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Database: PDB
Entry: 4A0C
LinkDB: 4A0C
Original site: 4A0C 
HEADER    CELL CYCLE                              08-SEP-11   4A0C              
TITLE     STRUCTURE OF THE CAND1-CUL4B-RBX1 COMPLEX                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CULLIN-ASSOCIATED NEDD8-DISSOCIATED PROTEIN 1;             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CULLIN-ASSOCIATED AND NEDDYLATION-DISSOCIATED PROTEIN 1,    
COMPND   5 TBP-INTERACTING PROTEIN OF 120 KDA A, TBP-INTERACTING PROTEIN 120A,  
COMPND   6 P120 CAND1;                                                          
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CULLIN-4B;                                                 
COMPND  10 CHAIN: C, E;                                                         
COMPND  11 SYNONYM: CUL-4B;                                                     
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RBX1;                          
COMPND  15 CHAIN: D, F;                                                         
COMPND  16 SYNONYM: RING FINGER PROTEIN 75, RING-BOX PROTEIN 1, RBX1;           
COMPND  17 EC: 6.3.2.-;                                                         
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DERIVED;                         
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  16 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DERIVED;                         
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  23 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  24 ORGANISM_TAXID: 10090;                                               
SOURCE  25 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  26 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  28 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DERIVED                          
KEYWDS    TRANSCRIPTION, LIGASE, UBIQUITIN, CELL CYCLE, DNA DAMAGE REPAIR       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.SCRIMA,E.S.FISCHER,M.FATY,H.GUT,N.H.THOMA                           
REVDAT   4   03-APR-19 4A0C    1       SOURCE                                   
REVDAT   3   23-AUG-17 4A0C    1       REMARK                                   
REVDAT   2   07-DEC-11 4A0C    1       JRNL                                     
REVDAT   1   30-NOV-11 4A0C    0                                                
JRNL        AUTH   A.SCRIMA,E.S.FISCHER,S.IWAI,H.GUT,N.H.THOMA                  
JRNL        TITL   THE MOLECULAR BASIS OF CRL4(DDB2/CSA) UBIQUITIN LIGASE       
JRNL        TITL 2 ARCHITECTURE, TARGETING, AND ACTIVATION                      
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 147  1024 2011              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   22118460                                                     
JRNL        DOI    10.1016/J.CELL.2011.10.035                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 3.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 56857                          
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) : 0.242                           
REMARK   3   R VALUE            (WORKING SET) : 0.238                           
REMARK   3   FREE R VALUE                     : 0.319                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2993                            
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) : 3.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4140                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3250                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 218                          
REMARK   3   BIN FREE R VALUE                    : 0.3670                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 30798                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 128.5                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.10000                                              
REMARK   3    B22 (A**2) : -0.61000                                             
REMARK   3    B33 (A**2) : -0.51000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.73000                                              
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): 0.906         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.797         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 56.264        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.929                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.882                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 31305 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 42261 ; 1.139 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3846 ; 5.789 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1363 ;39.151 ;24.703       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  6034 ;21.222 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   182 ;17.625 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4945 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 22755 ; 0.004 ; 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): 19308 ; 0.291 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31334 ; 0.532 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 11997 ; 0.362 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 10927 ; 0.669 ; 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  : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.U VALUES REFINED INDIVIDUALLY.                            
REMARK   4                                                                      
REMARK   4 4A0C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-SEP-11.                  
REMARK 100 THE DEPOSITION ID IS D_1290049578.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUL-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59850                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
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: PDB ENTRIES 1U6G, 2HYE                               
REMARK 200                                                                      
REMARK 200 REMARK: CAND1 USED AS MODEL FROM 1U6G, CUL4B MODEL GENERATED USING   
REMARK 200  MODELLER BASED ON CUL4A FROM 2HYE                                   
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.3, 30% PEG 200, 2% PEG   
REMARK 280  8000.                                                               
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       76.18000            
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                                                    
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12430 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 85930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, F                               
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12350 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 86780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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   -22                                                      
REMARK 465     ALA A   -21                                                      
REMARK 465     SER A   -20                                                      
REMARK 465     TRP A   -19                                                      
REMARK 465     SER A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     PRO A   -16                                                      
REMARK 465     GLN A   -15                                                      
REMARK 465     PHE A   -14                                                      
REMARK 465     GLU A   -13                                                      
REMARK 465     LYS A   -12                                                      
REMARK 465     VAL A   -11                                                      
REMARK 465     ASP A   -10                                                      
REMARK 465     GLU A    -9                                                      
REMARK 465     ASN A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     TYR A    -6                                                      
REMARK 465     PHE A    -5                                                      
REMARK 465     GLN A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ARG A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     PRO A   119                                                      
REMARK 465     ALA A   120                                                      
REMARK 465     SER A   121                                                      
REMARK 465     SER A   122                                                      
REMARK 465     GLY A   123                                                      
REMARK 465     ASP A   308                                                      
REMARK 465     PRO A   309                                                      
REMARK 465     ASN A   310                                                      
REMARK 465     TYR A   311                                                      
REMARK 465     ASN A   312                                                      
REMARK 465     TYR A   313                                                      
REMARK 465     ASP A   314                                                      
REMARK 465     ASP A   315                                                      
REMARK 465     GLU A   316                                                      
REMARK 465     ASP A   317                                                      
REMARK 465     GLU A   318                                                      
REMARK 465     ASP A   319                                                      
REMARK 465     GLU A   320                                                      
REMARK 465     ASN A   321                                                      
REMARK 465     ALA A   322                                                      
REMARK 465     MET A   323                                                      
REMARK 465     ASP A   324                                                      
REMARK 465     ALA A   325                                                      
REMARK 465     ASP A   326                                                      
REMARK 465     GLY A   327                                                      
REMARK 465     GLY A   328                                                      
REMARK 465     ASP A   329                                                      
REMARK 465     ASP A   330                                                      
REMARK 465     ASP A   331                                                      
REMARK 465     ASP A   332                                                      
REMARK 465     GLN A   333                                                      
REMARK 465     GLY A   334                                                      
REMARK 465     SER A   335                                                      
REMARK 465     ASP A   336                                                      
REMARK 465     ASP A   337                                                      
REMARK 465     GLU A   338                                                      
REMARK 465     TYR A   339                                                      
REMARK 465     SER A   340                                                      
REMARK 465     ASP A   341                                                      
REMARK 465     ASP A   342                                                      
REMARK 465     ASP A   343                                                      
REMARK 465     SER A   410                                                      
REMARK 465     TRP A   411                                                      
REMARK 465     LEU A   412                                                      
REMARK 465     CYS A   413                                                      
REMARK 465     ASP A   414                                                      
REMARK 465     PRO A   415                                                      
REMARK 465     ASP A   416                                                      
REMARK 465     ALA A   417                                                      
REMARK 465     MET A   418                                                      
REMARK 465     GLU A   419                                                      
REMARK 465     GLN A   420                                                      
REMARK 465     SER A   787                                                      
REMARK 465     THR A   788                                                      
REMARK 465     ALA A   789                                                      
REMARK 465     LEU A   790                                                      
REMARK 465     THR A   791                                                      
REMARK 465     HIS A   792                                                      
REMARK 465     LYS A  1217                                                      
REMARK 465     ASP A  1218                                                      
REMARK 465     SER A  1219                                                      
REMARK 465     SER A  1220                                                      
REMARK 465     SER A  1221                                                      
REMARK 465     THR A  1222                                                      
REMARK 465     ASN A  1223                                                      
REMARK 465     LEU A  1224                                                      
REMARK 465     GLU A  1225                                                      
REMARK 465     SER A  1226                                                      
REMARK 465     MET A  1227                                                      
REMARK 465     ASP A  1228                                                      
REMARK 465     THR A  1229                                                      
REMARK 465     SER A  1230                                                      
REMARK 465     MET B   -22                                                      
REMARK 465     ALA B   -21                                                      
REMARK 465     SER B   -20                                                      
REMARK 465     TRP B   -19                                                      
REMARK 465     SER B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     PRO B   -16                                                      
REMARK 465     GLN B   -15                                                      
REMARK 465     PHE B   -14                                                      
REMARK 465     GLU B   -13                                                      
REMARK 465     LYS B   -12                                                      
REMARK 465     VAL B   -11                                                      
REMARK 465     ASP B   -10                                                      
REMARK 465     GLU B    -9                                                      
REMARK 465     ASN B    -8                                                      
REMARK 465     LEU B    -7                                                      
REMARK 465     TYR B    -6                                                      
REMARK 465     PHE B    -5                                                      
REMARK 465     GLN B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     ARG B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ALA B   120                                                      
REMARK 465     SER B   121                                                      
REMARK 465     SER B   122                                                      
REMARK 465     ASP B   308                                                      
REMARK 465     PRO B   309                                                      
REMARK 465     ASN B   310                                                      
REMARK 465     TYR B   311                                                      
REMARK 465     ASN B   312                                                      
REMARK 465     TYR B   313                                                      
REMARK 465     ASP B   314                                                      
REMARK 465     ASP B   315                                                      
REMARK 465     GLU B   316                                                      
REMARK 465     ASP B   317                                                      
REMARK 465     GLU B   318                                                      
REMARK 465     ASP B   319                                                      
REMARK 465     GLU B   320                                                      
REMARK 465     ASN B   321                                                      
REMARK 465     ALA B   322                                                      
REMARK 465     MET B   323                                                      
REMARK 465     ASP B   324                                                      
REMARK 465     ALA B   325                                                      
REMARK 465     ASP B   326                                                      
REMARK 465     GLY B   327                                                      
REMARK 465     GLY B   328                                                      
REMARK 465     ASP B   329                                                      
REMARK 465     ASP B   330                                                      
REMARK 465     ASP B   331                                                      
REMARK 465     ASP B   332                                                      
REMARK 465     GLN B   333                                                      
REMARK 465     GLY B   334                                                      
REMARK 465     SER B   335                                                      
REMARK 465     ASP B   336                                                      
REMARK 465     ASP B   337                                                      
REMARK 465     GLU B   338                                                      
REMARK 465     TYR B   339                                                      
REMARK 465     SER B   340                                                      
REMARK 465     ASP B   341                                                      
REMARK 465     ASP B   342                                                      
REMARK 465     ASP B   343                                                      
REMARK 465     VAL B   408                                                      
REMARK 465     GLN B   409                                                      
REMARK 465     SER B   410                                                      
REMARK 465     TRP B   411                                                      
REMARK 465     LEU B   412                                                      
REMARK 465     CYS B   413                                                      
REMARK 465     ASP B   414                                                      
REMARK 465     PRO B   415                                                      
REMARK 465     ASP B   416                                                      
REMARK 465     ALA B   417                                                      
REMARK 465     MET B   418                                                      
REMARK 465     GLU B   419                                                      
REMARK 465     GLN B   420                                                      
REMARK 465     GLY B   421                                                      
REMARK 465     SER B   787                                                      
REMARK 465     THR B   788                                                      
REMARK 465     ALA B   789                                                      
REMARK 465     LEU B   790                                                      
REMARK 465     GLY B  1069                                                      
REMARK 465     PRO B  1070                                                      
REMARK 465     PHE B  1071                                                      
REMARK 465     LYS B  1217                                                      
REMARK 465     ASP B  1218                                                      
REMARK 465     SER B  1219                                                      
REMARK 465     SER B  1220                                                      
REMARK 465     SER B  1221                                                      
REMARK 465     THR B  1222                                                      
REMARK 465     ASN B  1223                                                      
REMARK 465     LEU B  1224                                                      
REMARK 465     GLU B  1225                                                      
REMARK 465     SER B  1226                                                      
REMARK 465     MET B  1227                                                      
REMARK 465     ASP B  1228                                                      
REMARK 465     THR B  1229                                                      
REMARK 465     SER B  1230                                                      
REMARK 465     MET C   173                                                      
REMARK 465     HIS C   174                                                      
REMARK 465     HIS C   175                                                      
REMARK 465     HIS C   176                                                      
REMARK 465     HIS C   177                                                      
REMARK 465     HIS C   178                                                      
REMARK 465     HIS C   179                                                      
REMARK 465     VAL C   180                                                      
REMARK 465     ASP C   181                                                      
REMARK 465     GLU C   182                                                      
REMARK 465     ASN C   183                                                      
REMARK 465     LEU C   184                                                      
REMARK 465     TYR C   185                                                      
REMARK 465     PHE C   186                                                      
REMARK 465     GLN C   187                                                      
REMARK 465     GLY C   188                                                      
REMARK 465     GLY C   189                                                      
REMARK 465     GLY C   190                                                      
REMARK 465     ARG C   191                                                      
REMARK 465     GLY C   192                                                      
REMARK 465     SER C   193                                                      
REMARK 465     ALA C   194                                                      
REMARK 465     LYS C   195                                                      
REMARK 465     LYS C   196                                                      
REMARK 465     LEU C   197                                                      
REMARK 465     VAL C   198                                                      
REMARK 465     ILE C   199                                                      
REMARK 465     LYS C   200                                                      
REMARK 465     ASN C   201                                                      
REMARK 465     PHE C   202                                                      
REMARK 465     LYS C   203                                                      
REMARK 465     ASP C   204                                                      
REMARK 465     LYS C   205                                                      
REMARK 465     PRO C   206                                                      
REMARK 465     LYS C   207                                                      
REMARK 465     LEU C   208                                                      
REMARK 465     PRO C   209                                                      
REMARK 465     GLU C   210                                                      
REMARK 465     ASN C   211                                                      
REMARK 465     TYR C   212                                                      
REMARK 465     VAL C   315                                                      
REMARK 465     LEU C   316                                                      
REMARK 465     GLN C   317                                                      
REMARK 465     ASN C   318                                                      
REMARK 465     SER C   319                                                      
REMARK 465     MET C   320                                                      
REMARK 465     LYS C   576                                                      
REMARK 465     GLU C   577                                                      
REMARK 465     ALA C   578                                                      
REMARK 465     MET D    11                                                      
REMARK 465     GLY D    12                                                      
REMARK 465     THR D    13                                                      
REMARK 465     ASN D    14                                                      
REMARK 465     SER D    15                                                      
REMARK 465     GLY D    16                                                      
REMARK 465     ALA D    17                                                      
REMARK 465     GLY D    18                                                      
REMARK 465     LYS D    19                                                      
REMARK 465     MET E   173                                                      
REMARK 465     HIS E   174                                                      
REMARK 465     HIS E   175                                                      
REMARK 465     HIS E   176                                                      
REMARK 465     HIS E   177                                                      
REMARK 465     HIS E   178                                                      
REMARK 465     HIS E   179                                                      
REMARK 465     VAL E   180                                                      
REMARK 465     ASP E   181                                                      
REMARK 465     GLU E   182                                                      
REMARK 465     ASN E   183                                                      
REMARK 465     LEU E   184                                                      
REMARK 465     TYR E   185                                                      
REMARK 465     PHE E   186                                                      
REMARK 465     GLN E   187                                                      
REMARK 465     GLY E   188                                                      
REMARK 465     GLY E   189                                                      
REMARK 465     GLY E   190                                                      
REMARK 465     ARG E   191                                                      
REMARK 465     GLY E   192                                                      
REMARK 465     SER E   193                                                      
REMARK 465     ALA E   194                                                      
REMARK 465     LYS E   195                                                      
REMARK 465     LYS E   196                                                      
REMARK 465     LEU E   197                                                      
REMARK 465     VAL E   198                                                      
REMARK 465     ILE E   199                                                      
REMARK 465     LYS E   200                                                      
REMARK 465     ASN E   201                                                      
REMARK 465     PHE E   202                                                      
REMARK 465     LYS E   203                                                      
REMARK 465     ASP E   204                                                      
REMARK 465     LYS E   205                                                      
REMARK 465     PRO E   206                                                      
REMARK 465     LYS E   207                                                      
REMARK 465     LEU E   208                                                      
REMARK 465     PRO E   209                                                      
REMARK 465     GLU E   210                                                      
REMARK 465     GLY E   574                                                      
REMARK 465     ASN E   575                                                      
REMARK 465     LYS E   576                                                      
REMARK 465     VAL E   671                                                      
REMARK 465     PRO E   672                                                      
REMARK 465     GLY E   673                                                      
REMARK 465     ASN E   674                                                      
REMARK 465     MET F    11                                                      
REMARK 465     GLY F    12                                                      
REMARK 465     THR F    13                                                      
REMARK 465     ASN F    14                                                      
REMARK 465     SER F    15                                                      
REMARK 465     GLY F    16                                                      
REMARK 465     ALA F    17                                                      
REMARK 465     GLY F    18                                                      
REMARK 465     ALA F    58                                                      
REMARK 465     ASN F    59                                                      
REMARK 465     GLN F    60                                                      
REMARK 465     ALA F    61                                                      
REMARK 465     SER F    62                                                      
REMARK 465     ALA F    63                                                      
REMARK 465     THR F    64                                                      
REMARK 465     SER F    65                                                      
REMARK 465     GLU F    66                                                      
REMARK 465     GLU F    67                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     TYR A 307    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 370    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 793    CG   CD   CE   NZ                                   
REMARK 470     GLN A 794    CG   CD   OE1  NE2                                  
REMARK 470     SER A 795    OG                                                  
REMARK 470     TYR A 796    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR B 307    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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    THR A  16       41.76   -148.57                                   
REMARK 500    LYS A  36     -148.84    -85.67                                   
REMARK 500    SER A  38       97.91     60.38                                   
REMARK 500    LYS A  40      100.64     69.35                                   
REMARK 500    ASP A  43        4.19    -66.50                                   
REMARK 500    PRO A  74       25.71    -70.11                                   
REMARK 500    LYS A  78       22.08   -140.62                                   
REMARK 500    SER A  97      156.94     71.44                                   
REMARK 500    ASP A  98      -73.70   -112.51                                   
REMARK 500    GLU A 116       25.60    -74.54                                   
REMARK 500    ALA A 125      -70.70    -72.03                                   
REMARK 500    GLN A 145      112.44    -36.74                                   
REMARK 500    GLU A 146      108.28    -54.84                                   
REMARK 500    VAL A 148      -74.85    -54.47                                   
REMARK 500    ARG A 164      -67.37    -95.98                                   
REMARK 500    GLN A 165       58.75   -107.48                                   
REMARK 500    THR A 185       57.81   -108.97                                   
REMARK 500    ASN A 208      -66.29      2.58                                   
REMARK 500    ASN A 225      -39.99     61.57                                   
REMARK 500    ASP A 226      -78.40     30.31                                   
REMARK 500    LEU A 253      -33.16   -146.26                                   
REMARK 500    ASP A 267      104.84    -59.33                                   
REMARK 500    ASP A 268      110.09   -176.60                                   
REMARK 500    GLU A 270      -71.75    -55.01                                   
REMARK 500    SER A 281       25.60    -71.80                                   
REMARK 500    PRO A 287       14.79    -60.73                                   
REMARK 500    VAL A 290       93.96     20.80                                   
REMARK 500    THR A 306      -76.28    -69.11                                   
REMARK 500    PRO A 369      -72.95    -43.11                                   
REMARK 500    PHE A 371      -71.82    -50.87                                   
REMARK 500    PHE A 383       33.69    -83.75                                   
REMARK 500    ARG A 386     -127.43    155.48                                   
REMARK 500    GLU A 422      137.43     73.38                                   
REMARK 500    LEU A 469       49.34   -103.09                                   
REMARK 500    GLN A 471       24.10    -79.60                                   
REMARK 500    PHE A 482      -77.10    -53.24                                   
REMARK 500    PRO A 552       74.67      9.08                                   
REMARK 500    ALA A 579       10.28     51.97                                   
REMARK 500    LEU A 600       74.22   -100.50                                   
REMARK 500    LYS A 641       97.32    -41.73                                   
REMARK 500    LEU A 644        4.99   -155.59                                   
REMARK 500    ASN A 662       28.16     37.58                                   
REMARK 500    ARG A 664      -61.50     63.90                                   
REMARK 500    TYR A 723       75.86   -152.24                                   
REMARK 500    SER A 728       -8.38    -59.48                                   
REMARK 500    SER A 733      -45.86     68.89                                   
REMARK 500    ASN A 769      -41.59     80.04                                   
REMARK 500    TYR A 784       61.89   -111.18                                   
REMARK 500    SER A 785      -62.78   -146.70                                   
REMARK 500    GLN A 794      -94.21     88.86                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     297 RAMACHANDRAN OUTLIERS.                        
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 D4001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  45   SG                                                     
REMARK 620 2 HIS D  80   ND1  97.9                                              
REMARK 620 3 CYS D  83   SG   90.0 109.1                                        
REMARK 620 4 CYS D  42   SG  111.4 113.2 128.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D4002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  77   ND1                                                    
REMARK 620 2 CYS D  94   SG  117.8                                              
REMARK 620 3 CYS D  75   SG  110.1  94.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D4003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  56   SG                                                     
REMARK 620 2 CYS D  68   SG   97.2                                              
REMARK 620 3 CYS D  53   SG   99.2 114.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F4001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F  45   SG                                                     
REMARK 620 2 CYS F  42   SG  111.2                                              
REMARK 620 3 HIS F  80   ND1 109.6  98.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F4002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F  94   SG                                                     
REMARK 620 2 HIS F  77   ND1 109.9                                              
REMARK 620 3 CYS F  75   SG  104.6  80.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F4003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F  53   SG                                                     
REMARK 620 2 CYS F  68   SG  125.5                                              
REMARK 620 3 CYS F  56   SG  114.4 105.7                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 4001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 4002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 4003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 4001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 4002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 4003                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1U6G   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CAND1-CUL1-ROC1 COMPLEX                     
REMARK 900 RELATED ID: 4A0L   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4A0K   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 CHAINS A AND B CONTAINS NATURAL VARIANT A952V                        
DBREF  4A0C A    1  1230  UNP    Q86VP6   CAND1_HUMAN      1   1230             
DBREF  4A0C B    1  1230  UNP    Q86VP6   CAND1_HUMAN      1   1230             
DBREF  4A0C C  192   913  UNP    Q13620   CUL4B_HUMAN    192    913             
DBREF  4A0C D   12   108  UNP    P62878   RBX1_MOUSE      12    108             
DBREF  4A0C E  192   913  UNP    Q13620   CUL4B_HUMAN    192    913             
DBREF  4A0C F   12   108  UNP    P62878   RBX1_MOUSE      12    108             
SEQADV 4A0C MET A  -22  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C ALA A  -21  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C SER A  -20  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C TRP A  -19  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C SER A  -18  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C HIS A  -17  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C PRO A  -16  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C GLN A  -15  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C PHE A  -14  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C GLU A  -13  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C LYS A  -12  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C VAL A  -11  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C ASP A  -10  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C GLU A   -9  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C ASN A   -8  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C LEU A   -7  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C TYR A   -6  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C PHE A   -5  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C GLN A   -4  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C GLY A   -3  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C GLY A   -2  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C GLY A   -1  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C ARG A    0  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C VAL A  952  UNP  Q86VP6    ALA   952 VARIANT                        
SEQADV 4A0C MET B  -22  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C ALA B  -21  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C SER B  -20  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C TRP B  -19  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C SER B  -18  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C HIS B  -17  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C PRO B  -16  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C GLN B  -15  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C PHE B  -14  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C GLU B  -13  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C LYS B  -12  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C VAL B  -11  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C ASP B  -10  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C GLU B   -9  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C ASN B   -8  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C LEU B   -7  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C TYR B   -6  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C PHE B   -5  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C GLN B   -4  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C GLY B   -3  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C GLY B   -2  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C GLY B   -1  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C ARG B    0  UNP  Q86VP6              EXPRESSION TAG                 
SEQADV 4A0C VAL B  952  UNP  Q86VP6    ALA   952 VARIANT                        
SEQADV 4A0C MET C  173  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C HIS C  174  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C HIS C  175  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C HIS C  176  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C HIS C  177  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C HIS C  178  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C HIS C  179  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C VAL C  180  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C ASP C  181  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C GLU C  182  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C ASN C  183  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C LEU C  184  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C TYR C  185  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C PHE C  186  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C GLN C  187  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C GLY C  188  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C GLY C  189  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C GLY C  190  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C ARG C  191  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C MET D   11  UNP  P62878              EXPRESSION TAG                 
SEQADV 4A0C MET E  173  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C HIS E  174  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C HIS E  175  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C HIS E  176  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C HIS E  177  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C HIS E  178  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C HIS E  179  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C VAL E  180  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C ASP E  181  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C GLU E  182  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C ASN E  183  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C LEU E  184  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C TYR E  185  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C PHE E  186  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C GLN E  187  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C GLY E  188  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C GLY E  189  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C GLY E  190  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C ARG E  191  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0C MET F   11  UNP  P62878              EXPRESSION TAG                 
SEQRES   1 A 1253  MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS VAL ASP          
SEQRES   2 A 1253  GLU ASN LEU TYR PHE GLN GLY GLY GLY ARG MET ALA SER          
SEQRES   3 A 1253  ALA SER TYR HIS ILE SER ASN LEU LEU GLU LYS MET THR          
SEQRES   4 A 1253  SER SER ASP LYS ASP PHE ARG PHE MET ALA THR ASN ASP          
SEQRES   5 A 1253  LEU MET THR GLU LEU GLN LYS ASP SER ILE LYS LEU ASP          
SEQRES   6 A 1253  ASP ASP SER GLU ARG LYS VAL VAL LYS MET ILE LEU LYS          
SEQRES   7 A 1253  LEU LEU GLU ASP LYS ASN GLY GLU VAL GLN ASN LEU ALA          
SEQRES   8 A 1253  VAL LYS CYS LEU GLY PRO LEU VAL SER LYS VAL LYS GLU          
SEQRES   9 A 1253  TYR GLN VAL GLU THR ILE VAL ASP THR LEU CYS THR ASN          
SEQRES  10 A 1253  MET LEU SER ASP LYS GLU GLN LEU ARG ASP ILE SER SER          
SEQRES  11 A 1253  ILE GLY LEU LYS THR VAL ILE GLY GLU LEU PRO PRO ALA          
SEQRES  12 A 1253  SER SER GLY SER ALA LEU ALA ALA ASN VAL CYS LYS LYS          
SEQRES  13 A 1253  ILE THR GLY ARG LEU THR SER ALA ILE ALA LYS GLN GLU          
SEQRES  14 A 1253  ASP VAL SER VAL GLN LEU GLU ALA LEU ASP ILE MET ALA          
SEQRES  15 A 1253  ASP MET LEU SER ARG GLN GLY GLY LEU LEU VAL ASN PHE          
SEQRES  16 A 1253  HIS PRO SER ILE LEU THR CYS LEU LEU PRO GLN LEU THR          
SEQRES  17 A 1253  SER PRO ARG LEU ALA VAL ARG LYS ARG THR ILE ILE ALA          
SEQRES  18 A 1253  LEU GLY HIS LEU VAL MET SER CYS GLY ASN ILE VAL PHE          
SEQRES  19 A 1253  VAL ASP LEU ILE GLU HIS LEU LEU SER GLU LEU SER LYS          
SEQRES  20 A 1253  ASN ASP SER MET SER THR THR ARG THR TYR ILE GLN CYS          
SEQRES  21 A 1253  ILE ALA ALA ILE SER ARG GLN ALA GLY HIS ARG ILE GLY          
SEQRES  22 A 1253  GLU TYR LEU GLU LYS ILE ILE PRO LEU VAL VAL LYS PHE          
SEQRES  23 A 1253  CYS ASN VAL ASP ASP ASP GLU LEU ARG GLU TYR CYS ILE          
SEQRES  24 A 1253  GLN ALA PHE GLU SER PHE VAL ARG ARG CYS PRO LYS GLU          
SEQRES  25 A 1253  VAL TYR PRO HIS VAL SER THR ILE ILE ASN ILE CYS LEU          
SEQRES  26 A 1253  LYS TYR LEU THR TYR ASP PRO ASN TYR ASN TYR ASP ASP          
SEQRES  27 A 1253  GLU ASP GLU ASP GLU ASN ALA MET ASP ALA ASP GLY GLY          
SEQRES  28 A 1253  ASP ASP ASP ASP GLN GLY SER ASP ASP GLU TYR SER ASP          
SEQRES  29 A 1253  ASP ASP ASP MET SER TRP LYS VAL ARG ARG ALA ALA ALA          
SEQRES  30 A 1253  LYS CYS LEU ASP ALA VAL VAL SER THR ARG HIS GLU MET          
SEQRES  31 A 1253  LEU PRO GLU PHE TYR LYS THR VAL SER PRO ALA LEU ILE          
SEQRES  32 A 1253  SER ARG PHE LYS GLU ARG GLU GLU ASN VAL LYS ALA ASP          
SEQRES  33 A 1253  VAL PHE HIS ALA TYR LEU SER LEU LEU LYS GLN THR ARG          
SEQRES  34 A 1253  PRO VAL GLN SER TRP LEU CYS ASP PRO ASP ALA MET GLU          
SEQRES  35 A 1253  GLN GLY GLU THR PRO LEU THR MET LEU GLN SER GLN VAL          
SEQRES  36 A 1253  PRO ASN ILE VAL LYS ALA LEU HIS LYS GLN MET LYS GLU          
SEQRES  37 A 1253  LYS SER VAL LYS THR ARG GLN CYS CYS PHE ASN MET LEU          
SEQRES  38 A 1253  THR GLU LEU VAL ASN VAL LEU PRO GLY ALA LEU THR GLN          
SEQRES  39 A 1253  HIS ILE PRO VAL LEU VAL PRO GLY ILE ILE PHE SER LEU          
SEQRES  40 A 1253  ASN ASP LYS SER SER SER SER ASN LEU LYS ILE ASP ALA          
SEQRES  41 A 1253  LEU SER CYS LEU TYR VAL ILE LEU CYS ASN HIS SER PRO          
SEQRES  42 A 1253  GLN VAL PHE HIS PRO HIS VAL GLN ALA LEU VAL PRO PRO          
SEQRES  43 A 1253  VAL VAL ALA CYS VAL GLY ASP PRO PHE TYR LYS ILE THR          
SEQRES  44 A 1253  SER GLU ALA LEU LEU VAL THR GLN GLN LEU VAL LYS VAL          
SEQRES  45 A 1253  ILE ARG PRO LEU ASP GLN PRO SER SER PHE ASP ALA THR          
SEQRES  46 A 1253  PRO TYR ILE LYS ASP LEU PHE THR CYS THR ILE LYS ARG          
SEQRES  47 A 1253  LEU LYS ALA ALA ASP ILE ASP GLN GLU VAL LYS GLU ARG          
SEQRES  48 A 1253  ALA ILE SER CYS MET GLY GLN ILE ILE CYS ASN LEU GLY          
SEQRES  49 A 1253  ASP ASN LEU GLY SER ASP LEU PRO ASN THR LEU GLN ILE          
SEQRES  50 A 1253  PHE LEU GLU ARG LEU LYS ASN GLU ILE THR ARG LEU THR          
SEQRES  51 A 1253  THR VAL LYS ALA LEU THR LEU ILE ALA GLY SER PRO LEU          
SEQRES  52 A 1253  LYS ILE ASP LEU ARG PRO VAL LEU GLY GLU GLY VAL PRO          
SEQRES  53 A 1253  ILE LEU ALA SER PHE LEU ARG LYS ASN GLN ARG ALA LEU          
SEQRES  54 A 1253  LYS LEU GLY THR LEU SER ALA LEU ASP ILE LEU ILE LYS          
SEQRES  55 A 1253  ASN TYR SER ASP SER LEU THR ALA ALA MET ILE ASP ALA          
SEQRES  56 A 1253  VAL LEU ASP GLU LEU PRO PRO LEU ILE SER GLU SER ASP          
SEQRES  57 A 1253  MET HIS VAL SER GLN MET ALA ILE SER PHE LEU THR THR          
SEQRES  58 A 1253  LEU ALA LYS VAL TYR PRO SER SER LEU SER LYS ILE SER          
SEQRES  59 A 1253  GLY SER ILE LEU ASN GLU LEU ILE GLY LEU VAL ARG SER          
SEQRES  60 A 1253  PRO LEU LEU GLN GLY GLY ALA LEU SER ALA MET LEU ASP          
SEQRES  61 A 1253  PHE PHE GLN ALA LEU VAL VAL THR GLY THR ASN ASN LEU          
SEQRES  62 A 1253  GLY TYR MET ASP LEU LEU ARG MET LEU THR GLY PRO VAL          
SEQRES  63 A 1253  TYR SER GLN SER THR ALA LEU THR HIS LYS GLN SER TYR          
SEQRES  64 A 1253  TYR SER ILE ALA LYS CYS VAL ALA ALA LEU THR ARG ALA          
SEQRES  65 A 1253  CYS PRO LYS GLU GLY PRO ALA VAL VAL GLY GLN PHE ILE          
SEQRES  66 A 1253  GLN ASP VAL LYS ASN SER ARG SER THR ASP SER ILE ARG          
SEQRES  67 A 1253  LEU LEU ALA LEU LEU SER LEU GLY GLU VAL GLY HIS HIS          
SEQRES  68 A 1253  ILE ASP LEU SER GLY GLN LEU GLU LEU LYS SER VAL ILE          
SEQRES  69 A 1253  LEU GLU ALA PHE SER SER PRO SER GLU GLU VAL LYS SER          
SEQRES  70 A 1253  ALA ALA SER TYR ALA LEU GLY SER ILE SER VAL GLY ASN          
SEQRES  71 A 1253  LEU PRO GLU TYR LEU PRO PHE VAL LEU GLN GLU ILE THR          
SEQRES  72 A 1253  SER GLN PRO LYS ARG GLN TYR LEU LEU LEU HIS SER LEU          
SEQRES  73 A 1253  LYS GLU ILE ILE SER SER ALA SER VAL VAL GLY LEU LYS          
SEQRES  74 A 1253  PRO TYR VAL GLU ASN ILE TRP ALA LEU LEU LEU LYS HIS          
SEQRES  75 A 1253  CYS GLU CYS ALA GLU GLU GLY THR ARG ASN VAL VAL VAL          
SEQRES  76 A 1253  GLU CYS LEU GLY LYS LEU THR LEU ILE ASP PRO GLU THR          
SEQRES  77 A 1253  LEU LEU PRO ARG LEU LYS GLY TYR LEU ILE SER GLY SER          
SEQRES  78 A 1253  SER TYR ALA ARG SER SER VAL VAL THR ALA VAL LYS PHE          
SEQRES  79 A 1253  THR ILE SER ASP HIS PRO GLN PRO ILE ASP PRO LEU LEU          
SEQRES  80 A 1253  LYS ASN CYS ILE GLY ASP PHE LEU LYS THR LEU GLU ASP          
SEQRES  81 A 1253  PRO ASP LEU ASN VAL ARG ARG VAL ALA LEU VAL THR PHE          
SEQRES  82 A 1253  ASN SER ALA ALA HIS ASN LYS PRO SER LEU ILE ARG ASP          
SEQRES  83 A 1253  LEU LEU ASP THR VAL LEU PRO HIS LEU TYR ASN GLU THR          
SEQRES  84 A 1253  LYS VAL ARG LYS GLU LEU ILE ARG GLU VAL GLU MET GLY          
SEQRES  85 A 1253  PRO PHE LYS HIS THR VAL ASP ASP GLY LEU ASP ILE ARG          
SEQRES  86 A 1253  LYS ALA ALA PHE GLU CYS MET TYR THR LEU LEU ASP SER          
SEQRES  87 A 1253  CYS LEU ASP ARG LEU ASP ILE PHE GLU PHE LEU ASN HIS          
SEQRES  88 A 1253  VAL GLU ASP GLY LEU LYS ASP HIS TYR ASP ILE LYS MET          
SEQRES  89 A 1253  LEU THR PHE LEU MET LEU VAL ARG LEU SER THR LEU CYS          
SEQRES  90 A 1253  PRO SER ALA VAL LEU GLN ARG LEU ASP ARG LEU VAL GLU          
SEQRES  91 A 1253  PRO LEU ARG ALA THR CYS THR THR LYS VAL LYS ALA ASN          
SEQRES  92 A 1253  SER VAL LYS GLN GLU PHE GLU LYS GLN ASP GLU LEU LYS          
SEQRES  93 A 1253  ARG SER ALA MET ARG ALA VAL ALA ALA LEU LEU THR ILE          
SEQRES  94 A 1253  PRO GLU ALA GLU LYS SER PRO LEU MET SER GLU PHE GLN          
SEQRES  95 A 1253  SER GLN ILE SER SER ASN PRO GLU LEU ALA ALA ILE PHE          
SEQRES  96 A 1253  GLU SER ILE GLN LYS ASP SER SER SER THR ASN LEU GLU          
SEQRES  97 A 1253  SER MET ASP THR SER                                          
SEQRES   1 B 1253  MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS VAL ASP          
SEQRES   2 B 1253  GLU ASN LEU TYR PHE GLN GLY GLY GLY ARG MET ALA SER          
SEQRES   3 B 1253  ALA SER TYR HIS ILE SER ASN LEU LEU GLU LYS MET THR          
SEQRES   4 B 1253  SER SER ASP LYS ASP PHE ARG PHE MET ALA THR ASN ASP          
SEQRES   5 B 1253  LEU MET THR GLU LEU GLN LYS ASP SER ILE LYS LEU ASP          
SEQRES   6 B 1253  ASP ASP SER GLU ARG LYS VAL VAL LYS MET ILE LEU LYS          
SEQRES   7 B 1253  LEU LEU GLU ASP LYS ASN GLY GLU VAL GLN ASN LEU ALA          
SEQRES   8 B 1253  VAL LYS CYS LEU GLY PRO LEU VAL SER LYS VAL LYS GLU          
SEQRES   9 B 1253  TYR GLN VAL GLU THR ILE VAL ASP THR LEU CYS THR ASN          
SEQRES  10 B 1253  MET LEU SER ASP LYS GLU GLN LEU ARG ASP ILE SER SER          
SEQRES  11 B 1253  ILE GLY LEU LYS THR VAL ILE GLY GLU LEU PRO PRO ALA          
SEQRES  12 B 1253  SER SER GLY SER ALA LEU ALA ALA ASN VAL CYS LYS LYS          
SEQRES  13 B 1253  ILE THR GLY ARG LEU THR SER ALA ILE ALA LYS GLN GLU          
SEQRES  14 B 1253  ASP VAL SER VAL GLN LEU GLU ALA LEU ASP ILE MET ALA          
SEQRES  15 B 1253  ASP MET LEU SER ARG GLN GLY GLY LEU LEU VAL ASN PHE          
SEQRES  16 B 1253  HIS PRO SER ILE LEU THR CYS LEU LEU PRO GLN LEU THR          
SEQRES  17 B 1253  SER PRO ARG LEU ALA VAL ARG LYS ARG THR ILE ILE ALA          
SEQRES  18 B 1253  LEU GLY HIS LEU VAL MET SER CYS GLY ASN ILE VAL PHE          
SEQRES  19 B 1253  VAL ASP LEU ILE GLU HIS LEU LEU SER GLU LEU SER LYS          
SEQRES  20 B 1253  ASN ASP SER MET SER THR THR ARG THR TYR ILE GLN CYS          
SEQRES  21 B 1253  ILE ALA ALA ILE SER ARG GLN ALA GLY HIS ARG ILE GLY          
SEQRES  22 B 1253  GLU TYR LEU GLU LYS ILE ILE PRO LEU VAL VAL LYS PHE          
SEQRES  23 B 1253  CYS ASN VAL ASP ASP ASP GLU LEU ARG GLU TYR CYS ILE          
SEQRES  24 B 1253  GLN ALA PHE GLU SER PHE VAL ARG ARG CYS PRO LYS GLU          
SEQRES  25 B 1253  VAL TYR PRO HIS VAL SER THR ILE ILE ASN ILE CYS LEU          
SEQRES  26 B 1253  LYS TYR LEU THR TYR ASP PRO ASN TYR ASN TYR ASP ASP          
SEQRES  27 B 1253  GLU ASP GLU ASP GLU ASN ALA MET ASP ALA ASP GLY GLY          
SEQRES  28 B 1253  ASP ASP ASP ASP GLN GLY SER ASP ASP GLU TYR SER ASP          
SEQRES  29 B 1253  ASP ASP ASP MET SER TRP LYS VAL ARG ARG ALA ALA ALA          
SEQRES  30 B 1253  LYS CYS LEU ASP ALA VAL VAL SER THR ARG HIS GLU MET          
SEQRES  31 B 1253  LEU PRO GLU PHE TYR LYS THR VAL SER PRO ALA LEU ILE          
SEQRES  32 B 1253  SER ARG PHE LYS GLU ARG GLU GLU ASN VAL LYS ALA ASP          
SEQRES  33 B 1253  VAL PHE HIS ALA TYR LEU SER LEU LEU LYS GLN THR ARG          
SEQRES  34 B 1253  PRO VAL GLN SER TRP LEU CYS ASP PRO ASP ALA MET GLU          
SEQRES  35 B 1253  GLN GLY GLU THR PRO LEU THR MET LEU GLN SER GLN VAL          
SEQRES  36 B 1253  PRO ASN ILE VAL LYS ALA LEU HIS LYS GLN MET LYS GLU          
SEQRES  37 B 1253  LYS SER VAL LYS THR ARG GLN CYS CYS PHE ASN MET LEU          
SEQRES  38 B 1253  THR GLU LEU VAL ASN VAL LEU PRO GLY ALA LEU THR GLN          
SEQRES  39 B 1253  HIS ILE PRO VAL LEU VAL PRO GLY ILE ILE PHE SER LEU          
SEQRES  40 B 1253  ASN ASP LYS SER SER SER SER ASN LEU LYS ILE ASP ALA          
SEQRES  41 B 1253  LEU SER CYS LEU TYR VAL ILE LEU CYS ASN HIS SER PRO          
SEQRES  42 B 1253  GLN VAL PHE HIS PRO HIS VAL GLN ALA LEU VAL PRO PRO          
SEQRES  43 B 1253  VAL VAL ALA CYS VAL GLY ASP PRO PHE TYR LYS ILE THR          
SEQRES  44 B 1253  SER GLU ALA LEU LEU VAL THR GLN GLN LEU VAL LYS VAL          
SEQRES  45 B 1253  ILE ARG PRO LEU ASP GLN PRO SER SER PHE ASP ALA THR          
SEQRES  46 B 1253  PRO TYR ILE LYS ASP LEU PHE THR CYS THR ILE LYS ARG          
SEQRES  47 B 1253  LEU LYS ALA ALA ASP ILE ASP GLN GLU VAL LYS GLU ARG          
SEQRES  48 B 1253  ALA ILE SER CYS MET GLY GLN ILE ILE CYS ASN LEU GLY          
SEQRES  49 B 1253  ASP ASN LEU GLY SER ASP LEU PRO ASN THR LEU GLN ILE          
SEQRES  50 B 1253  PHE LEU GLU ARG LEU LYS ASN GLU ILE THR ARG LEU THR          
SEQRES  51 B 1253  THR VAL LYS ALA LEU THR LEU ILE ALA GLY SER PRO LEU          
SEQRES  52 B 1253  LYS ILE ASP LEU ARG PRO VAL LEU GLY GLU GLY VAL PRO          
SEQRES  53 B 1253  ILE LEU ALA SER PHE LEU ARG LYS ASN GLN ARG ALA LEU          
SEQRES  54 B 1253  LYS LEU GLY THR LEU SER ALA LEU ASP ILE LEU ILE LYS          
SEQRES  55 B 1253  ASN TYR SER ASP SER LEU THR ALA ALA MET ILE ASP ALA          
SEQRES  56 B 1253  VAL LEU ASP GLU LEU PRO PRO LEU ILE SER GLU SER ASP          
SEQRES  57 B 1253  MET HIS VAL SER GLN MET ALA ILE SER PHE LEU THR THR          
SEQRES  58 B 1253  LEU ALA LYS VAL TYR PRO SER SER LEU SER LYS ILE SER          
SEQRES  59 B 1253  GLY SER ILE LEU ASN GLU LEU ILE GLY LEU VAL ARG SER          
SEQRES  60 B 1253  PRO LEU LEU GLN GLY GLY ALA LEU SER ALA MET LEU ASP          
SEQRES  61 B 1253  PHE PHE GLN ALA LEU VAL VAL THR GLY THR ASN ASN LEU          
SEQRES  62 B 1253  GLY TYR MET ASP LEU LEU ARG MET LEU THR GLY PRO VAL          
SEQRES  63 B 1253  TYR SER GLN SER THR ALA LEU THR HIS LYS GLN SER TYR          
SEQRES  64 B 1253  TYR SER ILE ALA LYS CYS VAL ALA ALA LEU THR ARG ALA          
SEQRES  65 B 1253  CYS PRO LYS GLU GLY PRO ALA VAL VAL GLY GLN PHE ILE          
SEQRES  66 B 1253  GLN ASP VAL LYS ASN SER ARG SER THR ASP SER ILE ARG          
SEQRES  67 B 1253  LEU LEU ALA LEU LEU SER LEU GLY GLU VAL GLY HIS HIS          
SEQRES  68 B 1253  ILE ASP LEU SER GLY GLN LEU GLU LEU LYS SER VAL ILE          
SEQRES  69 B 1253  LEU GLU ALA PHE SER SER PRO SER GLU GLU VAL LYS SER          
SEQRES  70 B 1253  ALA ALA SER TYR ALA LEU GLY SER ILE SER VAL GLY ASN          
SEQRES  71 B 1253  LEU PRO GLU TYR LEU PRO PHE VAL LEU GLN GLU ILE THR          
SEQRES  72 B 1253  SER GLN PRO LYS ARG GLN TYR LEU LEU LEU HIS SER LEU          
SEQRES  73 B 1253  LYS GLU ILE ILE SER SER ALA SER VAL VAL GLY LEU LYS          
SEQRES  74 B 1253  PRO TYR VAL GLU ASN ILE TRP ALA LEU LEU LEU LYS HIS          
SEQRES  75 B 1253  CYS GLU CYS ALA GLU GLU GLY THR ARG ASN VAL VAL VAL          
SEQRES  76 B 1253  GLU CYS LEU GLY LYS LEU THR LEU ILE ASP PRO GLU THR          
SEQRES  77 B 1253  LEU LEU PRO ARG LEU LYS GLY TYR LEU ILE SER GLY SER          
SEQRES  78 B 1253  SER TYR ALA ARG SER SER VAL VAL THR ALA VAL LYS PHE          
SEQRES  79 B 1253  THR ILE SER ASP HIS PRO GLN PRO ILE ASP PRO LEU LEU          
SEQRES  80 B 1253  LYS ASN CYS ILE GLY ASP PHE LEU LYS THR LEU GLU ASP          
SEQRES  81 B 1253  PRO ASP LEU ASN VAL ARG ARG VAL ALA LEU VAL THR PHE          
SEQRES  82 B 1253  ASN SER ALA ALA HIS ASN LYS PRO SER LEU ILE ARG ASP          
SEQRES  83 B 1253  LEU LEU ASP THR VAL LEU PRO HIS LEU TYR ASN GLU THR          
SEQRES  84 B 1253  LYS VAL ARG LYS GLU LEU ILE ARG GLU VAL GLU MET GLY          
SEQRES  85 B 1253  PRO PHE LYS HIS THR VAL ASP ASP GLY LEU ASP ILE ARG          
SEQRES  86 B 1253  LYS ALA ALA PHE GLU CYS MET TYR THR LEU LEU ASP SER          
SEQRES  87 B 1253  CYS LEU ASP ARG LEU ASP ILE PHE GLU PHE LEU ASN HIS          
SEQRES  88 B 1253  VAL GLU ASP GLY LEU LYS ASP HIS TYR ASP ILE LYS MET          
SEQRES  89 B 1253  LEU THR PHE LEU MET LEU VAL ARG LEU SER THR LEU CYS          
SEQRES  90 B 1253  PRO SER ALA VAL LEU GLN ARG LEU ASP ARG LEU VAL GLU          
SEQRES  91 B 1253  PRO LEU ARG ALA THR CYS THR THR LYS VAL LYS ALA ASN          
SEQRES  92 B 1253  SER VAL LYS GLN GLU PHE GLU LYS GLN ASP GLU LEU LYS          
SEQRES  93 B 1253  ARG SER ALA MET ARG ALA VAL ALA ALA LEU LEU THR ILE          
SEQRES  94 B 1253  PRO GLU ALA GLU LYS SER PRO LEU MET SER GLU PHE GLN          
SEQRES  95 B 1253  SER GLN ILE SER SER ASN PRO GLU LEU ALA ALA ILE PHE          
SEQRES  96 B 1253  GLU SER ILE GLN LYS ASP SER SER SER THR ASN LEU GLU          
SEQRES  97 B 1253  SER MET ASP THR SER                                          
SEQRES   1 C  741  MET HIS HIS HIS HIS HIS HIS VAL ASP GLU ASN LEU TYR          
SEQRES   2 C  741  PHE GLN GLY GLY GLY ARG GLY SER ALA LYS LYS LEU VAL          
SEQRES   3 C  741  ILE LYS ASN PHE LYS ASP LYS PRO LYS LEU PRO GLU ASN          
SEQRES   4 C  741  TYR THR ASP GLU THR TRP GLN LYS LEU LYS GLU ALA VAL          
SEQRES   5 C  741  GLU ALA ILE GLN ASN SER THR SER ILE LYS TYR ASN LEU          
SEQRES   6 C  741  GLU GLU LEU TYR GLN ALA VAL GLU ASN LEU CYS SER TYR          
SEQRES   7 C  741  LYS ILE SER ALA ASN LEU TYR LYS GLN LEU ARG GLN ILE          
SEQRES   8 C  741  CYS GLU ASP HIS ILE LYS ALA GLN ILE HIS GLN PHE ARG          
SEQRES   9 C  741  GLU ASP SER LEU ASP SER VAL LEU PHE LEU LYS LYS ILE          
SEQRES  10 C  741  ASP ARG CYS TRP GLN ASN HIS CYS ARG GLN MET ILE MET          
SEQRES  11 C  741  ILE ARG SER ILE PHE LEU PHE LEU ASP ARG THR TYR VAL          
SEQRES  12 C  741  LEU GLN ASN SER MET LEU PRO SER ILE TRP ASP MET GLY          
SEQRES  13 C  741  LEU GLU LEU PHE ARG ALA HIS ILE ILE SER ASP GLN LYS          
SEQRES  14 C  741  VAL GLN ASN LYS THR ILE ASP GLY ILE LEU LEU LEU ILE          
SEQRES  15 C  741  GLU ARG GLU ARG ASN GLY GLU ALA ILE ASP ARG SER LEU          
SEQRES  16 C  741  LEU ARG SER LEU LEU SER MET LEU SER ASP LEU GLN ILE          
SEQRES  17 C  741  TYR GLN ASP SER PHE GLU GLN ARG PHE LEU GLU GLU THR          
SEQRES  18 C  741  ASN ARG LEU TYR ALA ALA GLU GLY GLN LYS LEU MET GLN          
SEQRES  19 C  741  GLU ARG GLU VAL PRO GLU TYR LEU HIS HIS VAL ASN LYS          
SEQRES  20 C  741  ARG LEU GLU GLU GLU ALA ASP ARG LEU ILE THR TYR LEU          
SEQRES  21 C  741  ASP GLN THR THR GLN LYS SER LEU ILE ALA THR VAL GLU          
SEQRES  22 C  741  LYS GLN LEU LEU GLY GLU HIS LEU THR ALA ILE LEU GLN          
SEQRES  23 C  741  LYS GLY LEU ASN ASN LEU LEU ASP GLU ASN ARG ILE GLN          
SEQRES  24 C  741  ASP LEU SER LEU LEU TYR GLN LEU PHE SER ARG VAL ARG          
SEQRES  25 C  741  GLY GLY VAL GLN VAL LEU LEU GLN GLN TRP ILE GLU TYR          
SEQRES  26 C  741  ILE LYS ALA PHE GLY SER THR ILE VAL ILE ASN PRO GLU          
SEQRES  27 C  741  LYS ASP LYS THR MET VAL GLN GLU LEU LEU ASP PHE LYS          
SEQRES  28 C  741  ASP LYS VAL ASP HIS ILE ILE ASP ILE CYS PHE LEU LYS          
SEQRES  29 C  741  ASN GLU LYS PHE ILE ASN ALA MET LYS GLU ALA PHE GLU          
SEQRES  30 C  741  THR PHE ILE ASN LYS ARG PRO ASN LYS PRO ALA GLU LEU          
SEQRES  31 C  741  ILE ALA LYS TYR VAL ASP SER LYS LEU ARG ALA GLY ASN          
SEQRES  32 C  741  LYS GLU ALA THR ASP GLU GLU LEU GLU LYS MET LEU ASP          
SEQRES  33 C  741  LYS ILE MET ILE ILE PHE ARG PHE ILE TYR GLY LYS ASP          
SEQRES  34 C  741  VAL PHE GLU ALA PHE TYR LYS LYS ASP LEU ALA LYS ARG          
SEQRES  35 C  741  LEU LEU VAL GLY LYS SER ALA SER VAL ASP ALA GLU LYS          
SEQRES  36 C  741  SER MET LEU SER LYS LEU LYS HIS GLU CYS GLY ALA ALA          
SEQRES  37 C  741  PHE THR SER LYS LEU GLU GLY MET PHE LYS ASP MET GLU          
SEQRES  38 C  741  LEU SER LYS ASP ILE MET ILE GLN PHE LYS GLN TYR MET          
SEQRES  39 C  741  GLN ASN GLN ASN VAL PRO GLY ASN ILE GLU LEU THR VAL          
SEQRES  40 C  741  ASN ILE LEU THR MET GLY TYR TRP PRO THR TYR VAL PRO          
SEQRES  41 C  741  MET GLU VAL HIS LEU PRO PRO GLU MET VAL LYS LEU GLN          
SEQRES  42 C  741  GLU ILE PHE LYS THR PHE TYR LEU GLY LYS HIS SER GLY          
SEQRES  43 C  741  ARG LYS LEU GLN TRP GLN SER THR LEU GLY HIS CYS VAL          
SEQRES  44 C  741  LEU LYS ALA GLU PHE LYS GLU GLY LYS LYS GLU LEU GLN          
SEQRES  45 C  741  VAL SER LEU PHE GLN THR LEU VAL LEU LEU MET PHE ASN          
SEQRES  46 C  741  GLU GLY GLU GLU PHE SER LEU GLU GLU ILE LYS GLN ALA          
SEQRES  47 C  741  THR GLY ILE GLU ASP GLY GLU LEU ARG ARG THR LEU GLN          
SEQRES  48 C  741  SER LEU ALA CYS GLY LYS ALA ARG VAL LEU ALA LYS ASN          
SEQRES  49 C  741  PRO LYS GLY LYS ASP ILE GLU ASP GLY ASP LYS PHE ILE          
SEQRES  50 C  741  CYS ASN ASP ASP PHE LYS HIS LYS LEU PHE ARG ILE LYS          
SEQRES  51 C  741  ILE ASN GLN ILE GLN MET LYS GLU THR VAL GLU GLU GLN          
SEQRES  52 C  741  ALA SER THR THR GLU ARG VAL PHE GLN ASP ARG GLN TYR          
SEQRES  53 C  741  GLN ILE ASP ALA ALA ILE VAL ARG ILE MET LYS MET ARG          
SEQRES  54 C  741  LYS THR LEU SER HIS ASN LEU LEU VAL SER GLU VAL TYR          
SEQRES  55 C  741  ASN GLN LEU LYS PHE PRO VAL LYS PRO ALA ASP LEU LYS          
SEQRES  56 C  741  LYS ARG ILE GLU SER LEU ILE ASP ARG ASP TYR MET GLU          
SEQRES  57 C  741  ARG ASP LYS GLU ASN PRO ASN GLN TYR ASN TYR ILE ALA          
SEQRES   1 D   98  MET GLY THR ASN SER GLY ALA GLY LYS LYS ARG PHE GLU          
SEQRES   2 D   98  VAL LYS LYS TRP ASN ALA VAL ALA LEU TRP ALA TRP ASP          
SEQRES   3 D   98  ILE VAL VAL ASP ASN CYS ALA ILE CYS ARG ASN HIS ILE          
SEQRES   4 D   98  MET ASP LEU CYS ILE GLU CYS GLN ALA ASN GLN ALA SER          
SEQRES   5 D   98  ALA THR SER GLU GLU CYS THR VAL ALA TRP GLY VAL CYS          
SEQRES   6 D   98  ASN HIS ALA PHE HIS PHE HIS CYS ILE SER ARG TRP LEU          
SEQRES   7 D   98  LYS THR ARG GLN VAL CYS PRO LEU ASP ASN ARG GLU TRP          
SEQRES   8 D   98  GLU PHE GLN LYS TYR GLY HIS                                  
SEQRES   1 E  741  MET HIS HIS HIS HIS HIS HIS VAL ASP GLU ASN LEU TYR          
SEQRES   2 E  741  PHE GLN GLY GLY GLY ARG GLY SER ALA LYS LYS LEU VAL          
SEQRES   3 E  741  ILE LYS ASN PHE LYS ASP LYS PRO LYS LEU PRO GLU ASN          
SEQRES   4 E  741  TYR THR ASP GLU THR TRP GLN LYS LEU LYS GLU ALA VAL          
SEQRES   5 E  741  GLU ALA ILE GLN ASN SER THR SER ILE LYS TYR ASN LEU          
SEQRES   6 E  741  GLU GLU LEU TYR GLN ALA VAL GLU ASN LEU CYS SER TYR          
SEQRES   7 E  741  LYS ILE SER ALA ASN LEU TYR LYS GLN LEU ARG GLN ILE          
SEQRES   8 E  741  CYS GLU ASP HIS ILE LYS ALA GLN ILE HIS GLN PHE ARG          
SEQRES   9 E  741  GLU ASP SER LEU ASP SER VAL LEU PHE LEU LYS LYS ILE          
SEQRES  10 E  741  ASP ARG CYS TRP GLN ASN HIS CYS ARG GLN MET ILE MET          
SEQRES  11 E  741  ILE ARG SER ILE PHE LEU PHE LEU ASP ARG THR TYR VAL          
SEQRES  12 E  741  LEU GLN ASN SER MET LEU PRO SER ILE TRP ASP MET GLY          
SEQRES  13 E  741  LEU GLU LEU PHE ARG ALA HIS ILE ILE SER ASP GLN LYS          
SEQRES  14 E  741  VAL GLN ASN LYS THR ILE ASP GLY ILE LEU LEU LEU ILE          
SEQRES  15 E  741  GLU ARG GLU ARG ASN GLY GLU ALA ILE ASP ARG SER LEU          
SEQRES  16 E  741  LEU ARG SER LEU LEU SER MET LEU SER ASP LEU GLN ILE          
SEQRES  17 E  741  TYR GLN ASP SER PHE GLU GLN ARG PHE LEU GLU GLU THR          
SEQRES  18 E  741  ASN ARG LEU TYR ALA ALA GLU GLY GLN LYS LEU MET GLN          
SEQRES  19 E  741  GLU ARG GLU VAL PRO GLU TYR LEU HIS HIS VAL ASN LYS          
SEQRES  20 E  741  ARG LEU GLU GLU GLU ALA ASP ARG LEU ILE THR TYR LEU          
SEQRES  21 E  741  ASP GLN THR THR GLN LYS SER LEU ILE ALA THR VAL GLU          
SEQRES  22 E  741  LYS GLN LEU LEU GLY GLU HIS LEU THR ALA ILE LEU GLN          
SEQRES  23 E  741  LYS GLY LEU ASN ASN LEU LEU ASP GLU ASN ARG ILE GLN          
SEQRES  24 E  741  ASP LEU SER LEU LEU TYR GLN LEU PHE SER ARG VAL ARG          
SEQRES  25 E  741  GLY GLY VAL GLN VAL LEU LEU GLN GLN TRP ILE GLU TYR          
SEQRES  26 E  741  ILE LYS ALA PHE GLY SER THR ILE VAL ILE ASN PRO GLU          
SEQRES  27 E  741  LYS ASP LYS THR MET VAL GLN GLU LEU LEU ASP PHE LYS          
SEQRES  28 E  741  ASP LYS VAL ASP HIS ILE ILE ASP ILE CYS PHE LEU LYS          
SEQRES  29 E  741  ASN GLU LYS PHE ILE ASN ALA MET LYS GLU ALA PHE GLU          
SEQRES  30 E  741  THR PHE ILE ASN LYS ARG PRO ASN LYS PRO ALA GLU LEU          
SEQRES  31 E  741  ILE ALA LYS TYR VAL ASP SER LYS LEU ARG ALA GLY ASN          
SEQRES  32 E  741  LYS GLU ALA THR ASP GLU GLU LEU GLU LYS MET LEU ASP          
SEQRES  33 E  741  LYS ILE MET ILE ILE PHE ARG PHE ILE TYR GLY LYS ASP          
SEQRES  34 E  741  VAL PHE GLU ALA PHE TYR LYS LYS ASP LEU ALA LYS ARG          
SEQRES  35 E  741  LEU LEU VAL GLY LYS SER ALA SER VAL ASP ALA GLU LYS          
SEQRES  36 E  741  SER MET LEU SER LYS LEU LYS HIS GLU CYS GLY ALA ALA          
SEQRES  37 E  741  PHE THR SER LYS LEU GLU GLY MET PHE LYS ASP MET GLU          
SEQRES  38 E  741  LEU SER LYS ASP ILE MET ILE GLN PHE LYS GLN TYR MET          
SEQRES  39 E  741  GLN ASN GLN ASN VAL PRO GLY ASN ILE GLU LEU THR VAL          
SEQRES  40 E  741  ASN ILE LEU THR MET GLY TYR TRP PRO THR TYR VAL PRO          
SEQRES  41 E  741  MET GLU VAL HIS LEU PRO PRO GLU MET VAL LYS LEU GLN          
SEQRES  42 E  741  GLU ILE PHE LYS THR PHE TYR LEU GLY LYS HIS SER GLY          
SEQRES  43 E  741  ARG LYS LEU GLN TRP GLN SER THR LEU GLY HIS CYS VAL          
SEQRES  44 E  741  LEU LYS ALA GLU PHE LYS GLU GLY LYS LYS GLU LEU GLN          
SEQRES  45 E  741  VAL SER LEU PHE GLN THR LEU VAL LEU LEU MET PHE ASN          
SEQRES  46 E  741  GLU GLY GLU GLU PHE SER LEU GLU GLU ILE LYS GLN ALA          
SEQRES  47 E  741  THR GLY ILE GLU ASP GLY GLU LEU ARG ARG THR LEU GLN          
SEQRES  48 E  741  SER LEU ALA CYS GLY LYS ALA ARG VAL LEU ALA LYS ASN          
SEQRES  49 E  741  PRO LYS GLY LYS ASP ILE GLU ASP GLY ASP LYS PHE ILE          
SEQRES  50 E  741  CYS ASN ASP ASP PHE LYS HIS LYS LEU PHE ARG ILE LYS          
SEQRES  51 E  741  ILE ASN GLN ILE GLN MET LYS GLU THR VAL GLU GLU GLN          
SEQRES  52 E  741  ALA SER THR THR GLU ARG VAL PHE GLN ASP ARG GLN TYR          
SEQRES  53 E  741  GLN ILE ASP ALA ALA ILE VAL ARG ILE MET LYS MET ARG          
SEQRES  54 E  741  LYS THR LEU SER HIS ASN LEU LEU VAL SER GLU VAL TYR          
SEQRES  55 E  741  ASN GLN LEU LYS PHE PRO VAL LYS PRO ALA ASP LEU LYS          
SEQRES  56 E  741  LYS ARG ILE GLU SER LEU ILE ASP ARG ASP TYR MET GLU          
SEQRES  57 E  741  ARG ASP LYS GLU ASN PRO ASN GLN TYR ASN TYR ILE ALA          
SEQRES   1 F   98  MET GLY THR ASN SER GLY ALA GLY LYS LYS ARG PHE GLU          
SEQRES   2 F   98  VAL LYS LYS TRP ASN ALA VAL ALA LEU TRP ALA TRP ASP          
SEQRES   3 F   98  ILE VAL VAL ASP ASN CYS ALA ILE CYS ARG ASN HIS ILE          
SEQRES   4 F   98  MET ASP LEU CYS ILE GLU CYS GLN ALA ASN GLN ALA SER          
SEQRES   5 F   98  ALA THR SER GLU GLU CYS THR VAL ALA TRP GLY VAL CYS          
SEQRES   6 F   98  ASN HIS ALA PHE HIS PHE HIS CYS ILE SER ARG TRP LEU          
SEQRES   7 F   98  LYS THR ARG GLN VAL CYS PRO LEU ASP ASN ARG GLU TRP          
SEQRES   8 F   98  GLU PHE GLN LYS TYR GLY HIS                                  
HET     ZN  D4001       1                                                       
HET     ZN  D4002       1                                                       
HET     ZN  D4003       1                                                       
HET     ZN  F4001       1                                                       
HET     ZN  F4002       1                                                       
HET     ZN  F4003       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   7   ZN    6(ZN 2+)                                                     
HELIX    1   1 HIS A    7  MET A   15  1                                   9    
HELIX    2   2 ASP A   19  LEU A   34  1                                  16    
HELIX    3   3 SER A   45  LEU A   57  1                                  13    
HELIX    4   4 ASN A   61  SER A   77  1                                  17    
HELIX    5   5 LYS A   80  SER A   97  1                                  18    
HELIX    6   6 LYS A   99  GLU A  116  1                                  18    
HELIX    7   7 LEU A  126  ALA A  143  1                                  18    
HELIX    8   8 ASP A  147  SER A  163  1                                  17    
HELIX    9   9 LEU A  169  ASN A  171  5                                   3    
HELIX   10  10 PHE A  172  LEU A  181  1                                  10    
HELIX   11  11 PRO A  182  LEU A  184  5                                   3    
HELIX   12  12 ARG A  188  CYS A  206  1                                  19    
HELIX   13  13 GLY A  207  ASN A  225  1                                  19    
HELIX   14  14 SER A  227  ARG A  232  1                                   6    
HELIX   15  15 ARG A  232  ALA A  245  1                                  14    
HELIX   16  16 HIS A  247  GLU A  251  5                                   5    
HELIX   17  17 ILE A  256  ASN A  265  1                                  10    
HELIX   18  18 ASP A  268  ARG A  284  1                                  17    
HELIX   19  19 PRO A  292  ILE A  300  1                                   9    
HELIX   20  20 SER A  346  SER A  362  1                                  17    
HELIX   21  21 GLU A  370  SER A  376  1                                   7    
HELIX   22  22 SER A  376  SER A  381  1                                   6    
HELIX   23  23 GLU A  387  THR A  405  1                                  19    
HELIX   24  24 THR A  423  MET A  443  1                                  21    
HELIX   25  25 SER A  447  LEU A  465  1                                  19    
HELIX   26  26 HIS A  472  VAL A  475  5                                   4    
HELIX   27  27 LEU A  476  ASP A  486  1                                  11    
HELIX   28  28 SER A  490  ASN A  507  1                                  18    
HELIX   29  29 PHE A  513  PRO A  515  5                                   3    
HELIX   30  30 HIS A  516  GLY A  529  1                                  14    
HELIX   31  31 PHE A  532  ARG A  551  1                                  20    
HELIX   32  32 ALA A  561  LYS A  577  1                                  17    
HELIX   33  33 ASP A  582  LEU A  600  1                                  19    
HELIX   34  34 SER A  606  ARG A  618  1                                  13    
HELIX   35  35 THR A  624  GLY A  637  1                                  14    
HELIX   36  36 LEU A  644  PHE A  658  1                                  15    
HELIX   37  37 LEU A  659  LYS A  661  5                                   3    
HELIX   38  38 ARG A  664  TYR A  681  1                                  18    
HELIX   39  39 THR A  686  ASP A  695  1                                  10    
HELIX   40  40 ASP A  705  TYR A  723  1                                  19    
HELIX   41  41 SER A  725  ILE A  730  5                                   6    
HELIX   42  42 SER A  733  ARG A  743  1                                  11    
HELIX   43  43 GLN A  748  ALA A  761  1                                  14    
HELIX   44  44 GLY A  771  GLY A  781  1                                  11    
HELIX   45  45 PRO A  782  TYR A  784  5                                   3    
HELIX   46  46 TYR A  796  ARG A  808  1                                  13    
HELIX   47  47 LYS A  812  LYS A  826  1                                  15    
HELIX   48  48 THR A  831  GLY A  846  1                                  16    
HELIX   49  49 LEU A  857  LEU A  862  1                                   6    
HELIX   50  50 GLU A  863  SER A  867  5                                   5    
HELIX   51  51 SER A  869  GLY A  886  1                                  18    
HELIX   52  52 ASN A  887  GLN A  902  1                                  16    
HELIX   53  53 ARG A  905  SER A  918  1                                  14    
HELIX   54  54 SER A  921  LYS A  926  1                                   6    
HELIX   55  55 TYR A  928  HIS A  939  1                                  12    
HELIX   56  56 GLU A  945  ASP A  962  1                                  18    
HELIX   57  57 ASP A  962  ILE A  975  1                                  14    
HELIX   58  58 TYR A  980  VAL A  989  1                                  10    
HELIX   59  59 ILE A 1000  LYS A 1013  1                                  14    
HELIX   60  60 LEU A 1020  LYS A 1037  1                                  18    
HELIX   61  61 PRO A 1038  ILE A 1041  5                                   4    
HELIX   62  62 LEU A 1044  GLU A 1055  1                                  12    
HELIX   63  63 LEU A 1079  CYS A 1096  1                                  18    
HELIX   64  64 LEU A 1097  LEU A 1100  5                                   4    
HELIX   65  65 ASP A 1101  GLY A 1112  1                                  12    
HELIX   66  66 HIS A 1116  CYS A 1134  1                                  19    
HELIX   67  67 CYS A 1134  LEU A 1142  1                                   9    
HELIX   68  68 ASP A 1143  LEU A 1145  5                                   3    
HELIX   69  69 VAL A 1146  THR A 1155  1                                  10    
HELIX   70  70 VAL A 1162  THR A 1185  1                                  24    
HELIX   71  71 SER A 1192  SER A 1203  1                                  12    
HELIX   72  72 ALA B    4  LYS B   14  1                                  11    
HELIX   73  73 ASP B   19  GLN B   35  1                                  17    
HELIX   74  74 ASP B   43  LEU B   56  1                                  14    
HELIX   75  75 ASN B   61  CYS B   71  1                                  11    
HELIX   76  76 CYS B   71  LYS B   78  1                                   8    
HELIX   77  77 LYS B   80  ASN B   94  1                                  15    
HELIX   78  78 GLN B  101  ILE B  114  1                                  14    
HELIX   79  79 GLY B  115  LEU B  117  5                                   3    
HELIX   80  80 SER B  124  ALA B  143  1                                  20    
HELIX   81  81 VAL B  150  SER B  163  1                                  14    
HELIX   82  82 GLY B  166  VAL B  170  5                                   5    
HELIX   83  83 PHE B  172  LEU B  181  1                                  10    
HELIX   84  84 PRO B  182  LEU B  184  5                                   3    
HELIX   85  85 ARG B  188  CYS B  206  1                                  19    
HELIX   86  86 ILE B  209  LYS B  224  1                                  16    
HELIX   87  87 SER B  227  ALA B  245  1                                  19    
HELIX   88  88 GLY B  246  GLU B  251  1                                   6    
HELIX   89  89 TYR B  252  LYS B  255  5                                   4    
HELIX   90  90 ILE B  256  ASN B  265  1                                  10    
HELIX   91  91 ASP B  268  CYS B  286  1                                  19    
HELIX   92  92 PRO B  292  LEU B  302  1                                  11    
HELIX   93  93 SER B  346  ARG B  364  1                                  19    
HELIX   94  94 MET B  367  VAL B  375  1                                   9    
HELIX   95  95 SER B  376  ILE B  380  1                                   5    
HELIX   96  96 SER B  381  GLU B  385  5                                   5    
HELIX   97  97 GLU B  388  ARG B  406  1                                  19    
HELIX   98  98 THR B  423  MET B  443  1                                  21    
HELIX   99  99 SER B  447  LEU B  465  1                                  19    
HELIX  100 100 HIS B  472  ASP B  486  1                                  15    
HELIX  101 101 SER B  490  ASN B  507  1                                  18    
HELIX  102 102 PHE B  513  GLY B  529  1                                  17    
HELIX  103 103 PHE B  532  ARG B  551  1                                  20    
HELIX  104 104 ALA B  561  PRO B  563  5                                   3    
HELIX  105 105 TYR B  564  LYS B  577  1                                  14    
HELIX  106 106 ASP B  582  LEU B  600  1                                  19    
HELIX  107 107 ASP B  607  LYS B  620  1                                  14    
HELIX  108 108 THR B  624  ALA B  636  1                                  13    
HELIX  109 109 LEU B  644  LEU B  659  1                                  16    
HELIX  110 110 GLN B  663  LEU B  674  1                                  12    
HELIX  111 111 LEU B  674  LYS B  679  1                                   6    
HELIX  112 112 TYR B  681  LEU B  685  5                                   5    
HELIX  113 113 MET B  689  LEU B  694  1                                   6    
HELIX  114 114 ASP B  695  LEU B  697  5                                   3    
HELIX  115 115 ASP B  705  TYR B  723  1                                  19    
HELIX  116 116 SER B  726  ILE B  730  5                                   5    
HELIX  117 117 GLY B  732  ARG B  743  1                                  12    
HELIX  118 118 GLN B  748  VAL B  764  1                                  17    
HELIX  119 119 GLY B  771  GLY B  781  1                                  11    
HELIX  120 120 PRO B  782  TYR B  784  5                                   3    
HELIX  121 121 GLN B  794  ARG B  808  1                                  15    
HELIX  122 122 GLY B  814  ILE B  822  1                                   9    
HELIX  123 123 THR B  831  GLY B  846  1                                  16    
HELIX  124 124 GLU B  856  PHE B  865  1                                  10    
HELIX  125 125 SER B  869  ASN B  887  1                                  19    
HELIX  126 126 ASN B  887  GLN B  902  1                                  16    
HELIX  127 127 ARG B  905  ALA B  920  1                                  16    
HELIX  128 128 SER B  921  LYS B  926  1                                   6    
HELIX  129 129 TYR B  928  LYS B  938  1                                  11    
HELIX  130 130 GLU B  944  LEU B  960  1                                  17    
HELIX  131 131 ASP B  962  LYS B  971  1                                  10    
HELIX  132 132 GLY B  972  GLY B  977  1                                   6    
HELIX  133 133 SER B  979  LYS B  990  1                                  12    
HELIX  134 134 ILE B 1000  PHE B 1011  1                                  12    
HELIX  135 135 ASN B 1021  LYS B 1037  1                                  17    
HELIX  136 136 LEU B 1044  THR B 1056  1                                  13    
HELIX  137 137 LEU B 1079  LEU B 1092  1                                  14    
HELIX  138 138 ASP B 1101  ASP B 1111  1                                  11    
HELIX  139 139 HIS B 1116  VAL B 1128  1                                  13    
HELIX  140 140 CYS B 1134  ARG B 1141  1                                   8    
HELIX  141 141 LEU B 1145  THR B 1155  1                                  11    
HELIX  142 142 VAL B 1162  ARG B 1174  1                                  13    
HELIX  143 143 MET B 1177  ILE B 1186  1                                  10    
HELIX  144 144 SER B 1192  ASN B 1205  1                                  14    
HELIX  145 145 ASN B 1205  ALA B 1210  1                                   6    
HELIX  146 146 ALA C  223  GLN C  228  1                                   6    
HELIX  147 147 ASN C  236  VAL C  244  1                                   9    
HELIX  148 148 LEU C  256  ILE C  263  1                                   8    
HELIX  149 149 CYS C  264  LYS C  269  1                                   6    
HELIX  150 150 ALA C  270  PHE C  275  5                                   6    
HELIX  151 151 ASP C  281  PHE C  307  1                                  27    
HELIX  152 152 LEU C  308  ASP C  311  5                                   4    
HELIX  153 153 SER C  323  ILE C  336  1                                  14    
HELIX  154 154 VAL C  342  GLY C  360  1                                  19    
HELIX  155 155 ASP C  364  LEU C  378  1                                  15    
HELIX  156 156 ILE C  380  PHE C  385  1                                   6    
HELIX  157 157 PHE C  385  ARG C  408  1                                  24    
HELIX  158 158 GLU C  409  TYR C  431  1                                  23    
HELIX  159 159 THR C  436  LEU C  449  1                                  14    
HELIX  160 160 HIS C  452  LEU C  461  1                                  10    
HELIX  161 161 LEU C  461  ASP C  466  1                                   6    
HELIX  162 162 ARG C  469  VAL C  483  1                                  15    
HELIX  163 163 GLY C  485  ILE C  507  1                                  23    
HELIX  164 164 GLU C  510  LYS C  513  5                                   4    
HELIX  165 165 THR C  514  CYS C  533  1                                  20    
HELIX  166 166 PHE C  540  ILE C  552  1                                  13    
HELIX  167 167 ASN C  557  LEU C  571  1                                  15    
HELIX  168 168 GLU C  584  ARG C  595  1                                  12    
HELIX  169 169 LYS C  600  VAL C  617  1                                  18    
HELIX  170 170 SER C  622  HIS C  635  1                                  14    
HELIX  171 171 THR C  642  LEU C  654  1                                  13    
HELIX  172 172 ILE C  658  MET C  666  1                                   9    
HELIX  173 173 GLY C  685  TRP C  687  5                                   3    
HELIX  174 174 PRO C  698  LEU C  713  1                                  16    
HELIX  175 175 LEU C  747  LEU C  751  1                                   5    
HELIX  176 176 LEU C  764  GLY C  772  1                                   9    
HELIX  177 177 GLU C  774  LEU C  782  1                                   9    
HELIX  178 178 GLN C  783  GLY C  788  1                                   6    
HELIX  179 179 THR C  831  ARG C  861  1                                  31    
HELIX  180 180 LEU C  869  LEU C  877  1                                   9    
HELIX  181 181 LYS C  882  ILE C  894  1                                  13    
HELIX  182 182 ASP C  895  ASP C  897  5                                   3    
HELIX  183 183 CYS D   53  ALA D   58  1                                   6    
HELIX  184 184 THR D   64  CYS D   68  5                                   5    
HELIX  185 185 PHE D   81  ARG D   86  1                                   6    
HELIX  186 186 TRP D   87  LYS D   89  5                                   3    
HELIX  187 187 ASN E  211  TRP E  217  1                                   7    
HELIX  188 188 ALA E  223  GLN E  228  1                                   6    
HELIX  189 189 GLU E  239  GLU E  245  1                                   7    
HELIX  190 190 SER E  253  LYS E  269  1                                  17    
HELIX  191 191 GLN E  271  ARG E  276  1                                   6    
HELIX  192 192 ASP E  281  PHE E  307  1                                  27    
HELIX  193 193 PHE E  307  THR E  313  1                                   7    
HELIX  194 194 THR E  313  ASN E  318  1                                   6    
HELIX  195 195 SER E  323  ILE E  336  1                                  14    
HELIX  196 196 LYS E  341  ARG E  358  1                                  18    
HELIX  197 197 ASP E  364  LEU E  378  1                                  15    
HELIX  198 198 ILE E  380  PHE E  385  1                                   6    
HELIX  199 199 PHE E  385  LEU E  404  1                                  20    
HELIX  200 200 GLU E  409  TYR E  431  1                                  23    
HELIX  201 201 ASP E  433  THR E  435  5                                   3    
HELIX  202 202 THR E  436  LEU E  449  1                                  14    
HELIX  203 203 HIS E  452  GLY E  460  1                                   9    
HELIX  204 204 GLY E  460  GLU E  467  1                                   8    
HELIX  205 205 ARG E  469  SER E  481  1                                  13    
HELIX  206 206 GLY E  485  VAL E  506  1                                  22    
HELIX  207 207 ASN E  508  ASP E  512  5                                   5    
HELIX  208 208 MET E  515  CYS E  533  1                                  19    
HELIX  209 209 ASN E  537  ASN E  553  1                                  17    
HELIX  210 210 ASN E  557  LYS E  570  1                                  14    
HELIX  211 211 LEU E  583  ARG E  595  1                                  13    
HELIX  212 212 LYS E  600  VAL E  617  1                                  18    
HELIX  213 213 ASP E  624  LYS E  632  1                                   9    
HELIX  214 214 ALA E  639  LYS E  644  1                                   6    
HELIX  215 215 GLU E  646  ASN E  670  1                                  25    
HELIX  216 216 GLU E  700  GLN E  705  1                                   6    
HELIX  217 217 GLN E  705  LEU E  713  1                                   9    
HELIX  218 218 LEU E  747  MET E  755  1                                   9    
HELIX  219 219 PHE E  756  GLU E  758  5                                   3    
HELIX  220 220 LEU E  764  GLY E  772  1                                   9    
HELIX  221 221 GLU E  774  LEU E  782  1                                   9    
HELIX  222 222 GLN E  825  LYS E  829  5                                   5    
HELIX  223 223 THR E  831  ARG E  861  1                                  31    
HELIX  224 224 LEU E  869  LEU E  877  1                                   9    
HELIX  225 225 LYS E  882  ASP E  895  1                                  14    
HELIX  226 226 ILE F   37  ASN F   41  5                                   5    
HELIX  227 227 HIS F   80  ARG F   91  1                                  12    
SHEET    1  AA 2 ILE A1063  GLU A1065  0                                        
SHEET    2  AA 2 THR A1074  ASP A1076 -1  O  VAL A1075   N  ARG A1064           
SHEET    1  CA 2 GLU C 676  THR C 683  0                                        
SHEET    2  CA 2 LYS D  26  TRP D  35  1  O  TRP D  27   N  THR C 678           
SHEET    1  CB 2 ARG C 719  TRP C 723  0                                        
SHEET    2  CB 2 LYS D  26  TRP D  35  1  O  LEU D  32   N  GLN C 722           
SHEET    1  CC 5 ILE C 821  LYS C 822  0                                        
SHEET    2  CC 5 LEU C 743  SER C 746  1  N  GLN C 744   O  ILE C 821           
SHEET    3  CC 5 HIS C 729  VAL C 731 -1  O  CYS C 730   N  VAL C 745           
SHEET    4  CC 5 LYS D  26  TRP D  35 -1  O  LYS D  26   N  VAL C 731           
SHEET    5  CC 5 ARG C 719  TRP C 723  1  O  LYS C 720   N  ALA D  34           
SHEET    1  CD 5 ILE C 821  LYS C 822  0                                        
SHEET    2  CD 5 LEU C 743  SER C 746  1  N  GLN C 744   O  ILE C 821           
SHEET    3  CD 5 HIS C 729  VAL C 731 -1  O  CYS C 730   N  VAL C 745           
SHEET    4  CD 5 LYS D  26  TRP D  35 -1  O  LYS D  26   N  VAL C 731           
SHEET    5  CD 5 GLU C 676  THR C 683  1  O  GLU C 676   N  TRP D  27           
SHEET    1  CE 2 ALA C 734  GLU C 735  0                                        
SHEET    2  CE 2 LYS C 740  LYS C 741 -1  O  LYS C 741   N  ALA C 734           
SHEET    1  CF 3 PHE C 762  SER C 763  0                                        
SHEET    2  CF 3 LYS C 807  CYS C 810 -1  O  PHE C 808   N  PHE C 762           
SHEET    3  CF 3 LEU C 793  LYS C 795 -1  O  ALA C 794   N  ILE C 809           
SHEET    1  CG 3 THR C 863  SER C 865  0                                        
SHEET    2  CG 3 GLN C 908  ASN C 910 -1  O  TYR C 909   N  LEU C 864           
SHEET    3  CG 3 GLU C 900  ARG C 901 -1  O  GLU C 900   N  ASN C 910           
SHEET    1  DA 3 ALA D  78  HIS D  80  0                                        
SHEET    2  DA 3 VAL D  70  TRP D  72 -1  O  ALA D  71   N  PHE D  79           
SHEET    3  DA 3 LYS D 105  TYR D 106 -1  O  LYS D 105   N  TRP D  72           
SHEET    1  EA 2 GLU E 676  LEU E 677  0                                        
SHEET    2  EA 2 LYS F  26  TRP F  35 -1  N  TRP F  27   O  GLU E 676           
SHEET    1  EB 2 ASN E 680  THR E 683  0                                        
SHEET    2  EB 2 LYS F  26  TRP F  35  1  O  ALA F  29   N  ASN E 680           
SHEET    1  EC 4 ILE E 821  LYS E 822  0                                        
SHEET    2  EC 4 GLU E 742  SER E 746  1  O  GLU E 742   N  ILE E 821           
SHEET    3  EC 4 ARG E 719  ALA E 734 -1  O  CYS E 730   N  VAL E 745           
SHEET    4  EC 4 PHE F  22  VAL F  24  1  O  GLU F  23   N  LYS E 733           
SHEET    1  ED 5 ILE E 821  LYS E 822  0                                        
SHEET    2  ED 5 GLU E 742  SER E 746  1  O  GLU E 742   N  ILE E 821           
SHEET    3  ED 5 ARG E 719  ALA E 734 -1  O  CYS E 730   N  VAL E 745           
SHEET    4  ED 5 LYS F  26  TRP F  35 -1  N  LYS F  26   O  VAL E 731           
SHEET    5  ED 5 ASN E 680  THR E 683  1  O  ASN E 680   N  ALA F  31           
SHEET    1  FA 2 PHE F  22  VAL F  24  0                                        
SHEET    2  FA 2 ARG E 719  ALA E 734  1  O  LYS E 733   N  GLU F  23           
SHEET    1  EE 5 ILE E 821  LYS E 822  0                                        
SHEET    2  EE 5 GLU E 742  SER E 746  1  O  GLU E 742   N  ILE E 821           
SHEET    3  EE 5 ARG E 719  ALA E 734 -1  O  CYS E 730   N  VAL E 745           
SHEET    4  EE 5 LYS F  26  TRP F  35 -1  N  LYS F  26   O  VAL E 731           
SHEET    5  EE 5 GLU E 676  LEU E 677 -1  O  GLU E 676   N  TRP F  27           
SHEET    1  EF 3 PHE E 762  SER E 763  0                                        
SHEET    2  EF 3 LYS E 807  CYS E 810 -1  O  PHE E 808   N  PHE E 762           
SHEET    3  EF 3 LEU E 793  LYS E 795 -1  O  ALA E 794   N  ILE E 809           
SHEET    1  EG 3 THR E 863  SER E 865  0                                        
SHEET    2  EG 3 GLN E 908  ASN E 910 -1  O  TYR E 909   N  LEU E 864           
SHEET    3  EG 3 GLU E 900  ARG E 901 -1  O  GLU E 900   N  ASN E 910           
SHEET    1  FB 2 ALA F  71  TRP F  72  0                                        
SHEET    2  FB 2 LYS F 105  TYR F 106 -1  O  LYS F 105   N  TRP F  72           
LINK        ZN    ZN D4001                 SG  CYS D  45     1555   1555  2.37  
LINK        ZN    ZN D4001                 ND1 HIS D  80     1555   1555  2.03  
LINK        ZN    ZN D4001                 SG  CYS D  83     1555   1555  2.59  
LINK        ZN    ZN D4001                 SG  CYS D  42     1555   1555  2.04  
LINK        ZN    ZN D4002                 ND1 HIS D  77     1555   1555  2.11  
LINK        ZN    ZN D4002                 SG  CYS D  94     1555   1555  2.55  
LINK        ZN    ZN D4002                 SG  CYS D  75     1555   1555  2.39  
LINK        ZN    ZN D4003                 SG  CYS D  56     1555   1555  2.31  
LINK        ZN    ZN D4003                 SG  CYS D  68     1555   1555  2.84  
LINK        ZN    ZN D4003                 SG  CYS D  53     1555   1555  2.56  
LINK         SG  CYS F  45                ZN    ZN F4001     1555   1555  1.74  
LINK        ZN    ZN F4001                 SG  CYS F  42     1555   1555  2.41  
LINK        ZN    ZN F4001                 ND1 HIS F  80     1555   1555  2.48  
LINK        ZN    ZN F4002                 SG  CYS F  94     1555   1555  2.39  
LINK        ZN    ZN F4002                 ND1 HIS F  77     1555   1555  2.68  
LINK        ZN    ZN F4002                 SG  CYS F  75     1555   1555  2.15  
LINK        ZN    ZN F4003                 SG  CYS F  53     1555   1555  2.66  
LINK        ZN    ZN F4003                 SG  CYS F  68     1555   1555  2.46  
LINK        ZN    ZN F4003                 SG  CYS F  56     1555   1555  2.47  
SITE     1 AC1  4 CYS D  42  CYS D  45  HIS D  80  CYS D  83                    
SITE     1 AC2  4 CYS D  75  HIS D  77  CYS D  94  ASP D  97                    
SITE     1 AC3  4 CYS D  53  CYS D  56  CYS D  68  HIS D  82                    
SITE     1 AC4  4 CYS F  42  CYS F  45  HIS F  80  CYS F  83                    
SITE     1 AC5  4 CYS F  75  HIS F  77  CYS F  94  ASP F  97                    
SITE     1 AC6  4 CYS F  53  CYS F  56  CYS F  68  HIS F  82                    
CRYST1   77.090  152.360  263.010  90.00  89.37  90.00 P 1 21 1      4          
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      0.012972  0.000000 -0.000143        0.00000                         
SCALE2      0.000000  0.006563  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003802        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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