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LongText Report for: 3AIN-pdb

Name Class
3AIN-pdb
HEADER    HYDROLASE                               16-MAY-10   3AIN              
TITLE     R267G MUTANT OF A HSL-LIKE CARBOXYLESTERASE FROM SULFOLOBUS TOKODAII  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 303AA LONG HYPOTHETICAL ESTERASE;                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: CARBOXYLESTERASE;                                           
COMPND   5 EC: 3.1.1.1;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SULFOLOBUS TOKODAII;                            
SOURCE   3 ORGANISM_TAXID: 111955;                                              
SOURCE   4 STRAIN: 7;                                                           
SOURCE   5 GENE: ST0071;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODONPLUS;                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A+                                   
KEYWDS    CARBOXYLESTERASE, THERMOPHILIC, DIMER, ARCHAEA, R267G, HYDROLASE      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.ANGKAWIDJAJA,S.KANAYA                                               
REVDAT   1   08-JUN-11 3AIN    0                                                
JRNL        AUTH   C.ANGKAWIDJAJA,Y.KOGA,K.TAKANO,S.KANAYA                      
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF A HSL-LIKE CARBOXYLESTERASE   
JRNL        TITL 2 FROM A THERMOACIDOPHILIC ARCHAEON SULFOLOBUS TOKODAII        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.35                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 188002                         
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) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9993                            
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) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 13678                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.06                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2710                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 706                          
REMARK   3   BIN FREE R VALUE                    : 0.2840                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8920                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 121                                     
REMARK   3   SOLVENT ATOMS            : 755                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
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): 0.076         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.048         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.399         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9247 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12560 ; 1.239 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1128 ; 6.938 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   428 ;33.803 ;24.112       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1468 ;16.400 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;20.971 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1364 ; 0.116 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7056 ; 0.021 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  5612 ; 2.136 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9044 ; 3.301 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3635 ; 5.084 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3516 ; 7.730 ; 4.500       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3AIN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029299.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL38B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 198205                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 25.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: 3AIK                         
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH 8.5, 0.2M AMMONIUM      
REMARK 280  PHOSPHATE MONOBASIC, 50% MPD, VAPOR DIFFUSION, SITTING DROP,        
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       57.47650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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 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   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ILE A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     ILE A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     ILE A    14                                                      
REMARK 465     GLN A    15                                                      
REMARK 465     LEU A    16                                                      
REMARK 465     PRO A    17                                                      
REMARK 465     ILE A    18                                                      
REMARK 465     GLY A    19                                                      
REMARK 465     LYS A    20                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ILE B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     ILE B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 465     ILE B    14                                                      
REMARK 465     GLN B    15                                                      
REMARK 465     LEU B    16                                                      
REMARK 465     PRO B    17                                                      
REMARK 465     ILE B    18                                                      
REMARK 465     GLY B    19                                                      
REMARK 465     LYS B    20                                                      
REMARK 465     MET C   -19                                                      
REMARK 465     GLY C   -18                                                      
REMARK 465     SER C   -17                                                      
REMARK 465     SER C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     GLY C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     VAL C    -5                                                      
REMARK 465     PRO C    -4                                                      
REMARK 465     ARG C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ILE C     2                                                      
REMARK 465     ASP C     3                                                      
REMARK 465     PRO C     4                                                      
REMARK 465     LYS C     5                                                      
REMARK 465     ILE C     6                                                      
REMARK 465     LYS C     7                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     LEU C     9                                                      
REMARK 465     LEU C    10                                                      
REMARK 465     GLU C    11                                                      
REMARK 465     SER C    12                                                      
REMARK 465     THR C    13                                                      
REMARK 465     ILE C    14                                                      
REMARK 465     GLN C    15                                                      
REMARK 465     LEU C    16                                                      
REMARK 465     PRO C    17                                                      
REMARK 465     ILE C    18                                                      
REMARK 465     GLY C    19                                                      
REMARK 465     LYS C    20                                                      
REMARK 465     MET D   -19                                                      
REMARK 465     GLY D   -18                                                      
REMARK 465     SER D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     GLY D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     VAL D    -5                                                      
REMARK 465     PRO D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ILE D     2                                                      
REMARK 465     ASP D     3                                                      
REMARK 465     PRO D     4                                                      
REMARK 465     LYS D     5                                                      
REMARK 465     ILE D     6                                                      
REMARK 465     LYS D     7                                                      
REMARK 465     LYS D     8                                                      
REMARK 465     LEU D     9                                                      
REMARK 465     LEU D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     SER D    12                                                      
REMARK 465     THR D    13                                                      
REMARK 465     ILE D    14                                                      
REMARK 465     GLN D    15                                                      
REMARK 465     LEU D    16                                                      
REMARK 465     PRO D    17                                                      
REMARK 465     ILE D    18                                                      
REMARK 465     GLY D    19                                                      
REMARK 465     LYS D    20                                                      
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 B    39     O    HOH B   555              1.63            
REMARK 500   O4   MPD A   307     O    HOH A   650              2.10            
REMARK 500   OE1  GLU B    46     O    HOH B   658              2.16            
REMARK 500   CG   GLU C    41     O    HOH C   430              2.17            
REMARK 500   O    HOH B   413     O    HOH B   549              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    PHE A 117      140.45    -38.93                                   
REMARK 500    PRO A 118       30.87    -97.15                                   
REMARK 500    SER A 150     -120.59     60.85                                   
REMARK 500    TYR A 177       63.34     32.15                                   
REMARK 500    PHE A 197      -57.82     73.72                                   
REMARK 500    HIS A 242       48.15    -99.16                                   
REMARK 500    PHE A 278       30.83    -95.42                                   
REMARK 500    VAL B  42     -168.12   -124.42                                   
REMARK 500    ASP B  85     -179.78   -177.45                                   
REMARK 500    SER B 150     -123.42     61.20                                   
REMARK 500    TYR B 177       62.47     36.89                                   
REMARK 500    PHE B 197      -58.54     75.74                                   
REMARK 500    HIS B 242       55.52    -96.42                                   
REMARK 500    PHE B 278       32.75    -97.54                                   
REMARK 500    VAL C  42     -167.41   -123.25                                   
REMARK 500    LYS C  44      144.55   -170.36                                   
REMARK 500    ASP C  85     -176.35   -177.46                                   
REMARK 500    PHE C 117      139.08    -37.16                                   
REMARK 500    PRO C 118       33.96    -96.56                                   
REMARK 500    SER C 150     -122.70     64.36                                   
REMARK 500    TYR C 177       60.75     35.72                                   
REMARK 500    PHE C 197      -58.70     75.89                                   
REMARK 500    HIS C 242       49.39   -100.98                                   
REMARK 500    VAL D  42     -168.16   -123.28                                   
REMARK 500    LYS D  44      135.66   -177.69                                   
REMARK 500    ASP D  85     -177.90   -175.75                                   
REMARK 500    PHE D 117      134.21    -34.61                                   
REMARK 500    SER D 150     -120.62     63.88                                   
REMARK 500    TYR D 177       64.27     31.90                                   
REMARK 500    PHE D 197      -57.33     75.47                                   
REMARK 500    HIS D 242       51.43    -97.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TYR B   70     GLY B   71                  149.93                    
REMARK 500 TYR D   70     GLY D   71                  148.34                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR C 294         0.07    SIDE CHAIN                              
REMARK 500    TYR D 294         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLU C  24         10.27                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 494        DISTANCE =  5.62 ANGSTROMS                       
REMARK 525    HOH A 709        DISTANCE =  7.23 ANGSTROMS                       
REMARK 525    HOH B 732        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH B 739        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH B 740        DISTANCE =  7.31 ANGSTROMS                       
REMARK 525    HOH C 765        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH D 460        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH D 717        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH D 734        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH D 737        DISTANCE =  6.79 ANGSTROMS                       
REMARK 525    HOH D 763        DISTANCE =  5.51 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD C 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD C 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD D 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD D 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD D 307                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3AIK   RELATED DB: PDB                                   
REMARK 900 PARENT PROTEIN                                                       
REMARK 900 RELATED ID: 3AIL   RELATED DB: PDB                                   
REMARK 900 PARENT PROTEIN COMPLEXED WITH INHIBITOR                              
REMARK 900 RELATED ID: 3AIM   RELATED DB: PDB                                   
REMARK 900 R267E MUTANT OF PARENT PROTEIN                                       
REMARK 900 RELATED ID: 3AIO   RELATED DB: PDB                                   
DBREF  3AIN A    1   303  UNP    Q976W8   Q976W8_SULTO     1    303             
DBREF  3AIN B    1   303  UNP    Q976W8   Q976W8_SULTO     1    303             
DBREF  3AIN C    1   303  UNP    Q976W8   Q976W8_SULTO     1    303             
DBREF  3AIN D    1   303  UNP    Q976W8   Q976W8_SULTO     1    303             
SEQADV 3AIN MET A  -19  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN GLY A  -18  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER A  -17  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER A  -16  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS A  -15  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS A  -14  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS A  -13  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS A  -12  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS A  -11  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS A  -10  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER A   -9  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER A   -8  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN GLY A   -7  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN LEU A   -6  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN VAL A   -5  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN PRO A   -4  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN ARG A   -3  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN GLY A   -2  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER A   -1  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS A    0  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN GLY A  267  UNP  Q976W8    ARG   267 ENGINEERED MUTATION            
SEQADV 3AIN MET B  -19  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN GLY B  -18  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER B  -17  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER B  -16  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS B  -15  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS B  -14  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS B  -13  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS B  -12  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS B  -11  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS B  -10  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER B   -9  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER B   -8  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN GLY B   -7  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN LEU B   -6  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN VAL B   -5  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN PRO B   -4  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN ARG B   -3  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN GLY B   -2  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER B   -1  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS B    0  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN GLY B  267  UNP  Q976W8    ARG   267 ENGINEERED MUTATION            
SEQADV 3AIN MET C  -19  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN GLY C  -18  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER C  -17  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER C  -16  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS C  -15  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS C  -14  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS C  -13  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS C  -12  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS C  -11  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS C  -10  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER C   -9  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER C   -8  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN GLY C   -7  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN LEU C   -6  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN VAL C   -5  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN PRO C   -4  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN ARG C   -3  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN GLY C   -2  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER C   -1  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS C    0  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN GLY C  267  UNP  Q976W8    ARG   267 ENGINEERED MUTATION            
SEQADV 3AIN MET D  -19  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN GLY D  -18  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER D  -17  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER D  -16  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS D  -15  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS D  -14  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS D  -13  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS D  -12  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS D  -11  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS D  -10  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER D   -9  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER D   -8  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN GLY D   -7  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN LEU D   -6  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN VAL D   -5  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN PRO D   -4  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN ARG D   -3  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN GLY D   -2  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN SER D   -1  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN HIS D    0  UNP  Q976W8              EXPRESSION TAG                 
SEQADV 3AIN GLY D  267  UNP  Q976W8    ARG   267 ENGINEERED MUTATION            
SEQRES   1 A  323  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  323  LEU VAL PRO ARG GLY SER HIS MET ILE ASP PRO LYS ILE          
SEQRES   3 A  323  LYS LYS LEU LEU GLU SER THR ILE GLN LEU PRO ILE GLY          
SEQRES   4 A  323  LYS ALA SER VAL GLU GLU ILE ARG SER LEU PHE LYS GLN          
SEQRES   5 A  323  PHE SER SER LEU THR PRO ARG GLU GLU VAL GLY LYS ILE          
SEQRES   6 A  323  GLU ASP ILE THR ILE PRO GLY SER GLU THR ASN ILE LYS          
SEQRES   7 A  323  ALA ARG VAL TYR TYR PRO LYS THR GLN GLY PRO TYR GLY          
SEQRES   8 A  323  VAL LEU VAL TYR TYR HIS GLY GLY GLY PHE VAL LEU GLY          
SEQRES   9 A  323  ASP ILE GLU SER TYR ASP PRO LEU CYS ARG ALA ILE THR          
SEQRES  10 A  323  ASN SER CYS GLN CYS VAL THR ILE SER VAL ASP TYR ARG          
SEQRES  11 A  323  LEU ALA PRO GLU ASN LYS PHE PRO ALA ALA VAL VAL ASP          
SEQRES  12 A  323  SER PHE ASP ALA LEU LYS TRP VAL TYR ASN ASN SER GLU          
SEQRES  13 A  323  LYS PHE ASN GLY LYS TYR GLY ILE ALA VAL GLY GLY ASP          
SEQRES  14 A  323  SER ALA GLY GLY ASN LEU ALA ALA VAL THR ALA ILE LEU          
SEQRES  15 A  323  SER LYS LYS GLU ASN ILE LYS LEU LYS TYR GLN VAL LEU          
SEQRES  16 A  323  ILE TYR PRO ALA VAL SER PHE ASP LEU ILE THR LYS SER          
SEQRES  17 A  323  LEU TYR ASP ASN GLY GLU GLY PHE PHE LEU THR ARG GLU          
SEQRES  18 A  323  HIS ILE ASP TRP PHE GLY GLN GLN TYR LEU ARG SER PHE          
SEQRES  19 A  323  ALA ASP LEU LEU ASP PHE ARG PHE SER PRO ILE LEU ALA          
SEQRES  20 A  323  ASP LEU ASN ASP LEU PRO PRO ALA LEU ILE ILE THR ALA          
SEQRES  21 A  323  GLU HIS ASP PRO LEU ARG ASP GLN GLY GLU ALA TYR ALA          
SEQRES  22 A  323  ASN LYS LEU LEU GLN SER GLY VAL GLN VAL THR SER VAL          
SEQRES  23 A  323  GLY PHE ASN ASN VAL ILE HIS GLY PHE VAL SER PHE PHE          
SEQRES  24 A  323  PRO PHE ILE GLU GLN GLY ARG ASP ALA ILE GLY LEU ILE          
SEQRES  25 A  323  GLY TYR VAL LEU ARG LYS VAL PHE TYR GLY LYS                  
SEQRES   1 B  323  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  323  LEU VAL PRO ARG GLY SER HIS MET ILE ASP PRO LYS ILE          
SEQRES   3 B  323  LYS LYS LEU LEU GLU SER THR ILE GLN LEU PRO ILE GLY          
SEQRES   4 B  323  LYS ALA SER VAL GLU GLU ILE ARG SER LEU PHE LYS GLN          
SEQRES   5 B  323  PHE SER SER LEU THR PRO ARG GLU GLU VAL GLY LYS ILE          
SEQRES   6 B  323  GLU ASP ILE THR ILE PRO GLY SER GLU THR ASN ILE LYS          
SEQRES   7 B  323  ALA ARG VAL TYR TYR PRO LYS THR GLN GLY PRO TYR GLY          
SEQRES   8 B  323  VAL LEU VAL TYR TYR HIS GLY GLY GLY PHE VAL LEU GLY          
SEQRES   9 B  323  ASP ILE GLU SER TYR ASP PRO LEU CYS ARG ALA ILE THR          
SEQRES  10 B  323  ASN SER CYS GLN CYS VAL THR ILE SER VAL ASP TYR ARG          
SEQRES  11 B  323  LEU ALA PRO GLU ASN LYS PHE PRO ALA ALA VAL VAL ASP          
SEQRES  12 B  323  SER PHE ASP ALA LEU LYS TRP VAL TYR ASN ASN SER GLU          
SEQRES  13 B  323  LYS PHE ASN GLY LYS TYR GLY ILE ALA VAL GLY GLY ASP          
SEQRES  14 B  323  SER ALA GLY GLY ASN LEU ALA ALA VAL THR ALA ILE LEU          
SEQRES  15 B  323  SER LYS LYS GLU ASN ILE LYS LEU LYS TYR GLN VAL LEU          
SEQRES  16 B  323  ILE TYR PRO ALA VAL SER PHE ASP LEU ILE THR LYS SER          
SEQRES  17 B  323  LEU TYR ASP ASN GLY GLU GLY PHE PHE LEU THR ARG GLU          
SEQRES  18 B  323  HIS ILE ASP TRP PHE GLY GLN GLN TYR LEU ARG SER PHE          
SEQRES  19 B  323  ALA ASP LEU LEU ASP PHE ARG PHE SER PRO ILE LEU ALA          
SEQRES  20 B  323  ASP LEU ASN ASP LEU PRO PRO ALA LEU ILE ILE THR ALA          
SEQRES  21 B  323  GLU HIS ASP PRO LEU ARG ASP GLN GLY GLU ALA TYR ALA          
SEQRES  22 B  323  ASN LYS LEU LEU GLN SER GLY VAL GLN VAL THR SER VAL          
SEQRES  23 B  323  GLY PHE ASN ASN VAL ILE HIS GLY PHE VAL SER PHE PHE          
SEQRES  24 B  323  PRO PHE ILE GLU GLN GLY ARG ASP ALA ILE GLY LEU ILE          
SEQRES  25 B  323  GLY TYR VAL LEU ARG LYS VAL PHE TYR GLY LYS                  
SEQRES   1 C  323  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  323  LEU VAL PRO ARG GLY SER HIS MET ILE ASP PRO LYS ILE          
SEQRES   3 C  323  LYS LYS LEU LEU GLU SER THR ILE GLN LEU PRO ILE GLY          
SEQRES   4 C  323  LYS ALA SER VAL GLU GLU ILE ARG SER LEU PHE LYS GLN          
SEQRES   5 C  323  PHE SER SER LEU THR PRO ARG GLU GLU VAL GLY LYS ILE          
SEQRES   6 C  323  GLU ASP ILE THR ILE PRO GLY SER GLU THR ASN ILE LYS          
SEQRES   7 C  323  ALA ARG VAL TYR TYR PRO LYS THR GLN GLY PRO TYR GLY          
SEQRES   8 C  323  VAL LEU VAL TYR TYR HIS GLY GLY GLY PHE VAL LEU GLY          
SEQRES   9 C  323  ASP ILE GLU SER TYR ASP PRO LEU CYS ARG ALA ILE THR          
SEQRES  10 C  323  ASN SER CYS GLN CYS VAL THR ILE SER VAL ASP TYR ARG          
SEQRES  11 C  323  LEU ALA PRO GLU ASN LYS PHE PRO ALA ALA VAL VAL ASP          
SEQRES  12 C  323  SER PHE ASP ALA LEU LYS TRP VAL TYR ASN ASN SER GLU          
SEQRES  13 C  323  LYS PHE ASN GLY LYS TYR GLY ILE ALA VAL GLY GLY ASP          
SEQRES  14 C  323  SER ALA GLY GLY ASN LEU ALA ALA VAL THR ALA ILE LEU          
SEQRES  15 C  323  SER LYS LYS GLU ASN ILE LYS LEU LYS TYR GLN VAL LEU          
SEQRES  16 C  323  ILE TYR PRO ALA VAL SER PHE ASP LEU ILE THR LYS SER          
SEQRES  17 C  323  LEU TYR ASP ASN GLY GLU GLY PHE PHE LEU THR ARG GLU          
SEQRES  18 C  323  HIS ILE ASP TRP PHE GLY GLN GLN TYR LEU ARG SER PHE          
SEQRES  19 C  323  ALA ASP LEU LEU ASP PHE ARG PHE SER PRO ILE LEU ALA          
SEQRES  20 C  323  ASP LEU ASN ASP LEU PRO PRO ALA LEU ILE ILE THR ALA          
SEQRES  21 C  323  GLU HIS ASP PRO LEU ARG ASP GLN GLY GLU ALA TYR ALA          
SEQRES  22 C  323  ASN LYS LEU LEU GLN SER GLY VAL GLN VAL THR SER VAL          
SEQRES  23 C  323  GLY PHE ASN ASN VAL ILE HIS GLY PHE VAL SER PHE PHE          
SEQRES  24 C  323  PRO PHE ILE GLU GLN GLY ARG ASP ALA ILE GLY LEU ILE          
SEQRES  25 C  323  GLY TYR VAL LEU ARG LYS VAL PHE TYR GLY LYS                  
SEQRES   1 D  323  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  323  LEU VAL PRO ARG GLY SER HIS MET ILE ASP PRO LYS ILE          
SEQRES   3 D  323  LYS LYS LEU LEU GLU SER THR ILE GLN LEU PRO ILE GLY          
SEQRES   4 D  323  LYS ALA SER VAL GLU GLU ILE ARG SER LEU PHE LYS GLN          
SEQRES   5 D  323  PHE SER SER LEU THR PRO ARG GLU GLU VAL GLY LYS ILE          
SEQRES   6 D  323  GLU ASP ILE THR ILE PRO GLY SER GLU THR ASN ILE LYS          
SEQRES   7 D  323  ALA ARG VAL TYR TYR PRO LYS THR GLN GLY PRO TYR GLY          
SEQRES   8 D  323  VAL LEU VAL TYR TYR HIS GLY GLY GLY PHE VAL LEU GLY          
SEQRES   9 D  323  ASP ILE GLU SER TYR ASP PRO LEU CYS ARG ALA ILE THR          
SEQRES  10 D  323  ASN SER CYS GLN CYS VAL THR ILE SER VAL ASP TYR ARG          
SEQRES  11 D  323  LEU ALA PRO GLU ASN LYS PHE PRO ALA ALA VAL VAL ASP          
SEQRES  12 D  323  SER PHE ASP ALA LEU LYS TRP VAL TYR ASN ASN SER GLU          
SEQRES  13 D  323  LYS PHE ASN GLY LYS TYR GLY ILE ALA VAL GLY GLY ASP          
SEQRES  14 D  323  SER ALA GLY GLY ASN LEU ALA ALA VAL THR ALA ILE LEU          
SEQRES  15 D  323  SER LYS LYS GLU ASN ILE LYS LEU LYS TYR GLN VAL LEU          
SEQRES  16 D  323  ILE TYR PRO ALA VAL SER PHE ASP LEU ILE THR LYS SER          
SEQRES  17 D  323  LEU TYR ASP ASN GLY GLU GLY PHE PHE LEU THR ARG GLU          
SEQRES  18 D  323  HIS ILE ASP TRP PHE GLY GLN GLN TYR LEU ARG SER PHE          
SEQRES  19 D  323  ALA ASP LEU LEU ASP PHE ARG PHE SER PRO ILE LEU ALA          
SEQRES  20 D  323  ASP LEU ASN ASP LEU PRO PRO ALA LEU ILE ILE THR ALA          
SEQRES  21 D  323  GLU HIS ASP PRO LEU ARG ASP GLN GLY GLU ALA TYR ALA          
SEQRES  22 D  323  ASN LYS LEU LEU GLN SER GLY VAL GLN VAL THR SER VAL          
SEQRES  23 D  323  GLY PHE ASN ASN VAL ILE HIS GLY PHE VAL SER PHE PHE          
SEQRES  24 D  323  PRO PHE ILE GLU GLN GLY ARG ASP ALA ILE GLY LEU ILE          
SEQRES  25 D  323  GLY TYR VAL LEU ARG LYS VAL PHE TYR GLY LYS                  
HET    MPD  A 304       8                                                       
HET    PO4  A 305       5                                                       
HET    PO4  A 306       5                                                       
HET    MPD  A 307       8                                                       
HET    MPD  A 308       8                                                       
HET    MPD  B 304       8                                                       
HET    MPD  B 305       8                                                       
HET    MPD  B 306       8                                                       
HET    PO4  B 307       5                                                       
HET    MRD  B 308       8                                                       
HET    MRD  C 304       8                                                       
HET    MRD  C 305       8                                                       
HET    PO4  C 306       5                                                       
HET    MRD  D 304       8                                                       
HET    PO4  D 305       5                                                       
HET    MRD  D 306       8                                                       
HET    MRD  D 307       8                                                       
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     MRD (4R)-2-METHYLPENTANE-2,4-DIOL                                    
FORMUL   5  MPD    6(C6 H14 O2)                                                 
FORMUL   6  PO4    5(O4 P 3-)                                                   
FORMUL  14  MRD    6(C6 H14 O2)                                                 
FORMUL  22  HOH   *755(H2 O)                                                    
HELIX    1   1 SER A   22  SER A   35  1                                  14    
HELIX    2   2 TYR A   89  GLN A  101  1                                  13    
HELIX    3   3 PRO A  118  ASN A  134  1                                  17    
HELIX    4   4 SER A  135  ASN A  139  5                                   5    
HELIX    5   5 SER A  150  GLU A  166  1                                  17    
HELIX    6   6 THR A  186  GLY A  193  1                                   8    
HELIX    7   7 THR A  199  LEU A  211  1                                  13    
HELIX    8   8 SER A  213  ASP A  219  5                                   7    
HELIX    9   9 SER A  223  ALA A  227  5                                   5    
HELIX   10  10 LEU A  245  SER A  259  1                                  15    
HELIX   11  11 GLY A  274  PHE A  279  5                                   6    
HELIX   12  12 ILE A  282  GLY A  302  1                                  21    
HELIX   13  13 SER B   22  SER B   35  1                                  14    
HELIX   14  14 TYR B   89  GLN B  101  1                                  13    
HELIX   15  15 PRO B  118  ASN B  134  1                                  17    
HELIX   16  16 SER B  135  ASN B  139  5                                   5    
HELIX   17  17 SER B  150  GLU B  166  1                                  17    
HELIX   18  18 THR B  186  GLY B  193  1                                   8    
HELIX   19  19 THR B  199  LEU B  211  1                                  13    
HELIX   20  20 SER B  213  ASP B  219  5                                   7    
HELIX   21  21 SER B  223  ALA B  227  5                                   5    
HELIX   22  22 LEU B  245  SER B  259  1                                  15    
HELIX   23  23 GLY B  274  PHE B  279  5                                   6    
HELIX   24  24 ILE B  282  GLY B  302  1                                  21    
HELIX   25  25 SER C   22  SER C   35  1                                  14    
HELIX   26  26 ASP C   85  GLN C  101  1                                  17    
HELIX   27  27 PRO C  118  SER C  135  1                                  18    
HELIX   28  28 GLU C  136  ASN C  139  5                                   4    
HELIX   29  29 SER C  150  GLU C  166  1                                  17    
HELIX   30  30 THR C  186  GLY C  193  1                                   8    
HELIX   31  31 THR C  199  LEU C  211  1                                  13    
HELIX   32  32 SER C  213  ASP C  219  5                                   7    
HELIX   33  33 SER C  223  ALA C  227  5                                   5    
HELIX   34  34 LEU C  245  SER C  259  1                                  15    
HELIX   35  35 GLY C  274  PHE C  279  5                                   6    
HELIX   36  36 ILE C  282  GLY C  302  1                                  21    
HELIX   37  37 SER D   22  SER D   35  1                                  14    
HELIX   38  38 TYR D   89  GLN D  101  1                                  13    
HELIX   39  39 PRO D  118  ASN D  134  1                                  17    
HELIX   40  40 SER D  135  ASN D  139  5                                   5    
HELIX   41  41 SER D  150  GLU D  166  1                                  17    
HELIX   42  42 THR D  186  GLY D  193  1                                   8    
HELIX   43  43 THR D  199  LEU D  211  1                                  13    
HELIX   44  44 SER D  213  ASP D  219  5                                   7    
HELIX   45  45 SER D  223  ALA D  227  5                                   5    
HELIX   46  46 LEU D  245  SER D  259  1                                  15    
HELIX   47  47 GLY D  274  PHE D  279  5                                   6    
HELIX   48  48 ILE D  282  GLY D  302  1                                  21    
SHEET    1   A16 LYS A  44  PRO A  51  0                                        
SHEET    2   A16 ASN A  56  TYR A  63 -1  O  ILE A  57   N  ILE A  50           
SHEET    3   A16 VAL A 103  VAL A 107 -1  O  THR A 104   N  TYR A  62           
SHEET    4   A16 VAL A  72  TYR A  76  1  N  LEU A  73   O  VAL A 103           
SHEET    5   A16 ILE A 144  ASP A 149  1  O  ALA A 145   N  VAL A  74           
SHEET    6   A16 TYR A 172  ILE A 176  1  O  ILE A 176   N  GLY A 148           
SHEET    7   A16 ALA A 235  ALA A 240  1  O  LEU A 236   N  LEU A 175           
SHEET    8   A16 VAL A 263  PHE A 268  1  O  PHE A 268   N  THR A 239           
SHEET    9   A16 VAL D 263  ILE D 272 -1  O  GLY D 267   N  GLY A 267           
SHEET   10   A16 ALA D 235  HIS D 242  1  N  THR D 239   O  PHE D 268           
SHEET   11   A16 TYR D 172  ILE D 176  1  N  LEU D 175   O  LEU D 236           
SHEET   12   A16 GLY D 143  ASP D 149  1  N  GLY D 148   O  ILE D 176           
SHEET   13   A16 GLY D  71  TYR D  76  1  N  VAL D  74   O  ALA D 145           
SHEET   14   A16 VAL D 103  VAL D 107  1  O  VAL D 103   N  LEU D  73           
SHEET   15   A16 ASN D  56  TYR D  63 -1  N  TYR D  62   O  THR D 104           
SHEET   16   A16 LYS D  44  PRO D  51 -1  N  GLU D  46   O  VAL D  61           
SHEET    1   B16 LYS B  44  PRO B  51  0                                        
SHEET    2   B16 ASN B  56  TYR B  63 -1  O  ILE B  57   N  ILE B  50           
SHEET    3   B16 VAL B 103  VAL B 107 -1  O  THR B 104   N  TYR B  62           
SHEET    4   B16 GLY B  71  TYR B  76  1  N  LEU B  73   O  VAL B 103           
SHEET    5   B16 GLY B 143  ASP B 149  1  O  ALA B 145   N  VAL B  72           
SHEET    6   B16 TYR B 172  ILE B 176  1  O  ILE B 176   N  GLY B 148           
SHEET    7   B16 ALA B 235  HIS B 242  1  O  LEU B 236   N  LEU B 175           
SHEET    8   B16 VAL B 263  ILE B 272  1  O  PHE B 268   N  THR B 239           
SHEET    9   B16 VAL C 263  ILE C 272 -1  O  GLY C 267   N  GLY B 267           
SHEET   10   B16 ALA C 235  HIS C 242  1  N  THR C 239   O  PHE C 268           
SHEET   11   B16 TYR C 172  ILE C 176  1  N  LEU C 175   O  LEU C 236           
SHEET   12   B16 ILE C 144  ASP C 149  1  N  GLY C 148   O  ILE C 176           
SHEET   13   B16 VAL C  72  TYR C  76  1  N  VAL C  72   O  ALA C 145           
SHEET   14   B16 VAL C 103  VAL C 107  1  O  VAL C 103   N  LEU C  73           
SHEET   15   B16 ASN C  56  TYR C  63 -1  N  TYR C  62   O  THR C 104           
SHEET   16   B16 LYS C  44  PRO C  51 -1  N  GLU C  46   O  VAL C  61           
SSBOND   1 CYS A  100    CYS A  102                          1555   1555  2.11  
SSBOND   2 CYS B  100    CYS B  102                          1555   1555  2.10  
SSBOND   3 CYS D  100    CYS D  102                          1555   1555  2.09  
CISPEP   1 GLY A   68    PRO A   69          0         9.92                     
CISPEP   2 ALA A  112    PRO A  113          0        -1.37                     
CISPEP   3 PHE A  117    PRO A  118          0         0.37                     
CISPEP   4 GLY B   68    PRO B   69          0        10.32                     
CISPEP   5 ALA B  112    PRO B  113          0         5.66                     
CISPEP   6 PHE B  117    PRO B  118          0        10.03                     
CISPEP   7 GLY C   68    PRO C   69          0         5.58                     
CISPEP   8 ALA C  112    PRO C  113          0        10.41                     
CISPEP   9 PHE C  117    PRO C  118          0         1.67                     
CISPEP  10 GLY D   68    PRO D   69          0         1.39                     
CISPEP  11 ALA D  112    PRO D  113          0         6.72                     
CISPEP  12 PHE D  117    PRO D  118          0         5.70                     
SITE     1 AC1  5 PHE A  81  ALA A 151  ALA A 179  GLY A 207                    
SITE     2 AC1  5 HOH A 324                                                     
SITE     1 AC2  4 PHE A  30  GLY A  79  TYR A  89  HOH A 389                    
SITE     1 AC3  4 ARG A 212  ARG A 221  HOH A 414  HOH A 602                    
SITE     1 AC4  5 PHE A 182  LEU A 217  HOH A 406  HOH A 650                    
SITE     2 AC4  5 SER B 181                                                     
SITE     1 AC5  2 GLY A 207  GLN A 208                                          
SITE     1 AC6  5 PHE B  81  ALA B 151  ALA B 179  GLY B 207                    
SITE     2 AC6  5 HOH B 719                                                     
SITE     1 AC7  7 SER B  34  THR B  37  SER B  88  TYR B  89                    
SITE     2 AC7  7 PRO B  91  LEU B  92  SER B 277                               
SITE     1 AC8  6 PHE B  30  GLY B  79  TYR B  89  HIS B 273                    
SITE     2 AC8  6 SER B 277  HOH B 350                                          
SITE     1 AC9  4 ARG B 212  ARG B 221  HOH B 433  HOH B 659                    
SITE     1 BC1  5 ARG B 110  LEU B 111  ASN B 115  HOH B 326                    
SITE     2 BC1  5 HOH B 404                                                     
SITE     1 BC2  6 PHE C  81  ALA C 151  ALA C 179  GLY C 207                    
SITE     2 BC2  6 LEU C 245  HOH C 328                                          
SITE     1 BC3  3 GLY C 207  GLN C 208  SER C 213                               
SITE     1 BC4  2 ARG C 212  ARG C 221                                          
SITE     1 BC5  6 PHE D  81  ALA D 151  ALA D 179  GLY D 207                    
SITE     2 BC5  6 LEU D 245  HOH D 308                                          
SITE     1 BC6  2 ARG D 212  ARG D 221                                          
SITE     1 BC7  4 GLY D 207  GLN D 208  SER D 213  HOH D 647                    
SITE     1 BC8  6 LEU C 217  HOH C 645  PHE D 182  HOH D 386                    
SITE     2 BC8  6 HOH D 391  HOH D 600                                          
CRYST1   76.370  114.953  102.064  90.00 109.55  90.00 P 1 21 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      0.013094  0.000000  0.004650        0.00000                         
SCALE2      0.000000  0.008699  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010397        0.00000                         
TER    2231      LYS A 303                                                      
TER    4462      LYS B 303                                                      
TER    6693      LYS C 303                                                      
TER    8924      LYS D 303                                                      
MASTER      623    0   17   48   32    0   26    6 9796    4  127  100          
END                                                                             

Send your questions or comments to :
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.
For technical information about these pages see:
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