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LongText Report for: 7buk-pdb

Name Class
7buk-pdb
HEADER    HYDROLASE                               07-APR-20   7BUK              
TITLE     T1 LIPASE MUTANT - 5M (D43E/T118N/E226D/E250L/N304E)                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE;                                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.1.3;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GEOBACILLUS ZALIHAE;                            
SOURCE   3 ORGANISM_TAXID: 213419;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PLYSS                                     
KEYWDS    LIPASE, MUTATION, TRIGLYCERIDES, HYDROLASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.N.H.ISHAK,R.N.Z.R.A.RAHMAN,M.S.M.ALI,A.T.C.LEOW,N.H.A.KAMARUDIN     
REVDAT   1   07-APR-21 7BUK    0                                                
JRNL        AUTH   S.N.H.ISHAK,M.S.M.ALI,A.T.C.LEOW,N.H.A.KAMARUDIN,            
JRNL        AUTH 2 R.N.Z.R.A.RAHMAN                                             
JRNL        TITL   CRYSTALLIZATION AND STRUCTURE ELUCIDATION OF 5M MUTANT OF T1 
JRNL        TITL 2 LIPASE GEOBACILLUS ZALIHAE.                                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.64 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0238                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.64                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 23631                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1188                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.64                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.71                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1505                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.32                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 77                           
REMARK   3   BIN FREE R VALUE                    : 0.4020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6112                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 183                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.93                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.22000                                              
REMARK   3    B22 (A**2) : -1.83000                                             
REMARK   3    B33 (A**2) : 0.36000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.90000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.376         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.241         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.524        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.926                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.856                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6280 ; 0.009 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  5564 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8540 ; 1.587 ; 1.642       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 12848 ; 1.247 ; 1.573       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   772 ; 7.324 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   366 ;30.584 ;21.148       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   954 ;16.499 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    52 ;18.431 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   768 ; 0.069 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7230 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1478 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 7BUK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-APR-20.                  
REMARK 100 THE DEPOSITION ID IS D_1300015947.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUN-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : CU                                 
REMARK 200  OPTICS                         : DEXTRIS 200K                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24822                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.9                               
REMARK 200  DATA REDUNDANCY                : 2.100                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.12900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 2DSN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5 M SODIUM CACODYLATE TRIHYDRATE,      
REMARK 280  0.4 M SODIUM CITRATE TRIBASIC PH 6.5, 0.2 M NACL, VAPOR             
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293.15K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       58.79600            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.63450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       58.79600            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       40.63450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2                            
REMARK 350 SURFACE AREA OF THE COMPLEX: 14930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2                            
REMARK 350 SURFACE AREA OF THE COMPLEX: 14960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 578  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     PRO A   -15                                                      
REMARK 465     ILE A   -14                                                      
REMARK 465     SER A   -13                                                      
REMARK 465     ARG A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     VAL A    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     ARG A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     MET B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     PRO B   -15                                                      
REMARK 465     ILE B   -14                                                      
REMARK 465     SER B   -13                                                      
REMARK 465     ARG B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     VAL B    -4                                                      
REMARK 465     PRO B    -3                                                      
REMARK 465     ARG B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH2  ARG A    92     OD2  ASP A   205              2.05            
REMARK 500   NH2  ARG B    92     OD2  ASP B   205              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 113     -144.51     64.76                                   
REMARK 500    PHE A 154        8.29   -150.43                                   
REMARK 500    VAL A 203      -59.24     70.38                                   
REMARK 500    LEU A 208       33.24    -99.87                                   
REMARK 500    ARG A 214      136.50   -170.92                                   
REMARK 500    PRO A 217      125.84    -34.28                                   
REMARK 500    ARG A 271       43.02   -145.69                                   
REMARK 500    ASN A 288      131.64    -38.65                                   
REMARK 500    ASP A 310     -148.15   -116.01                                   
REMARK 500    ILE A 319      -40.20   -137.19                                   
REMARK 500    LYS A 329      -56.91   -137.17                                   
REMARK 500    ASN A 367       94.69   -160.29                                   
REMARK 500    LEU B  98       58.97   -147.19                                   
REMARK 500    SER B 113     -137.44     60.61                                   
REMARK 500    ASP B 175       51.67   -108.04                                   
REMARK 500    ALA B 192      -12.20     81.66                                   
REMARK 500    VAL B 203      -70.60     68.60                                   
REMARK 500    ARG B 271       42.63   -148.23                                   
REMARK 500    LEU B 277      -80.21    -70.95                                   
REMARK 500    LEU B 285      128.40    -39.55                                   
REMARK 500    ASP B 310     -156.10   -139.74                                   
REMARK 500    LYS B 329      -53.71   -122.66                                   
REMARK 500    ASN B 367       93.96   -172.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  61   OD1                                                    
REMARK 620 2 ASP A  61   OD2  54.5                                              
REMARK 620 3 HIS A  81   NE2  95.9 150.3                                        
REMARK 620 4 HIS A  87   NE2 115.9  89.3 107.1                                  
REMARK 620 5 ASP A 238   OD2 128.7 102.0  96.6 107.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 402  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 286   O                                                      
REMARK 620 2 GLU A 360   OE2  84.0                                              
REMARK 620 3 ASP A 365   OD2  99.8 113.0                                        
REMARK 620 4 PRO A 366   O   166.2  95.5  93.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  61   OD1                                                    
REMARK 620 2 HIS B  81   NE2 102.9                                              
REMARK 620 3 HIS B  87   NE2 115.1 103.3                                        
REMARK 620 4 ASP B 238   OD2 132.5  95.4 102.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 402  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B 286   O                                                      
REMARK 620 2 GLU B 360   OE2  81.4                                              
REMARK 620 3 ASP B 365   OD2 110.5 120.0                                        
REMARK 620 4 PRO B 366   O   165.1  96.2  83.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 402                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THIS IS D43E/T118N/E226D/E250L/N304E MUTANT.                         
REMARK 999 AND 18 N-TERMINAL RESIDUES (MSPISRHHHHHHLVPRGS) ARE EXPRESSION TAGS. 
DBREF  7BUK A  -17   388  PDB    7BUK     7BUK           -17    388             
DBREF  7BUK B  -17   388  PDB    7BUK     7BUK           -17    388             
SEQRES   1 A  406  MET SER PRO ILE SER ARG HIS HIS HIS HIS HIS HIS LEU          
SEQRES   2 A  406  VAL PRO ARG GLY SER ALA SER LEU ARG ALA ASN ASP ALA          
SEQRES   3 A  406  PRO ILE VAL LEU LEU HIS GLY PHE THR GLY TRP GLY ARG          
SEQRES   4 A  406  GLU GLU MET PHE GLY PHE LYS TYR TRP GLY GLY VAL ARG          
SEQRES   5 A  406  GLY ASP ILE GLU GLN TRP LEU ASN GLU ASN GLY TYR ARG          
SEQRES   6 A  406  THR TYR THR LEU ALA VAL GLY PRO LEU SER SER ASN TRP          
SEQRES   7 A  406  ASP ARG ALA CYS GLU ALA TYR ALA GLN LEU VAL GLY GLY          
SEQRES   8 A  406  THR VAL ASP TYR GLY ALA ALA HIS ALA ALA LYS HIS GLY          
SEQRES   9 A  406  HIS ALA ARG PHE GLY ARG THR TYR PRO GLY LEU LEU PRO          
SEQRES  10 A  406  GLU LEU LYS ARG GLY GLY ARG ILE HIS ILE ILE ALA HIS          
SEQRES  11 A  406  SER GLN GLY GLY GLN ASN ALA ARG MET LEU VAL SER LEU          
SEQRES  12 A  406  LEU GLU ASN GLY SER GLN GLU GLU ARG GLU TYR ALA LYS          
SEQRES  13 A  406  ALA HIS ASN VAL SER LEU SER PRO LEU PHE GLU GLY GLY          
SEQRES  14 A  406  HIS HIS PHE VAL LEU SER VAL THR THR ILE ALA THR PRO          
SEQRES  15 A  406  HIS ASP GLY THR THR LEU VAL ASN MET VAL ASP PHE THR          
SEQRES  16 A  406  ASP ARG PHE PHE ASP LEU GLN LYS ALA VAL LEU GLU ALA          
SEQRES  17 A  406  ALA ALA VAL ALA SER ASN VAL PRO TYR THR SER GLN VAL          
SEQRES  18 A  406  TYR ASP PHE LYS LEU ASP GLN TRP GLY LEU ARG ARG GLN          
SEQRES  19 A  406  PRO GLY GLU SER PHE ASP HIS TYR PHE ASP ARG LEU LYS          
SEQRES  20 A  406  ARG SER PRO VAL TRP THR SER THR ASP THR ALA ARG TYR          
SEQRES  21 A  406  ASP LEU SER VAL SER GLY ALA LEU LYS LEU ASN GLN TRP          
SEQRES  22 A  406  VAL GLN ALA SER PRO ASN THR TYR TYR LEU SER PHE SER          
SEQRES  23 A  406  THR GLU ARG THR TYR ARG GLY ALA LEU THR GLY ASN HIS          
SEQRES  24 A  406  TYR PRO GLU LEU GLY MET ASN ALA PHE SER ALA VAL VAL          
SEQRES  25 A  406  CYS ALA PRO PHE LEU GLY SER TYR ARG GLU PRO THR LEU          
SEQRES  26 A  406  GLY ILE ASP ASP ARG TRP LEU GLU ASN ASP GLY ILE VAL          
SEQRES  27 A  406  ASN THR VAL SER MET ASN GLY PRO LYS ARG GLY SER SER          
SEQRES  28 A  406  ASP ARG ILE VAL PRO TYR ASP GLY THR LEU LYS LYS GLY          
SEQRES  29 A  406  VAL TRP ASN ASP MET GLY THR TYR ASN VAL ASP HIS LEU          
SEQRES  30 A  406  GLU ILE ILE GLY VAL ASP PRO ASN PRO SER PHE ASP ILE          
SEQRES  31 A  406  ARG ALA PHE TYR LEU ARG LEU ALA GLU GLN LEU ALA SER          
SEQRES  32 A  406  LEU ARG PRO                                                  
SEQRES   1 B  406  MET SER PRO ILE SER ARG HIS HIS HIS HIS HIS HIS LEU          
SEQRES   2 B  406  VAL PRO ARG GLY SER ALA SER LEU ARG ALA ASN ASP ALA          
SEQRES   3 B  406  PRO ILE VAL LEU LEU HIS GLY PHE THR GLY TRP GLY ARG          
SEQRES   4 B  406  GLU GLU MET PHE GLY PHE LYS TYR TRP GLY GLY VAL ARG          
SEQRES   5 B  406  GLY ASP ILE GLU GLN TRP LEU ASN GLU ASN GLY TYR ARG          
SEQRES   6 B  406  THR TYR THR LEU ALA VAL GLY PRO LEU SER SER ASN TRP          
SEQRES   7 B  406  ASP ARG ALA CYS GLU ALA TYR ALA GLN LEU VAL GLY GLY          
SEQRES   8 B  406  THR VAL ASP TYR GLY ALA ALA HIS ALA ALA LYS HIS GLY          
SEQRES   9 B  406  HIS ALA ARG PHE GLY ARG THR TYR PRO GLY LEU LEU PRO          
SEQRES  10 B  406  GLU LEU LYS ARG GLY GLY ARG ILE HIS ILE ILE ALA HIS          
SEQRES  11 B  406  SER GLN GLY GLY GLN ASN ALA ARG MET LEU VAL SER LEU          
SEQRES  12 B  406  LEU GLU ASN GLY SER GLN GLU GLU ARG GLU TYR ALA LYS          
SEQRES  13 B  406  ALA HIS ASN VAL SER LEU SER PRO LEU PHE GLU GLY GLY          
SEQRES  14 B  406  HIS HIS PHE VAL LEU SER VAL THR THR ILE ALA THR PRO          
SEQRES  15 B  406  HIS ASP GLY THR THR LEU VAL ASN MET VAL ASP PHE THR          
SEQRES  16 B  406  ASP ARG PHE PHE ASP LEU GLN LYS ALA VAL LEU GLU ALA          
SEQRES  17 B  406  ALA ALA VAL ALA SER ASN VAL PRO TYR THR SER GLN VAL          
SEQRES  18 B  406  TYR ASP PHE LYS LEU ASP GLN TRP GLY LEU ARG ARG GLN          
SEQRES  19 B  406  PRO GLY GLU SER PHE ASP HIS TYR PHE ASP ARG LEU LYS          
SEQRES  20 B  406  ARG SER PRO VAL TRP THR SER THR ASP THR ALA ARG TYR          
SEQRES  21 B  406  ASP LEU SER VAL SER GLY ALA LEU LYS LEU ASN GLN TRP          
SEQRES  22 B  406  VAL GLN ALA SER PRO ASN THR TYR TYR LEU SER PHE SER          
SEQRES  23 B  406  THR GLU ARG THR TYR ARG GLY ALA LEU THR GLY ASN HIS          
SEQRES  24 B  406  TYR PRO GLU LEU GLY MET ASN ALA PHE SER ALA VAL VAL          
SEQRES  25 B  406  CYS ALA PRO PHE LEU GLY SER TYR ARG GLU PRO THR LEU          
SEQRES  26 B  406  GLY ILE ASP ASP ARG TRP LEU GLU ASN ASP GLY ILE VAL          
SEQRES  27 B  406  ASN THR VAL SER MET ASN GLY PRO LYS ARG GLY SER SER          
SEQRES  28 B  406  ASP ARG ILE VAL PRO TYR ASP GLY THR LEU LYS LYS GLY          
SEQRES  29 B  406  VAL TRP ASN ASP MET GLY THR TYR ASN VAL ASP HIS LEU          
SEQRES  30 B  406  GLU ILE ILE GLY VAL ASP PRO ASN PRO SER PHE ASP ILE          
SEQRES  31 B  406  ARG ALA PHE TYR LEU ARG LEU ALA GLU GLN LEU ALA SER          
SEQRES  32 B  406  LEU ARG PRO                                                  
HET     ZN  A 401       1                                                       
HET     CA  A 402       1                                                       
HET     ZN  B 401       1                                                       
HET     CA  B 402       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4   CA    2(CA 2+)                                                     
FORMUL   7  HOH   *183(H2 O)                                                    
HELIX    1 AA1 GLU A   23  PHE A   27  5                                   5    
HELIX    2 AA2 GLY A   31  GLY A   35  5                                   5    
HELIX    3 AA3 ASP A   36  ASN A   44  1                                   9    
HELIX    4 AA4 SER A   58  GLY A   72  1                                  15    
HELIX    5 AA5 GLY A   78  GLY A   86  1                                   9    
HELIX    6 AA6 LEU A   98  GLY A  104  5                                   7    
HELIX    7 AA7 GLN A  114  GLY A  129  1                                  16    
HELIX    8 AA8 SER A  130  HIS A  140  1                                  11    
HELIX    9 AA9 SER A  145  GLU A  149  5                                   5    
HELIX   10 AB1 THR A  168  MET A  173  5                                   6    
HELIX   11 AB2 ASP A  175  ALA A  191  1                                  17    
HELIX   12 AB3 LEU A  208  GLY A  212  5                                   5    
HELIX   13 AB4 SER A  220  ARG A  230  1                                  11    
HELIX   14 AB5 SER A  231  SER A  236  1                                   6    
HELIX   15 AB6 THR A  239  SER A  245  1                                   7    
HELIX   16 AB7 SER A  245  GLN A  254  1                                  10    
HELIX   17 AB8 ASN A  288  CYS A  295  1                                   8    
HELIX   18 AB9 CYS A  295  GLY A  300  1                                   6    
HELIX   19 AC1 GLU A  304  GLY A  308  5                                   5    
HELIX   20 AC2 ASP A  310  LEU A  314  5                                   5    
HELIX   21 AC3 ASN A  321  ASN A  326  5                                   6    
HELIX   22 AC4 ASP A  371  SER A  385  1                                  15    
HELIX   23 AC5 GLU B   23  PHE B   27  5                                   5    
HELIX   24 AC6 GLY B   31  GLY B   35  5                                   5    
HELIX   25 AC7 ASP B   36  ASN B   44  1                                   9    
HELIX   26 AC8 SER B   58  GLY B   72  1                                  15    
HELIX   27 AC9 GLY B   78  GLY B   86  1                                   9    
HELIX   28 AD1 LEU B   98  LYS B  102  5                                   5    
HELIX   29 AD2 GLN B  114  GLY B  129  1                                  16    
HELIX   30 AD3 SER B  130  ASN B  141  1                                  12    
HELIX   31 AD4 SER B  145  GLU B  149  5                                   5    
HELIX   32 AD5 THR B  168  MET B  173  5                                   6    
HELIX   33 AD6 ASP B  175  ALA B  190  1                                  16    
HELIX   34 AD7 LEU B  208  GLY B  212  5                                   5    
HELIX   35 AD8 SER B  220  LYS B  229  1                                  10    
HELIX   36 AD9 SER B  231  SER B  236  1                                   6    
HELIX   37 AE1 THR B  239  SER B  245  1                                   7    
HELIX   38 AE2 SER B  245  GLN B  254  1                                  10    
HELIX   39 AE3 ASN B  288  CYS B  295  1                                   8    
HELIX   40 AE4 CYS B  295  GLY B  300  1                                   6    
HELIX   41 AE5 GLU B  304  GLY B  308  5                                   5    
HELIX   42 AE6 ASP B  310  LEU B  314  5                                   5    
HELIX   43 AE7 ASN B  321  ASN B  326  5                                   6    
HELIX   44 AE8 ASP B  371  SER B  385  1                                  15    
SHEET    1 AA1 7 THR A  48  LEU A  51  0                                        
SHEET    2 AA1 7 ILE A  10  LEU A  13  1  N  LEU A  12   O  LEU A  51           
SHEET    3 AA1 7 ILE A 107  HIS A 112  1  O  HIS A 108   N  VAL A  11           
SHEET    4 AA1 7 VAL A 155  ILE A 161  1  O  THR A 159   N  ALA A 111           
SHEET    5 AA1 7 TYR A 263  GLU A 270  1  O  TYR A 263   N  VAL A 158           
SHEET    6 AA1 7 TRP A 348  ASN A 355  1  O  MET A 351   N  SER A 266           
SHEET    7 AA1 7 ILE A 336  PRO A 338  1  N  VAL A 337   O  TRP A 348           
SHEET    1 AA2 2 GLY A  73  ASP A  76  0                                        
SHEET    2 AA2 2 PHE A  90  TYR A  94 -1  O  ARG A  92   N  VAL A  75           
SHEET    1 AA3 2 THR A 272  ARG A 274  0                                        
SHEET    2 AA3 2 HIS A 281  PRO A 283 -1  O  TYR A 282   N  TYR A 273           
SHEET    1 AA4 7 THR B  48  LEU B  51  0                                        
SHEET    2 AA4 7 ILE B  10  LEU B  13  1  N  LEU B  12   O  LEU B  51           
SHEET    3 AA4 7 ILE B 107  HIS B 112  1  O  HIS B 108   N  VAL B  11           
SHEET    4 AA4 7 VAL B 155  ILE B 161  1  O  SER B 157   N  ILE B 109           
SHEET    5 AA4 7 TYR B 263  THR B 269  1  O  PHE B 267   N  THR B 160           
SHEET    6 AA4 7 TRP B 348  TYR B 354  1  O  TYR B 354   N  SER B 268           
SHEET    7 AA4 7 ILE B 336  PRO B 338  1  N  VAL B 337   O  TRP B 348           
SHEET    1 AA5 2 GLY B  73  ASP B  76  0                                        
SHEET    2 AA5 2 PHE B  90  TYR B  94 -1  O  ARG B  92   N  VAL B  75           
SHEET    1 AA6 2 THR B 272  ARG B 274  0                                        
SHEET    2 AA6 2 HIS B 281  PRO B 283 -1  O  TYR B 282   N  TYR B 273           
LINK         OD1 ASP A  61                ZN    ZN A 401     1555   1555  2.08  
LINK         OD2 ASP A  61                ZN    ZN A 401     1555   1555  2.65  
LINK         NE2 HIS A  81                ZN    ZN A 401     1555   1555  2.43  
LINK         NE2 HIS A  87                ZN    ZN A 401     1555   1555  2.15  
LINK         OD2 ASP A 238                ZN    ZN A 401     1555   1555  1.98  
LINK         O   GLY A 286                CA    CA A 402     1555   1555  2.18  
LINK         OE2 GLU A 360                CA    CA A 402     1555   1555  2.37  
LINK         OD2 ASP A 365                CA    CA A 402     1555   1555  2.58  
LINK         O   PRO A 366                CA    CA A 402     1555   1555  2.46  
LINK         OD1 ASP B  61                ZN    ZN B 401     1555   1555  2.06  
LINK         NE2 HIS B  81                ZN    ZN B 401     1555   1555  2.07  
LINK         NE2 HIS B  87                ZN    ZN B 401     1555   1555  2.17  
LINK         OD2 ASP B 238                ZN    ZN B 401     1555   1555  1.94  
LINK         O   GLY B 286                CA    CA B 402     1555   1555  2.35  
LINK         OE2 GLU B 360                CA    CA B 402     1555   1555  2.30  
LINK         OD2 ASP B 365                CA    CA B 402     1555   1555  2.42  
LINK         O   PRO B 366                CA    CA B 402     1555   1555  2.36  
SITE     1 AC1  4 ASP A  61  HIS A  81  HIS A  87  ASP A 238                    
SITE     1 AC2  4 GLY A 286  GLU A 360  ASP A 365  PRO A 366                    
SITE     1 AC3  5 SER B  58  ASP B  61  HIS B  81  HIS B  87                    
SITE     2 AC3  5 ASP B 238                                                     
SITE     1 AC4  4 GLY B 286  GLU B 360  ASP B 365  PRO B 366                    
CRYST1  117.592   81.269   99.522  90.00  97.32  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008504  0.000000  0.001092        0.00000                         
SCALE2      0.000000  0.012305  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010131        0.00000                         
TER    3057      PRO A 388                                                      
TER    6114      PRO B 388                                                      
MASTER      418    0    4   44   22    0    5    6 6299    2   22   64          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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