2-carboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；0.1 M HEPES, pH 7.5, 25% (v/v) PEG400 and 350 mM ammonium acetate
|
Resolution 2.50 Å R-free 0.268 |
| 7L37 T4 Lysozyme L99A - Apo - RT Deposited 2020-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R12G/I137R/L99A | TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 CL CHLORIDE ION × 1 BME BETA-MERCAPTOETHANOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291 K；Crystals were grown from a 10 mg/mL frozen protein solution by the hanging drop method at 291-293K, with a 1:1 drop ratio of protein to solution and over a well solution of 0.1 M Tris-hydrochloride (pH 8), 20%-26% (w/v) PEG 4000, 70-170 mM lithium citrate, 8%-18% 2-propanol, 50 mM 2-mercaptoethanol, and 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.44 Å R-free 0.184 |
| 7L38 T4 Lysozyme L99A - Apo - cryo Deposited 2020-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R12G/I137R/L99A | TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 BME BETA-MERCAPTOETHANOL × 2 CL CHLORIDE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291 K；Crystals were grown from a 10 mg/mL frozen protein solution by the hanging drop method at 291-293K, with a 1:1 drop ratio of protein to solution and over a well solution of 0.1 M Tris-hydrochloride (pH 8), 20%-26% (w/v) PEG 4000, 70-170 mM lithium citrate, 8%-18% 2-propanol, 50 mM 2-mercaptoethanol, and 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.33 Å R-free 0.200 |
| 7L39 T4 Lysozyme L99A - toluene - RT Deposited 2020-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R12G/I137R/L99A | TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 CL CHLORIDE ION × 1 MBN TOLUENE × 1 BME BETA-MERCAPTOETHANOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291 K；Crystals were grown from a 10 mg/mL frozen protein solution by the hanging drop method at 291-293K, with a 1:1 drop ratio of protein to solution and over a well solution of 0.1 M Tris-hydrochloride (pH 8), 20%-26% (w/v) PEG 4000, 70-170 mM lithium citrate, 8%-18% 2-propanol, 50 mM 2-mercaptoethanol, and 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.35 Å R-free 0.167 |
| 7L3A T4 Lysozyme L99A - toluene - cryo Deposited 2020-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R12G/I137R/L99A | MBN TOLUENE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291 K；Crystals were grown from a 10 mg/mL frozen protein solution by the hanging drop method at 291-293K, with a 1:1 drop ratio of protein to solution and over a well solution of 0.1 M Tris-hydrochloride (pH 8), 20%-26% (w/v) PEG 4000, 70-170 mM lithium citrate, 8%-18% 2-propanol, 50 mM 2-mercaptoethanol, and 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.11 Å R-free 0.203 |
| 7L3B T4 Lysozyme L99A - iodobenzene - RT Deposited 2020-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R12G/I137R/L99A | TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 BME BETA-MERCAPTOETHANOL × 2 CL CHLORIDE ION × 1 PIH iodobenzene × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291 K；Crystals were grown from a 10 mg/mL frozen protein solution by the hanging drop method at 291-293K, with a 1:1 drop ratio of protein to solution and over a well solution of 0.1 M Tris-hydrochloride (pH 8), 20%-26% (w/v) PEG 4000, 70-170 mM lithium citrate, 8%-18% 2-propanol, 50 mM 2-mercaptoethanol, and 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.27 Å R-free 0.167 |
| 7L3C T4 Lysozyme L99A - o-xylene - RT Deposited 2020-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R12G/I137R/L99A | TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 CL CHLORIDE ION × 1 BME BETA-MERCAPTOETHANOL × 1 OXE ORTHO-XYLENE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291 K；Crystals were grown from a 10 mg/mL frozen protein solution by the hanging drop method at 291-293K, with a 1:1 drop ratio of protein to solution and over a well solution of 0.1 M Tris-hydrochloride (pH 8), 20%-26% (w/v) PEG 4000, 70-170 mM lithium citrate, 8%-18% 2-propanol, 50 mM 2-mercaptoethanol, and 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.31 Å R-free 0.177 |
| 7L3D T4 Lysozyme L99A - 3-iodotoluene - RT Deposited 2020-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R12G/I137R/L99A | TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 BME BETA-MERCAPTOETHANOL × 2 CL CHLORIDE ION × 1 XQJ 1-iodo-3-methylbenzene × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291 K；Crystals were grown from a 10 mg/mL frozen protein solution by the hanging drop method at 291-293K, with a 1:1 drop ratio of protein to solution and over a well solution of 0.1 M Tris-hydrochloride (pH 8), 20%-26% (w/v) PEG 4000, 70-170 mM lithium citrate, 8%-18% 2-propanol, 50 mM 2-mercaptoethanol, and 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.35 Å R-free 0.162 |
| 7L3E T4 Lysozyme L99A - 3-iodotoluene - cryo Deposited 2020-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R12G/I137R/L99A | TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 BME BETA-MERCAPTOETHANOL × 1 CL CHLORIDE ION × 1 XQJ 1-iodo-3-methylbenzene × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291 K；Crystals were grown from a 10 mg/mL frozen protein solution by the hanging drop method at 291-293K, with a 1:1 drop ratio of protein to solution and over a well solution of 0.1 M Tris-hydrochloride (pH 8), 20%-26% (w/v) PEG 4000, 70-170 mM lithium citrate, 8%-18% 2-propanol, 50 mM 2-mercaptoethanol, and 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.13 Å R-free 0.153 |
| 7L3F T4 Lysozyme L99A - 4-iodotoluene - RT Deposited 2020-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R12G/I137R/L99A | TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 CL CHLORIDE ION × 1 XQM 1-iodo-4-methylbenzene × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291 K；Crystals were grown from a 10 mg/mL frozen protein solution by the hanging drop method at 291-293K, with a 1:1 drop ratio of protein to solution and over a well solution of 0.1 M Tris-hydrochloride (pH 8), 20%-26% (w/v) PEG 4000, 70-170 mM lithium citrate, 8%-18% 2-propanol, 50 mM 2-mercaptoethanol, and 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.49 Å R-free 0.170 |
| 7L3G T4 Lysozyme L99A - 4-iodotoluene - cryo Deposited 2020-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R12G/I137R/L99A | TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 BME BETA-MERCAPTOETHANOL × 1 CA CALCIUM ION × 1 XQM 1-iodo-4-methylbenzene × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291 K；Crystals were grown from a 10 mg/mL frozen protein solution by the hanging drop method at 291-293K, with a 1:1 drop ratio of protein to solution and over a well solution of 0.1 M Tris-hydrochloride (pH 8), 20%-26% (w/v) PEG 4000, 70-170 mM lithium citrate, 8%-18% 2-propanol, 50 mM 2-mercaptoethanol, and 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.27 Å R-free 0.174 |
| 7L3H T4 Lysozyme L99A - ethylbenzene - RT Deposited 2020-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R12G/I137R/L99A | TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 BME BETA-MERCAPTOETHANOL × 1 CL CHLORIDE ION × 1 PYJ PHENYLETHANE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291 K；Crystals were grown from a 10 mg/mL frozen protein solution by the hanging drop method at 291-293K, with a 1:1 drop ratio of protein to solution and over a well solution of 0.1 M Tris-hydrochloride (pH 8), 20%-26% (w/v) PEG 4000, 70-170 mM lithium citrate, 8%-18% 2-propanol, 50 mM 2-mercaptoethanol, and 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.39 Å R-free 0.172 |
| 7L3I T4 Lysozyme L99A - propylbenzene - RT Deposited 2020-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R12G/I137R/L99A | TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 CL CHLORIDE ION × 1 3H0 propylbenzene × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291 K；Crystals were grown from a 10 mg/mL frozen protein solution by the hanging drop method at 291-293K, with a 1:1 drop ratio of protein to solution and over a well solution of 0.1 M Tris-hydrochloride (pH 8), 20%-26% (w/v) PEG 4000, 70-170 mM lithium citrate, 8%-18% 2-propanol, 50 mM 2-mercaptoethanol, and 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.46 Å R-free 0.168 |
| 7L3J T4 Lysozyme L99A - benzylacetate - RT Deposited 2020-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R12G/I137R/L99A | TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 BME BETA-MERCAPTOETHANOL × 1 CL CHLORIDE ION × 1 J0Z benzyl acetate × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291 K；Crystals were grown from a 10 mg/mL frozen protein solution by the hanging drop method at 291-293K, with a 1:1 drop ratio of protein to solution and over a well solution of 0.1 M Tris-hydrochloride (pH 8), 20%-26% (w/v) PEG 4000, 70-170 mM lithium citrate, 8%-18% 2-propanol, 50 mM 2-mercaptoethanol, and 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.49 Å R-free 0.173 |
| 7L3K T4 Lysozyme L99A - benzylacetate - cryo Deposited 2020-12-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Mutation：R12G/I137R/L99A | TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 BME BETA-MERCAPTOETHANOL × 1 CL CHLORIDE ION × 1 J0Z benzyl acetate × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291 K；Crystals were grown from a 10 mg/mL frozen protein solution by the hanging drop method at 291-293K, with a 1:1 drop ratio of protein to solution and over a well solution of 0.1 M Tris-hydrochloride (pH 8), 20%-26% (w/v) PEG 4000, 70-170 mM lithium citrate, 8%-18% 2-propanol, 50 mM 2-mercaptoethanol, and 50 mM 2-hydroxyethyl disulfide
|
Resolution 1.11 Å R-free 0.167 |
| 7LZM COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS Deposited 1991-01-25 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | CL CHLORIDE ION × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å |
| 7MI3 Signal subtracted reconstruction of AAA2, AAA3, and AAA4 domains of dynein in the presence of a pyrazolo-pyrimidinone-based compound, Model 4 Deposited 2021-04-16 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Not recorded | ZG7 (8S)-6-(3-bromophenoxy)-2-[1-(4-chlorophenyl)cyclopropyl]-7-hydroxypyrazolo[1,5-a]pyrimidine-3-carbonitrile × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.50 Å |
| 7MI6 Yeast dynein motor domain in the presence of a pyrazolo-pyrimidinone-based compound, Model 1 Deposited 2021-04-16 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：E1849Q | ZG7 (8S)-6-(3-bromophenoxy)-2-[1-(4-chlorophenyl)cyclopropyl]-7-hydroxypyrazolo[1,5-a]pyrimidine-3-carbonitrile × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.90 Å |
| 7MI8 Signal subtracted reconstruction of AAA5 and AAA6 domains of dynein in the presence of a pyrazolo-pyrimidinone-based compound, Model 5 Deposited 2021-04-16 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.70 Å |
| 7P2L thermostabilised 7TM domain of human mGlu5 receptor bound to photoswitchable ligand alloswitch-1 Deposited 2021-07-06 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：E579A,N667Y,I669A,G675M,T742A,S753A Non-standard monomer：Yes (specific site not provided by mmCIF) | 4YI 2-chloranyl-~{N}-[2-methoxy-4-[(~{E})-pyridin-2-yldiazenyl]phenyl]benzamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；295 K；0.15-0.25 M ammonium phosphate dibasic, 22-24 % polyethylene glycol 400, either with 0.10 M 2-(N-morpholino)ethanesulfonic acid (MES) pH 6.7-6.8 or 0.1 M HEPES pH 6.8
|
Resolution 2.54 Å R-free 0.285 |
| 7RX9 Structure of autoinhibited P-Rex1 Deposited 2021-08-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Not recorded | SO4 SULFATE ION × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；1.8 M (NH4)2SO4, 0.05 MES pH 6.0
|
Resolution 3.22 Å R-free 0.262 |
| 7SJ6 T4 Lysozyme L99A/M102H with 1,2-Azaborine bound Deposited 2021-10-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–164（164 aa）
|
Not recorded | B20 1,2-dihydro-1,2-azaborinine × 1 SO4 SULFATE ION × 2 BME BETA-MERCAPTOETHANOL × 1 HED 2-HYDROXYETHYL DISULFIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277.15 K；Crystals were grown from a 5 mg/ml solution of the protein by the hanging drop method at 4 oC over a well solution of 0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3 % trimethylamine N-oxide, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide.
|
Resolution 1.72 Å R-free 0.202 |
| 7SJ6 T4 Lysozyme L99A/M102H with 1,2-Azaborine bound Deposited 2021-10-16 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
1–164（164 aa）
|
Not recorded | B20 1,2-dihydro-1,2-azaborinine × 1 SO4 SULFATE ION × 3 BME BETA-MERCAPTOETHANOL × 1 ACT ACETATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277.15 K；Crystals were grown from a 5 mg/ml solution of the protein by the hanging drop method at 4 oC over a well solution of 0.1 M sodium acetate, pH 4.5, 30% (w/v) PEG-6000, 0.3 M LiSO4, 3 % trimethylamine N-oxide, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide.
|
Resolution 1.72 Å R-free 0.202 |
| 7XB5 Structure of the ligand-binding domain of S. cerevisiae Upc2 in fusion with T4 lysozyme Deposited 2022-03-20 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
2–161（160 aa）
|
Mutation：R727G,C769T,C812A,I852R,I925G | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；296 K；0.1 M HEPES pH 7.0, 12.5% PEG 8000, 0.2 M sodium citrate
|
Resolution 3.44 Å R-free 0.301 |
| 7XK9 Structure of human beta2 adrenergic receptor bound to constrained isoproterenol Deposited 2022-04-19 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：C918T,C962A,M1096T,M1098T,N1157E,C1265A | GJ6 (5R,6R)-6-(propan-2-ylamino)-5,6,7,8-tetrahydronaphthalene-1,2,5-triol × 1 NA SODIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；100mM Tris-HCl, pH 8.0, 150-200mM lithium acetate, 43-45% PEG 400
|
Resolution 3.40 Å R-free 0.261 |
| 7XKA Structure of human beta2 adrenergic receptor bound to constrained epinephrine Deposited 2022-04-19 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Mutation：C918T,C962A,M1096T,M1098T,N1157E,C1265A | G1I (5R,6R)-6-(methylamino)-5,6,7,8-tetrahydronaphthalene-1,2,5-triol × 1 NA SODIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；100mM Tris-HCl, pH 8.0, 150-200mM lithium acetate, 43-45% PEG400
|
Resolution 3.10 Å R-free 0.272 |
| 7Z36 Crystal structure of the KAP1 tripartite motif in complex with the ZNF93 KRAB domain Deposited 2022-03-01 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric |
Chain A
2–161（160 aa）
Chain B
2–161（160 aa）
|
Mutation：KAP1 B-box 1 domain (residues 141-202) deleted Mutation：KAP1 B-box 1 domain (residues 141-202) deleted | ZN ZINC ION × 8 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；11% (w/v) PEG 5000 MME
5% Tacsimate
0.1 M HEPES pH 7
|
Resolution 2.80 Å R-free 0.274 |
| 8A5X Crystal structure of phosphatidyl inositol 4-kinase II beta in complex with MM1373 Deposited 2022-06-16 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–164（163 aa）
|
Not recorded | L6A 4-azanyl-7-[3-(hydroxymethyl)phenyl]quinazoline-6-carboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；291 K；10% w/v PEG 8.000, 20% v/v ethylene glycol, 3% v/v DMSO,
100 mM bicine/Trizma base pH 8.5,
20 mM 1,6-hexanediol, 20 mM 1-butanol, 20 mM 1,2-propanediol, 20 mM 2-propanol, 20 mM 1,4-butanediol, 20 mM 1,3-propanediol
|
Resolution 2.40 Å R-free 0.231 |
| 8DCR Cryo-EM structure of dobutamine-bound beta1-adrenergic receptor in complex with heterotrimeric Gs-protein Deposited 2022-06-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric |
Chain R
2–161（160 aa）
|
Not recorded | Y00 DOBUTAMINE × 1 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.60 Å |
| 8DCS Cryo-EM structure of cyanopindolol-bound beta1-adrenergic receptor in complex with heterotrimeric Gs-protein Deposited 2022-06-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric |
Chain R
2–161（160 aa）
|
Not recorded | P32 Cyanopindolol × 1 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.50 Å |
| 8EIT Structure of FFAR1-Gq complex bound to DHA Deposited 2022-09-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric |
Chain R
2–161（160 aa）
|
Not recorded | HXA DOCOSA-4,7,10,13,16,19-HEXAENOIC ACID × 1 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.80 Å |
| 8THK Cryo-EM structure of A61603-bound alpha-1A-adrenergic receptor in complex with heterotrimeric Gq-protein Deposited 2023-07-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric |
Chain R
2–161（160 aa）
|
Not recorded | CGZ N-[(5S)-5-(4,5-dihydro-1H-imidazol-2-yl)-2-hydroxy-5,6,7,8-tetrahydronaphthalen-1-yl]methanesulfonamide × 1 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.60 Å |
| 8THL Cryo-EM structure of epinephrine-bound alpha-1A-adrenergic receptor in complex with heterotrimeric Gq-protein Deposited 2023-07-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric |
Chain R
2–161（160 aa）
|
Not recorded | ALE L-EPINEPHRINE × 1 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.10 Å |
| 8UGW Computational design of highly signaling active membrane receptors through de novo solvent-mediated allosteric networks Deposited 2023-10-06 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
60–164（105 aa）
Fragment：residues 2-322
|
Not recorded | NGI 2-[P-(2-CARBOXYETHYL)PHENYLETHYL-AMINO]-5'-N-ETHYLCARBOXAMIDO ADENOSINE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 7；295 K；100mM Hepes pH 7 + 27% PEG 300 + 50mM Sodium Potassium Tartrate
|
Resolution 3.90 Å R-free 0.330 |
| 8W1V The beta2 adrenergic receptor bound to a bitopic ligand Deposited 2024-02-19 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain A
2–161（160 aa）
Chain B
2–161（160 aa）
|
Mutation：N187E,C1054T,C1097A Mutation：N187E,C1054T,C1097A | A1AE2 (2S)-1-[(3-{1-[4-(4-{(2S)-2-hydroxy-3-[(propan-2-yl)amino]propoxy}phenyl)butyl]-1H-1,2,3-triazol-4-yl}propyl)amino]-3-(2-propylphenoxy)propan-2-ol × 2 AV0 Lauryl Maltose Neopentyl Glycol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；293 K；100 mM Tris buffer (pH 8.0), 100 to 175 mM lithium sulfate, 38% to 42% PEG400, and 10 mM EDTA
|
Resolution 3.00 Å R-free 0.292 |
| 8YIC SAR247799-bound S1PR1-Gi protein complex Deposited 2024-02-29 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain R
2–161（160 aa）
|
Not recorded | A1LYQ SAR247799 × 1 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.47 Å |
| 9CBL Cryo-EM structure of epinephrine-bound alpha-2A-adrenergic receptor in complex with heterotrimeric Gi-protein Deposited 2024-06-19 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain R
2–161（160 aa）
|
Not recorded | ALE L-EPINEPHRINE × 1 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.80 Å |
| 9CBM Cryo-EM structure of dexmedetomidine-bound alpha-2A-adrenergic receptor in complex with heterotrimeric Gi-protein Deposited 2024-06-19 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain R
2–161（160 aa）
|
Not recorded | CZX 4-[(1~{S})-1-(2,3-dimethylphenyl)ethyl]-1~{H}-imidazole × 1 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.20 Å |
| 9HC0 Dark structure of the human metabotropic glutamate receptor 5 transmembrane domain bound to photoswitchable ligand alloswitch-1 Deposited 2024-11-08 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–162（161 aa）
|
Mutation：E579A,N667Y,I669A,G675M,T742A,S753A Non-standard monomer：Yes (specific site not provided by mmCIF) | OLA OLEIC ACID × 5 4YI 2-chloranyl-~{N}-[2-methoxy-4-[(~{E})-pyridin-2-yldiazenyl]phenyl]benzamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 7.2；293 K；PEG300, di-ammonium hydrogen phosphate, 1,6-hexanediol, BIS-TRIS
|
Resolution 2.33 Å R-free 0.271 |
| 9HC3 Apo-state structure of the human metabotropic glutamate receptor 5 transmembrane domain freeze-trapped after light activation of photoswitchable ligand alloswitch-1 Deposited 2024-11-08 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–162（161 aa）
|
Mutation：E579A,N667Y,I669A,G675M,T742A,S753A Non-standard monomer：Yes (specific site not provided by mmCIF) | OLA OLEIC ACID × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；pH 7.2；293 K；PEG300, di-ammonium hydrogen phosphate, 1,6-hexanediol, BIS-TRIS
|
Resolution 2.90 Å R-free 0.302 |
| 9HHM Crystal structure of phosphatidyl inositol 4-kinase II beta in complex with HH5129 Deposited 2024-11-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–164（163 aa）
|
Not recorded | A1IVA (1~{S},2~{S},4~{S},5~{R})-6-[[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-bis(oxidanylidene)-$l^{6}-phosphanyl]oxy-bis(oxidanylidene)-$l^{6}-phosphanyl]methyl-bis(oxidanylidene)-$l^{6}-phosphanyl]oxycyclohexane-1,2,3,4,5-pentol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；291 K；100 mM HEPES, pH 7.0;
15 % (w/v) PEG 4,000
|
Resolution 2.25 Å R-free 0.240 |
| 9HHM Crystal structure of phosphatidyl inositol 4-kinase II beta in complex with HH5129 Deposited 2024-11-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–164（163 aa）
|
Not recorded | A1IVA (1~{S},2~{S},4~{S},5~{R})-6-[[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-bis(oxidanylidene)-$l^{6}-phosphanyl]oxy-bis(oxidanylidene)-$l^{6}-phosphanyl]methyl-bis(oxidanylidene)-$l^{6}-phosphanyl]oxycyclohexane-1,2,3,4,5-pentol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；291 K；100 mM HEPES, pH 7.0;
15 % (w/v) PEG 4,000
|
Resolution 2.25 Å R-free 0.240 |
| 9Q1F Choanoflagellate Salpingoeca macrocollata STING Deposited 2025-08-13 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–161（161 aa）
Chain B
1–161（161 aa）
|
Not recorded | 1SY cGAMP × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.65；293 K；5% ethylene glycol, 100 mM MOPS pH 6.65, and 10% (w/v) PEG8000
|
Resolution 2.65 Å R-free 0.275 |
| 9RKF Dark structure of beta-2 Adrenergic receptor with photoazolol in Dark state recorded at SwissFEL Deposited 2025-06-13 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–162（161 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) | SO4 SULFATE ION × 5 CLR CHOLESTEROL × 3 12P DODECAETHYLENE GLYCOL × 3 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 5 1PE PENTAETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 1 GOL GLYCEROL × 1 A1JHU ~{N}-[4-[(~{E})-[2-[(2~{S})-2-oxidanyl-3-(propan-2-ylamino)propoxy]phenyl]diazenyl]phenyl]ethanamide × 1 PLM PALMITIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；289 K；100mM tri-sodium citrate pH= 6.2, 245mM Li2SO4, 32% PEG 350 MME, 10uM photoazolol-1
|
Resolution 2.45 Å R-free 0.219 |
| 9RKG Mixed model refinement of beta-2 Adrenergic receptor with photoazolol in dark state and Light state, 10 seconds after light activation, recorded at SwissFEL Deposited 2025-06-13 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Not recorded | SO4 SULFATE ION × 6 ACM ACETAMIDE × 1 CLR CHOLESTEROL × 3 PLM PALMITIC ACID × 1 12P DODECAETHYLENE GLYCOL × 3 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 5 1PE PENTAETHYLENE GLYCOL × 3 EDO 1,2-ETHANEDIOL × 2 GOL GLYCEROL × 1 A1JHU ~{N}-[4-[(~{E})-[2-[(2~{S})-2-oxidanyl-3-(propan-2-ylamino)propoxy]phenyl]diazenyl]phenyl]ethanamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；289 K；100 mM tri-sodium citrate (pH= 6.2), 245 mM Li2SO4, 32% PEG 350 MME, 10 uM photoazolol-1
|
Resolution 2.45 Å R-free 0.217 |
| 9RKH Dark structure of beta-2 Adrenergic receptor with photoazolol in Dark state recorded at LCLS Deposited 2025-06-13 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–162（161 aa）
|
Non-standard monomer：Yes (specific site not provided by mmCIF) | SO4 SULFATE ION × 5 CLR CHOLESTEROL × 2 PLM PALMITIC ACID × 1 12P DODECAETHYLENE GLYCOL × 3 A1JHU ~{N}-[4-[(~{E})-[2-[(2~{S})-2-oxidanyl-3-(propan-2-ylamino)propoxy]phenyl]diazenyl]phenyl]ethanamide × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 7 EDO 1,2-ETHANEDIOL × 1 GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；289 K；100 mM tri-sodium citrate (pH= 6.2), 245 mM Li2SO4, 32% PEG 350 MME, 10 uM photoazolol-1
|
Resolution 2.50 Å R-free 0.218 |
| 9RKI Mixed model refinement of beta-2 Adrenergic receptor with photoazolol in dark state and Light state, 17 nanoseconds after light activation, recorded at LCLS Deposited 2025-06-13 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–161（160 aa）
|
Not recorded | SO4 SULFATE ION × 7 ACM ACETAMIDE × 1 CLR CHOLESTEROL × 3 PLM PALMITIC ACID × 1 12P DODECAETHYLENE GLYCOL × 3 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 7 EDO 1,2-ETHANEDIOL × 2 GOL GLYCEROL × 1 1PE PENTAETHYLENE GLYCOL × 1 A1JHU ~{N}-[4-[(~{E})-[2-[(2~{S})-2-oxidanyl-3-(propan-2-ylamino)propoxy]phenyl]diazenyl]phenyl]ethanamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
LIPIDIC CUBIC PHASE；289 K；100 mM tri-sodium citrate (pH= 6.2), 245 mM Li2SO4, 32% PEG 350 MME, 10 uM photoazolol-1
|
Resolution 2.60 Å R-free 0.234 |
| 9W3F Cryo-EM structure of the human beta2-adrenergic receptor in complex with a novel antagonist Deposited 2025-07-29 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
2–162（161 aa）
|
Not recorded | No recorded non-water small molecule | ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions | Resolution 3.04 Å |
721 other PDB entries and 846 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | LYS_BPT4 |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–164； UniProt 1–164 |
