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Database: PDB
Entry: 3SFX
LinkDB: 3SFX
Original site: 3SFX 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       14-JUN-11   3SFX              
TITLE     CRYPTOCOCCUS NEOFORMANS PROTEIN FARNESYLTRANSFERASE IN COMPLEX WITH   
TITLE    2 FPT-II AND TIPIFARNIB                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CRYPTOCOCCUS NEOFORMANS PROTEIN FARNESYLTRANSFERASE ALPHA  
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A;                                                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CRYPTOCOCCUS NEOFORMANS PROTEIN FARNESYLTRANSFERASE BETA   
COMPND   8 SUBUNIT;                                                             
COMPND   9 CHAIN: B;                                                            
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CRYPTOCOCCUS NEOFORMANS;                        
SOURCE   3 ORGANISM_TAXID: 235443;                                              
SOURCE   4 STRAIN: H99;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: CRYPTOCOCCUS NEOFORMANS;                        
SOURCE   9 ORGANISM_TAXID: 235443;                                              
SOURCE  10 STRAIN: H99;                                                         
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PRENYLTRANSFERASE, PROTEIN FARNESYLTRANSFERASE, TRANSFERASE-          
KEYWDS   2 TRANSFERASE INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.HAST,L.S.BEESE                                                    
REVDAT   3   28-FEB-24 3SFX    1       REMARK LINK                              
REVDAT   2   19-OCT-11 3SFX    1       JRNL                                     
REVDAT   1   03-AUG-11 3SFX    0                                                
JRNL        AUTH   M.A.HAST,C.B.NICHOLS,S.M.ARMSTRONG,S.M.KELLY,H.W.HELLINGA,   
JRNL        AUTH 2 J.A.ALSPAUGH,L.S.BEESE                                       
JRNL        TITL   STRUCTURES OF CRYPTOCOCCUS NEOFORMANS PROTEIN                
JRNL        TITL 2 FARNESYLTRANSFERASE REVEAL STRATEGIES FOR DEVELOPING         
JRNL        TITL 3 INHIBITORS THAT TARGET FUNGAL PATHOGENS.                     
JRNL        REF    J.BIOL.CHEM.                  V. 286 35149 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21816822                                                     
JRNL        DOI    10.1074/JBC.M111.250506                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.47                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 85314                          
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4538                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6207                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.51                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2550                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 338                          
REMARK   3   BIN FREE R VALUE                    : 0.2740                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6346                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 109                                     
REMARK   3   SOLVENT ATOMS            : 669                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.74                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
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): 0.117         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.079         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.162         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6638 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9029 ; 1.264 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   796 ; 5.338 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   302 ;33.429 ;23.377       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1050 ;14.239 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    47 ;15.035 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   961 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5097 ; 0.006 ; 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):  3997 ; 0.591 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6448 ; 1.121 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2641 ; 1.797 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2580 ; 2.924 ; 4.500       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     5        A   334                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.5823 -30.3482   8.3903              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0543 T22:   0.0521                                     
REMARK   3      T33:   0.0978 T12:  -0.0310                                     
REMARK   3      T13:  -0.0195 T23:  -0.0042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3164 L22:   0.9693                                     
REMARK   3      L33:   1.2698 L12:   0.0604                                     
REMARK   3      L13:  -0.0029 L23:  -0.1505                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0031 S12:  -0.0905 S13:   0.0338                       
REMARK   3      S21:   0.1054 S22:  -0.0279 S23:  -0.0891                       
REMARK   3      S31:  -0.1148 S32:   0.1506 S33:   0.0247                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B   519                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.0698 -32.1147 -10.3360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0245 T22:   0.0207                                     
REMARK   3      T33:   0.0718 T12:  -0.0190                                     
REMARK   3      T13:  -0.0006 T23:   0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5237 L22:   0.5538                                     
REMARK   3      L33:   1.3945 L12:   0.1161                                     
REMARK   3      L13:   0.0326 L23:  -0.1617                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0113 S12:  -0.0099 S13:   0.0197                       
REMARK   3      S21:  -0.0497 S22:   0.0057 S23:   0.0097                       
REMARK   3      S31:   0.0080 S32:  -0.0614 S33:   0.0056                       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3SFX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000066154.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-MAY-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 12.3.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.11                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 85314                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> 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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4K, CAPSO PH 9.5, LITHIUM SULFATE,    
REMARK 280  SODIUM CHLORIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       65.04800            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       71.08800            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       71.08800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       97.57200            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       71.08800            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       71.08800            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       32.52400            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       71.08800            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       71.08800            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       97.57200            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       71.08800            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       71.08800            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       32.52400            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       65.04800            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -105.0 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 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 B2738  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   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     GLN A    -1                                                      
REMARK 465     LEU A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     SER A   258                                                      
REMARK 465     LYS A   259                                                      
REMARK 465     LEU A   260                                                      
REMARK 465     ASN A   261                                                      
REMARK 465     PRO A   262                                                      
REMARK 465     ASP A   263                                                      
REMARK 465     ILE A   264                                                      
REMARK 465     GLU A   265                                                      
REMARK 465     THR A   266                                                      
REMARK 465     VAL A   267                                                      
REMARK 465     GLU A   268                                                      
REMARK 465     ALA A   269                                                      
REMARK 465     PHE A   270                                                      
REMARK 465     GLY A   271                                                      
REMARK 465     ASP A   277                                                      
REMARK 465     GLU A   335                                                      
REMARK 465     GLU A   336                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B   243                                                      
REMARK 465     VAL B   244                                                      
REMARK 465     VAL B   245                                                      
REMARK 465     PRO B   246                                                      
REMARK 465     SER B   247                                                      
REMARK 465     THR B   248                                                      
REMARK 465     SER B   249                                                      
REMARK 465     ALA B   250                                                      
REMARK 465     PHE B   251                                                      
REMARK 465     PRO B   252                                                      
REMARK 465     THR B   253                                                      
REMARK 465     SER B   254                                                      
REMARK 465     LYS B   350                                                      
REMARK 465     LYS B   351                                                      
REMARK 465     SER B   352                                                      
REMARK 465     ARG B   353                                                      
REMARK 465     ILE B   354                                                      
REMARK 465     GLU B   355                                                      
REMARK 465     VAL B   356                                                      
REMARK 465     PHE B   357                                                      
REMARK 465     GLU B   358                                                      
REMARK 465     GLU B   359                                                      
REMARK 465     GLU B   360                                                      
REMARK 465     LYS B   361                                                      
REMARK 465     GLU B   362                                                      
REMARK 465     GLY B   363                                                      
REMARK 465     ASP B   364                                                      
REMARK 465     TRP B   365                                                      
REMARK 465     GLU B   366                                                      
REMARK 465     ASP B   367                                                      
REMARK 465     VAL B   368                                                      
REMARK 465     PRO B   369                                                      
REMARK 465     PRO B   370                                                      
REMARK 465     ASN B   520                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1889     O    HOH A  2912     8555     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B 315   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG B 315   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 DEGREES          
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    VAL A  31       47.06     35.71                                   
REMARK 500    VAL A 198      -58.25   -121.90                                   
REMARK 500    GLU A 317      -55.89   -126.24                                   
REMARK 500    VAL B  51       67.42    -68.87                                   
REMARK 500    SER B  52      107.30    -54.49                                   
REMARK 500    GLN B  76      119.92   -173.14                                   
REMARK 500    ASN B 219       -5.94     69.82                                   
REMARK 500    ALA B 263     -169.43   -170.87                                   
REMARK 500    SER B 394     -136.69   -127.45                                   
REMARK 500    VAL B 500      -56.09     75.35                                   
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 B 521  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 323   OD2                                                    
REMARK 620 2 ASP B 323   OD1  54.4                                              
REMARK 620 3 CYS B 325   SG  105.6  89.6                                        
REMARK 620 4 HIS B 410   NE2 124.9  91.9 117.6                                  
REMARK 620 5 JAN B 526   N2  101.6 156.0  98.2 104.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 521                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3FX B 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3FX B 523                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3FX B 524                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FII B 525                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JAN B 526                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 527                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3Q73   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3Q75   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3Q78   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3Q79   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3Q7A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3Q7F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3SFY   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 THERE IS NO UNIPORT DATABASE REFERENCE SEQUENCE AVAILABLE AT THE     
REMARK 999 TIME OF THE DEPOSITION. THE SEQUENCES PRESENTED HERE ARE OF          
REMARK 999 FARNESYLTRANSFERASE ALPHA SUBUNIT(RESIDUES 15-349) AND BETA          
REMARK 999 SUBUNIT FROM CRYPTOCOCCUS NEOFORMANS VAR. GRUBII STRAIN H99. THE     
REMARK 999 FIRST 14 RESIDUES IN THE ALPHA SUBUNIT(CHAIN A) REPRESENT            
REMARK 999 EXPRESSION TAG.                                                      
DBREF  3SFX A  -12   336  PDB    3SFX     3SFX           -12    336             
DBREF  3SFX B    1   520  PDB    3SFX     3SFX             1    520             
SEQRES   1 A  349  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN LEU          
SEQRES   2 A  349  MET VAL THR SER THR TYR ILE PRO MET SER GLN ARG ARG          
SEQRES   3 A  349  SER TRP ALA ASP VAL LYS PRO ILE MET GLN ASP ASP GLY          
SEQRES   4 A  349  PRO ASN PRO VAL VAL PRO ILE MET TYR SER GLU GLU TYR          
SEQRES   5 A  349  LYS ASP ALA MET ASP TYR PHE ARG ALA ILE ALA ALA LYS          
SEQRES   6 A  349  GLU GLU LYS SER GLU ARG ALA LEU GLU LEU THR GLU ILE          
SEQRES   7 A  349  ILE VAL ARG MET ASN PRO ALA HIS TYR THR VAL TRP GLN          
SEQRES   8 A  349  TYR ARG PHE SER LEU LEU THR SER LEU ASN LYS SER LEU          
SEQRES   9 A  349  GLU ASP GLU LEU ARG LEU MET ASN GLU PHE ALA VAL GLN          
SEQRES  10 A  349  ASN LEU LYS SER TYR GLN VAL TRP HIS HIS ARG LEU LEU          
SEQRES  11 A  349  LEU LEU ASP ARG ILE SER PRO GLN ASP PRO VAL SER GLU          
SEQRES  12 A  349  ILE GLU TYR ILE HIS GLY SER LEU LEU PRO ASP PRO LYS          
SEQRES  13 A  349  ASN TYR HIS THR TRP ALA TYR LEU HIS TRP LEU TYR SER          
SEQRES  14 A  349  HIS PHE SER THR LEU GLY ARG ILE SER GLU ALA GLN TRP          
SEQRES  15 A  349  GLY SER GLU LEU ASP TRP CYS ASN GLU MET LEU ARG VAL          
SEQRES  16 A  349  ASP GLY ARG ASN ASN SER ALA TRP GLY TRP ARG TRP TYR          
SEQRES  17 A  349  LEU ARG VAL SER ARG PRO GLY ALA GLU THR SER SER ARG          
SEQRES  18 A  349  SER LEU GLN ASP GLU LEU ILE TYR ILE LEU LYS SER ILE          
SEQRES  19 A  349  HIS LEU ILE PRO HIS ASN VAL SER ALA TRP ASN TYR LEU          
SEQRES  20 A  349  ARG GLY PHE LEU LYS HIS PHE SER LEU PRO LEU VAL PRO          
SEQRES  21 A  349  ILE LEU PRO ALA ILE LEU PRO TYR THR ALA SER LYS LEU          
SEQRES  22 A  349  ASN PRO ASP ILE GLU THR VAL GLU ALA PHE GLY PHE PRO          
SEQRES  23 A  349  MET PRO SER ASP PRO LEU PRO GLU ASP THR PRO LEU PRO          
SEQRES  24 A  349  VAL PRO LEU ALA LEU GLU TYR LEU ALA ASP SER PHE ILE          
SEQRES  25 A  349  GLU GLN ASN ARG VAL ASP ASP ALA ALA LYS VAL PHE GLU          
SEQRES  26 A  349  LYS LEU SER SER GLU TYR ASP GLN MET ARG ALA GLY TYR          
SEQRES  27 A  349  TRP GLU PHE ARG ARG ARG GLU CYS ALA GLU GLU                  
SEQRES   1 B  520  MET ALA THR GLU PHE THR PRO SER VAL TYR SER LEU VAL          
SEQRES   2 B  520  SER LYS PRO LEU PRO SER ASN SER ARG PRO SER ALA THR          
SEQRES   3 B  520  LEU ASP GLU GLN ALA GLU THR GLU ASP LEU ILE SER GLN          
SEQRES   4 B  520  LEU PHE ASP LEU THR ALA ASP PRO ASN ALA LEU VAL SER          
SEQRES   5 B  520  GLU HIS GLY LYS ARG TYR SER GLY LEU ARG LYS GLN GLU          
SEQRES   6 B  520  HIS THR GLN PHE LEU ALA SER SER PHE PHE GLN LEU PRO          
SEQRES   7 B  520  GLY LYS PHE VAL SER LEU ASP ALA SER ARG PRO TRP LEU          
SEQRES   8 B  520  VAL PHE TRP THR VAL HIS SER LEU ASP LEU LEU GLY VAL          
SEQRES   9 B  520  ALA LEU ASP GLN GLY THR LYS ASP ARG VAL VAL SER THR          
SEQRES  10 B  520  LEU LEU HIS PHE LEU SER PRO LYS GLY GLY PHE GLY GLY          
SEQRES  11 B  520  GLY PRO ALA ASN SER GLN ILE PRO HIS LEU LEU PRO THR          
SEQRES  12 B  520  TYR ALA SER VAL CYS SER LEU ALA ILE ALA GLY ASN ASP          
SEQRES  13 B  520  SER SER THR GLY GLY TRP LYS ASP LEU ALA ALA ALA ARG          
SEQRES  14 B  520  GLN SER ILE TYR GLU PHE PHE MET ARG CYS LYS ARG PRO          
SEQRES  15 B  520  ASP GLY GLY PHE VAL VAL CYS GLU GLY GLY GLU VAL ASP          
SEQRES  16 B  520  VAL ARG GLY THR TYR CYS LEU LEU VAL VAL ALA THR LEU          
SEQRES  17 B  520  LEU ASP ILE ILE THR PRO GLU LEU LEU HIS ASN VAL ASP          
SEQRES  18 B  520  LYS PHE VAL SER ALA CYS GLN THR TYR GLU GLY GLY PHE          
SEQRES  19 B  520  ALA CYS ALA SER PHE PRO PHE PRO SER VAL VAL PRO SER          
SEQRES  20 B  520  THR SER ALA PHE PRO THR SER GLU PRO SER CYS ARG VAL          
SEQRES  21 B  520  SER MET ALA GLU ALA HIS GLY GLY TYR THR SER CYS SER          
SEQRES  22 B  520  LEU ASN SER HIS PHE LEU LEU THR SER VAL PRO LEU PRO          
SEQRES  23 B  520  SER PHE PRO LEU SER ILE ASP ALA ASN ALA ALA LEU ARG          
SEQRES  24 B  520  TRP THR VAL LEU GLN GLN GLY GLU PRO ILE GLU GLY GLY          
SEQRES  25 B  520  GLY PHE ARG GLY ARG THR ASN LYS LEU VAL ASP GLY CYS          
SEQRES  26 B  520  TYR SER TRP TRP VAL GLY GLY GLY ALA PRO VAL ALA GLU          
SEQRES  27 B  520  GLU LEU VAL ARG ARG GLU LYS SER ARG LYS VAL LYS LYS          
SEQRES  28 B  520  SER ARG ILE GLU VAL PHE GLU GLU GLU LYS GLU GLY ASP          
SEQRES  29 B  520  TRP GLU ASP VAL PRO PRO ILE PRO PRO ILE PHE ASN ARG          
SEQRES  30 B  520  VAL ALA LEU GLN GLU PHE THR LEU VAL ALA ALA GLN GLN          
SEQRES  31 B  520  ASP PRO GLY SER THR GLY GLY LEU ARG ASP LYS PRO GLY          
SEQRES  32 B  520  LYS ARG PRO ASP GLN TYR HIS THR CYS ASN ASN LEU SER          
SEQRES  33 B  520  GLY LEU SER ILE ALA GLN HIS LYS MET SER HIS SER PRO          
SEQRES  34 B  520  SER THR VAL SER SER ASN ARG LEU LYS PHE ASP ALA SER          
SEQRES  35 B  520  LYS GLY LEU PRO ALA VAL LYS PRO VAL ALA PRO GLY GLY          
SEQRES  36 B  520  GLY TRP LYS ASN GLU ASP GLU ARG GLN ASN ALA ARG ARG          
SEQRES  37 B  520  GLU ILE TRP ALA ASN ALA LEU GLY TRP ILE GLU GLU GLU          
SEQRES  38 B  520  GLY GLY GLU ILE ILE VAL GLY GLY LYS ASP ASN ARG ILE          
SEQRES  39 B  520  ASN THR THR THR PRO VAL PHE ASN ILE LEU GLY LEU ARG          
SEQRES  40 B  520  LEU LYS PRO PHE ILE ASN TYR PHE TYR CYS GLN GLU ASN          
HET     ZN  B 521       1                                                       
HET    3FX  B 522      15                                                       
HET    3FX  B 523      15                                                       
HET    3FX  B 524      15                                                       
HET    FII  B 525      24                                                       
HET    JAN  B 526      34                                                       
HET    SO4  B 527       5                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     3FX (2R)-3-(CYCLOHEXYLAMINO)-2-HYDROXYPROPANE-1-SULFONIC             
HETNAM   2 3FX  ACID                                                            
HETNAM     FII [(3,7,11-TRIMETHYL-DODECA-2,6,10-TRIENYLOXYCARBAMOYL)-           
HETNAM   2 FII  METHYL]-PHOSPHONIC ACID                                         
HETNAM     JAN 6-[(S)-AMINO(4-CHLOROPHENYL)(1-METHYL-1H-IMIDAZOL-5-             
HETNAM   2 JAN  YL)METHYL]-4-(3-CHLOROPHENYL)-1-METHYLQUINOLIN-2(1H)-           
HETNAM   3 JAN  ONE                                                             
HETNAM     SO4 SULFATE ION                                                      
HETSYN     FII FPP ANALOG                                                       
HETSYN     JAN R115777; TIPIFARNIB                                              
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4  3FX    3(C9 H19 N O4 S)                                             
FORMUL   7  FII    C17 H30 N O5 P                                               
FORMUL   8  JAN    C27 H22 CL2 N4 O                                             
FORMUL   9  SO4    O4 S 2-                                                      
FORMUL  10  HOH   *669(H2 O)                                                    
HELIX    1   1 PRO A    8  ALA A   16  5                                   9    
HELIX    2   2 SER A   36  LYS A   52  1                                  17    
HELIX    3   3 SER A   56  ASN A   70  1                                  15    
HELIX    4   4 HIS A   73  LEU A   87  1                                  15    
HELIX    5   5 SER A   90  GLN A  104  1                                  15    
HELIX    6   6 SER A  108  SER A  123  1                                  16    
HELIX    7   7 PRO A  127  LEU A  139  1                                  13    
HELIX    8   8 ASN A  144  LEU A  161  1                                  18    
HELIX    9   9 SER A  165  ASP A  183  1                                  19    
HELIX   10  10 ASN A  186  VAL A  198  1                                  13    
HELIX   11  11 SER A  206  ILE A  224  1                                  19    
HELIX   12  12 ASN A  227  PHE A  241  1                                  15    
HELIX   13  13 LEU A  245  PRO A  247  5                                   3    
HELIX   14  14 ILE A  248  LEU A  253  1                                   6    
HELIX   15  15 PRO A  254  THR A  256  5                                   3    
HELIX   16  16 VAL A  287  GLN A  301  1                                  15    
HELIX   17  17 ARG A  303  GLU A  317  1                                  15    
HELIX   18  18 ASP A  319  MET A  321  5                                   3    
HELIX   19  19 ARG A  322  ALA A  334  1                                  13    
HELIX   20  20 SER B    8  LEU B   12  5                                   5    
HELIX   21  21 SER B   24  THR B   44  1                                  21    
HELIX   22  22 ARG B   62  GLN B   76  1                                  15    
HELIX   23  23 PRO B   78  ASP B   85  5                                   8    
HELIX   24  24 SER B   87  GLY B  103  1                                  17    
HELIX   25  25 ASP B  107  HIS B  120  1                                  14    
HELIX   26  26 HIS B  139  GLY B  154  1                                  16    
HELIX   27  27 GLY B  161  ALA B  168  1                                   8    
HELIX   28  28 ALA B  168  LYS B  180  1                                  13    
HELIX   29  29 ASP B  195  ASP B  210  1                                  16    
HELIX   30  30 THR B  213  HIS B  218  1                                   6    
HELIX   31  31 ASN B  219  CYS B  227  1                                   9    
HELIX   32  32 HIS B  266  SER B  282  1                                  17    
HELIX   33  33 ASP B  293  GLN B  304  1                                  12    
HELIX   34  34 GLU B  307  GLY B  311  5                                   5    
HELIX   35  35 CYS B  325  VAL B  330  1                                   6    
HELIX   36  36 GLY B  333  VAL B  349  1                                  17    
HELIX   37  37 ASN B  376  ALA B  387  1                                  12    
HELIX   38  38 ASP B  407  HIS B  423  1                                  17    
HELIX   39  39 SER B  428  PHE B  439  1                                  12    
HELIX   40  40 ASN B  459  LEU B  475  1                                  17    
HELIX   41  41 GLY B  489  ARG B  493  5                                   5    
HELIX   42  42 LEU B  504  TYR B  516  1                                  13    
SHEET    1   A 2 SER B 238  PHE B 241  0                                        
SHEET    2   A 2 CYS B 258  SER B 261 -1  O  VAL B 260   N  PHE B 239           
SHEET    1   B 2 MET B 425  HIS B 427  0                                        
SHEET    2   B 2 TRP B 477  GLU B 479 -1  O  ILE B 478   N  SER B 426           
LINK         OD2 ASP B 323                ZN    ZN B 521     1555   1555  2.05  
LINK         OD1 ASP B 323                ZN    ZN B 521     1555   1555  2.61  
LINK         SG  CYS B 325                ZN    ZN B 521     1555   1555  2.30  
LINK         NE2 HIS B 410                ZN    ZN B 521     1555   1555  2.10  
LINK        ZN    ZN B 521                 N2  JAN B 526     1555   1555  2.18  
CISPEP   1 LEU A  285    PRO A  286          0        -1.33                     
CISPEP   2 PHE B  288    PRO B  289          0        -1.93                     
SITE     1 AC1  4 ASP B 323  CYS B 325  HIS B 410  JAN B 526                    
SITE     1 AC2 10 TYR B  58  ASP B 100  GLY B 489  LYS B 490                    
SITE     2 AC2 10 ASP B 491  ARG B 493  ASN B 495  HOH B1774                    
SITE     3 AC2 10 HOH B1900  HOH B2460                                          
SITE     1 AC3 10 ARG B  62  LYS B  63  GLN B  64  GLU B  65                    
SITE     2 AC3 10 PHE B  74  PHE B  75  HOH B1877  HOH B1972                    
SITE     3 AC3 10 HOH B1994  HOH B2102                                          
SITE     1 AC4  7 SER B 123  PRO B 124  LYS B 125  ALA B 133                    
SITE     2 AC4  7 ASN B 134  SER B 135  GLN B 136                               
SITE     1 AC5 17 HOH A2096  TRP B  90  LEU B 141  ARG B 197                    
SITE     2 AC5 17 HIS B 266  GLY B 268  TYR B 269  CYS B 272                    
SITE     3 AC5 17 ARG B 317  LYS B 320  TYR B 326  TRP B 329                    
SITE     4 AC5 17 JAN B 526  HOH B2087  HOH B2092  HOH B2101                    
SITE     5 AC5 17 HOH B2547                                                     
SITE     1 AC6 14 LEU B  84  TRP B  94  ARG B 197  ASP B 323                    
SITE     2 AC6 14 CYS B 325  TYR B 326  ASP B 407  TYR B 409                    
SITE     3 AC6 14 HIS B 410   ZN B 521  FII B 525  HOH B2588                    
SITE     4 AC6 14 HOH B2773  HOH B2869                                          
SITE     1 AC7  8 TYR A  74  ALA B  86  SER B  87  TRP B  90                    
SITE     2 AC7  8 HIS B 139  LEU B 141  PRO B 142  HOH B2111                    
CRYST1  142.176  142.176  130.096  90.00  90.00  90.00 P 43 21 2     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      0.007034  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007034  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007687        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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