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Database: PDB
Entry: 4KMH
LinkDB: 4KMH
Original site: 4KMH 
HEADER    PROTEIN BINDING                         08-MAY-13   4KMH              
TITLE     CRYSTAL STRUCTURE OF SUPPRESSOR OF FUSED D20                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPPRESSOR OF FUSED HOMOLOG;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 1-305, 326-484;                               
COMPND   5 SYNONYM: SUFUH;                                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SUFU, UNQ650/PRO1280;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    HELIX AND BETA STRAND, PROTEIN BINDING                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHANG,X.QI,Z.ZHANG,G.WU                                             
REVDAT   5   15-NOV-17 4KMH    1       REMARK                                   
REVDAT   4   23-AUG-17 4KMH    1       SOURCE REMARK                            
REVDAT   3   12-FEB-14 4KMH    1       JRNL                                     
REVDAT   2   27-NOV-13 4KMH    1       REMARK                                   
REVDAT   1   20-NOV-13 4KMH    0                                                
JRNL        AUTH   Y.ZHANG,L.FU,X.QI,Z.ZHANG,Y.XIA,J.JIA,J.JIANG,Y.ZHAO,G.WU    
JRNL        TITL   STRUCTURAL INSIGHT INTO THE MUTUAL RECOGNITION AND           
JRNL        TITL 2 REGULATION BETWEEN SUPPRESSOR OF FUSED AND GLI/CI.           
JRNL        REF    NAT COMMUN                    V.   4  2608 2013              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   24217340                                                     
JRNL        DOI    10.1038/NCOMMS3608                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.04 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 19786                          
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) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1010                            
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) : 3.04                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.12                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1070                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.08                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3180                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 57                           
REMARK   3   BIN FREE R VALUE                    : 0.3410                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6063                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 12                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 86.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.27000                                              
REMARK   3    B22 (A**2) : 7.27000                                              
REMARK   3    B33 (A**2) : -8.52000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.14000                                              
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): 0.492         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.409         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 51.335        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.931                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.897                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6236 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8491 ; 0.974 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   764 ; 4.907 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   290 ;35.539 ;24.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   970 ;15.689 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;16.250 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   913 ; 0.060 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4842 ; 0.003 ; 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):  3845 ; 1.582 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6201 ; 2.338 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2391 ; 0.494 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2290 ; 0.897 ; 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  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H,K,L                                           
REMARK   3      TWIN FRACTION : 0.6320                                          
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : -H,-K,L                                         
REMARK   3      TWIN FRACTION : 0.3680                                          
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -3        A   481                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.6100 -16.8537  25.1674              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0983 T22:   0.0857                                     
REMARK   3      T33:   0.0719 T12:   0.0818                                     
REMARK   3      T13:   0.0429 T23:   0.0179                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7687 L22:   0.3135                                     
REMARK   3      L33:   2.3569 L12:   0.1672                                     
REMARK   3      L13:  -0.5353 L23:  -0.1274                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0170 S12:   0.0162 S13:  -0.0583                       
REMARK   3      S21:  -0.0082 S22:  -0.0647 S23:  -0.0023                       
REMARK   3      S31:   0.3386 S32:   0.2923 S33:   0.0817                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    -6        B   481                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.1672  17.2660  34.0359              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1251 T22:   0.0889                                     
REMARK   3      T33:   0.0903 T12:  -0.0900                                     
REMARK   3      T13:  -0.0663 T23:   0.0274                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6696 L22:   0.2229                                     
REMARK   3      L33:   2.4929 L12:  -0.2376                                     
REMARK   3      L13:   0.3423 L23:  -0.0474                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0256 S12:   0.0062 S13:   0.0772                       
REMARK   3      S21:   0.0144 S22:  -0.0647 S23:  -0.0227                       
REMARK   3      S31:  -0.3508 S32:   0.2986 S33:   0.0903                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   501        A   506                          
REMARK   3    RESIDUE RANGE :   B   501        B   506                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.0046   6.1788  29.1895              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3241 T22:   0.0687                                     
REMARK   3      T33:   0.5006 T12:   0.0282                                     
REMARK   3      T13:  -0.1106 T23:  -0.0590                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0782 L22:   0.1320                                     
REMARK   3      L33:   0.8072 L12:  -0.0309                                     
REMARK   3      L13:  -0.2393 L23:   0.0700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0200 S12:  -0.0583 S13:   0.0089                       
REMARK   3      S21:  -0.0532 S22:   0.0733 S23:  -0.0869                       
REMARK   3      S31:  -0.0319 S32:   0.1536 S33:  -0.0533                       
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: RESIDUAL ONLY                                   
REMARK   4                                                                      
REMARK   4 4KMH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-MAY-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000079522.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-MAY-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19786                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 118.750                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.12800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4KM8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 3350, 0.1M AMMONIUM TARTRATE,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       36.81700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.16450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       36.81700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       61.16450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 36580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     ARG A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     PRO A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     PRO A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     PRO A    18                                                      
REMARK 465     GLY A    19                                                      
REMARK 465     ARG A   280                                                      
REMARK 465     PRO A   281                                                      
REMARK 465     PRO A   282                                                      
REMARK 465     GLU A   283                                                      
REMARK 465     ASP A   284                                                      
REMARK 465     ASP A   285                                                      
REMARK 465     GLU A   286                                                      
REMARK 465     ASP A   287                                                      
REMARK 465     SER A   288                                                      
REMARK 465     ARG A   289                                                      
REMARK 465     SER A   290                                                      
REMARK 465     ILE A   291                                                      
REMARK 465     CYS A   292                                                      
REMARK 465     ILE A   293                                                      
REMARK 465     GLY A   294                                                      
REMARK 465     THR A   295                                                      
REMARK 465     GLN A   296                                                      
REMARK 465     PRO A   297                                                      
REMARK 465     ARG A   298                                                      
REMARK 465     ARG A   299                                                      
REMARK 465     LEU A   300                                                      
REMARK 465     SER A   301                                                      
REMARK 465     GLY A   302                                                      
REMARK 465     LYS A   303                                                      
REMARK 465     ASP A   304                                                      
REMARK 465     THR A   305                                                      
REMARK 465     PRO A   326                                                      
REMARK 465     ILE A   327                                                      
REMARK 465     ASN A   328                                                      
REMARK 465     PRO A   329                                                      
REMARK 465     GLN A   330                                                      
REMARK 465     ARG A   331                                                      
REMARK 465     GLN A   332                                                      
REMARK 465     ASN A   333                                                      
REMARK 465     GLY A   334                                                      
REMARK 465     LEU A   335                                                      
REMARK 465     ALA A   336                                                      
REMARK 465     HIS A   337                                                      
REMARK 465     ASP A   338                                                      
REMARK 465     ARG A   339                                                      
REMARK 465     ALA A   340                                                      
REMARK 465     PRO A   341                                                      
REMARK 465     SER A   342                                                      
REMARK 465     ARG A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     ASP A   345                                                      
REMARK 465     SER A   346                                                      
REMARK 465     LEU A   347                                                      
REMARK 465     GLU A   348                                                      
REMARK 465     SER A   349                                                      
REMARK 465     ASP A   350                                                      
REMARK 465     SER A   351                                                      
REMARK 465     SER A   352                                                      
REMARK 465     THR A   353                                                      
REMARK 465     ALA A   354                                                      
REMARK 465     ILE A   355                                                      
REMARK 465     ILE A   356                                                      
REMARK 465     PRO A   357                                                      
REMARK 465     HIS A   358                                                      
REMARK 465     GLU A   359                                                      
REMARK 465     LEU A   360                                                      
REMARK 465     ILE A   361                                                      
REMARK 465     THR A   451                                                      
REMARK 465     SER A   452                                                      
REMARK 465     PRO A   453                                                      
REMARK 465     GLU A   454                                                      
REMARK 465     PRO A   482                                                      
REMARK 465     LEU A   483                                                      
REMARK 465     HIS A   484                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     PRO B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     PRO B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 465     ALA B    14                                                      
REMARK 465     PRO B    15                                                      
REMARK 465     PRO B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     PRO B    18                                                      
REMARK 465     GLY B    19                                                      
REMARK 465     PRO B   281                                                      
REMARK 465     PRO B   282                                                      
REMARK 465     GLU B   283                                                      
REMARK 465     ASP B   284                                                      
REMARK 465     ASP B   285                                                      
REMARK 465     GLU B   286                                                      
REMARK 465     ASP B   287                                                      
REMARK 465     SER B   288                                                      
REMARK 465     ARG B   289                                                      
REMARK 465     SER B   290                                                      
REMARK 465     ILE B   291                                                      
REMARK 465     CYS B   292                                                      
REMARK 465     ILE B   293                                                      
REMARK 465     GLY B   294                                                      
REMARK 465     THR B   295                                                      
REMARK 465     GLN B   296                                                      
REMARK 465     PRO B   297                                                      
REMARK 465     ARG B   298                                                      
REMARK 465     ARG B   299                                                      
REMARK 465     LEU B   300                                                      
REMARK 465     SER B   301                                                      
REMARK 465     GLY B   302                                                      
REMARK 465     LYS B   303                                                      
REMARK 465     ASP B   304                                                      
REMARK 465     THR B   305                                                      
REMARK 465     PRO B   326                                                      
REMARK 465     ILE B   327                                                      
REMARK 465     ASN B   328                                                      
REMARK 465     PRO B   329                                                      
REMARK 465     GLN B   330                                                      
REMARK 465     ARG B   331                                                      
REMARK 465     GLN B   332                                                      
REMARK 465     ASN B   333                                                      
REMARK 465     GLY B   334                                                      
REMARK 465     LEU B   335                                                      
REMARK 465     ALA B   336                                                      
REMARK 465     HIS B   337                                                      
REMARK 465     ASP B   338                                                      
REMARK 465     ARG B   339                                                      
REMARK 465     ALA B   340                                                      
REMARK 465     PRO B   341                                                      
REMARK 465     SER B   342                                                      
REMARK 465     ARG B   343                                                      
REMARK 465     LYS B   344                                                      
REMARK 465     ASP B   345                                                      
REMARK 465     SER B   346                                                      
REMARK 465     LEU B   347                                                      
REMARK 465     GLU B   348                                                      
REMARK 465     SER B   349                                                      
REMARK 465     ASP B   350                                                      
REMARK 465     SER B   351                                                      
REMARK 465     SER B   352                                                      
REMARK 465     THR B   353                                                      
REMARK 465     ALA B   354                                                      
REMARK 465     ILE B   355                                                      
REMARK 465     ILE B   356                                                      
REMARK 465     PRO B   357                                                      
REMARK 465     HIS B   358                                                      
REMARK 465     GLU B   359                                                      
REMARK 465     LEU B   360                                                      
REMARK 465     THR B   451                                                      
REMARK 465     SER B   452                                                      
REMARK 465     PRO B   453                                                      
REMARK 465     GLU B   454                                                      
REMARK 465     GLU B   455                                                      
REMARK 465     PRO B   482                                                      
REMARK 465     LEU B   483                                                      
REMARK 465     HIS B   484                                                      
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     ARG A  -3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO A  20    CG   CD                                             
REMARK 470     THR A  21    OG1  CG2                                            
REMARK 470     GLU A 455    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 456    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 457    CG   CD   CE   NZ                                   
REMARK 470     LEU B  -6    CG   CD1  CD2                                       
REMARK 470     ARG B  -3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO B  20    CG   CD                                             
REMARK 470     ARG B 280    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 361    CG1  CG2  CD1                                       
REMARK 470     ARG B 362    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B 456    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 457    CG   CD   CE   NZ                                   
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  21      -63.70     65.98                                   
REMARK 500    SER A  79       82.28   -156.87                                   
REMARK 500    VAL A 104      -53.10   -123.85                                   
REMARK 500    ASN A 169        8.96     58.16                                   
REMARK 500    TRP A 214     -108.59   -115.55                                   
REMARK 500    ARG A 388      -61.59   -132.14                                   
REMARK 500    GLU A 448     -106.31    -91.09                                   
REMARK 500    LYS A 457       36.35   -153.27                                   
REMARK 500    PRO B  -4      125.79    -37.85                                   
REMARK 500    THR B  21      -14.99     61.20                                   
REMARK 500    PHE B  26       70.19     62.47                                   
REMARK 500    SER B  79       80.64   -150.03                                   
REMARK 500    VAL B 104      -44.53   -131.07                                   
REMARK 500    SER B 172      131.36    -24.11                                   
REMARK 500    ILE B 174      100.86    -56.82                                   
REMARK 500    TRP B 214     -119.26    -93.22                                   
REMARK 500    ARG B 388      -63.96   -121.22                                   
REMARK 500    ASP B 449      116.96    -30.26                                   
REMARK 500    ASP B 480       34.80    -90.65                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4KM8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KM9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KMA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KMD   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 UNP RESIDUES 306-325 ARE DELETION.                                   
DBREF  4KMH A    1   305  UNP    Q9UMX1   SUFU_HUMAN       1    305             
DBREF  4KMH A  326   484  UNP    Q9UMX1   SUFU_HUMAN     326    484             
DBREF  4KMH B    1   305  UNP    Q9UMX1   SUFU_HUMAN       1    305             
DBREF  4KMH B  326   484  UNP    Q9UMX1   SUFU_HUMAN     326    484             
SEQADV 4KMH MET A  -19  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH GLY A  -18  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH SER A  -17  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH SER A  -16  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH HIS A  -15  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH HIS A  -14  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH HIS A  -13  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH HIS A  -12  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH HIS A  -11  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH HIS A  -10  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH SER A   -9  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH SER A   -8  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH GLY A   -7  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH LEU A   -6  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH VAL A   -5  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH PRO A   -4  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH ARG A   -3  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH GLY A   -2  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH SER A   -1  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH HIS A    0  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH MET B  -19  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH GLY B  -18  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH SER B  -17  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH SER B  -16  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH HIS B  -15  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH HIS B  -14  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH HIS B  -13  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH HIS B  -12  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH HIS B  -11  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH HIS B  -10  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH SER B   -9  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH SER B   -8  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH GLY B   -7  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH LEU B   -6  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH VAL B   -5  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH PRO B   -4  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH ARG B   -3  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH GLY B   -2  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH SER B   -1  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMH HIS B    0  UNP  Q9UMX1              EXPRESSION TAG                 
SEQRES   1 A  484  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  484  LEU VAL PRO ARG GLY SER HIS MET ALA GLU LEU ARG PRO          
SEQRES   3 A  484  SER GLY ALA PRO GLY PRO THR ALA PRO PRO ALA PRO GLY          
SEQRES   4 A  484  PRO THR ALA PRO PRO ALA PHE ALA SER LEU PHE PRO PRO          
SEQRES   5 A  484  GLY LEU HIS ALA ILE TYR GLY GLU CYS ARG ARG LEU TYR          
SEQRES   6 A  484  PRO ASP GLN PRO ASN PRO LEU GLN VAL THR ALA ILE VAL          
SEQRES   7 A  484  LYS TYR TRP LEU GLY GLY PRO ASP PRO LEU ASP TYR VAL          
SEQRES   8 A  484  SER MET TYR ARG ASN VAL GLY SER PRO SER ALA ASN ILE          
SEQRES   9 A  484  PRO GLU HIS TRP HIS TYR ILE SER PHE GLY LEU SER ASP          
SEQRES  10 A  484  LEU TYR GLY ASP ASN ARG VAL HIS GLU PHE THR GLY THR          
SEQRES  11 A  484  ASP GLY PRO SER GLY PHE GLY PHE GLU LEU THR PHE ARG          
SEQRES  12 A  484  LEU LYS ARG GLU THR GLY GLU SER ALA PRO PRO THR TRP          
SEQRES  13 A  484  PRO ALA GLU LEU MET GLN GLY LEU ALA ARG TYR VAL PHE          
SEQRES  14 A  484  GLN SER GLU ASN THR PHE CYS SER GLY ASP HIS VAL SER          
SEQRES  15 A  484  TRP HIS SER PRO LEU ASP ASN SER GLU SER ARG ILE GLN          
SEQRES  16 A  484  HIS MET LEU LEU THR GLU ASP PRO GLN MET GLN PRO VAL          
SEQRES  17 A  484  GLN THR PRO PHE GLY VAL VAL THR PHE LEU GLN ILE VAL          
SEQRES  18 A  484  GLY VAL CYS THR GLU GLU LEU HIS SER ALA GLN GLN TRP          
SEQRES  19 A  484  ASN GLY GLN GLY ILE LEU GLU LEU LEU ARG THR VAL PRO          
SEQRES  20 A  484  ILE ALA GLY GLY PRO TRP LEU ILE THR ASP MET ARG ARG          
SEQRES  21 A  484  GLY GLU THR ILE PHE GLU ILE ASP PRO HIS LEU GLN GLU          
SEQRES  22 A  484  ARG VAL ASP LYS GLY ILE GLU THR ASP GLY SER ASN LEU          
SEQRES  23 A  484  SER GLY VAL SER ALA LYS CYS ALA TRP ASP ASP LEU SER          
SEQRES  24 A  484  ARG PRO PRO GLU ASP ASP GLU ASP SER ARG SER ILE CYS          
SEQRES  25 A  484  ILE GLY THR GLN PRO ARG ARG LEU SER GLY LYS ASP THR          
SEQRES  26 A  484  PRO ILE ASN PRO GLN ARG GLN ASN GLY LEU ALA HIS ASP          
SEQRES  27 A  484  ARG ALA PRO SER ARG LYS ASP SER LEU GLU SER ASP SER          
SEQRES  28 A  484  SER THR ALA ILE ILE PRO HIS GLU LEU ILE ARG THR ARG          
SEQRES  29 A  484  GLN LEU GLU SER VAL HIS LEU LYS PHE ASN GLN GLU SER          
SEQRES  30 A  484  GLY ALA LEU ILE PRO LEU CYS LEU ARG GLY ARG LEU LEU          
SEQRES  31 A  484  HIS GLY ARG HIS PHE THR TYR LYS SER ILE THR GLY ASP          
SEQRES  32 A  484  MET ALA ILE THR PHE VAL SER THR GLY VAL GLU GLY ALA          
SEQRES  33 A  484  PHE ALA THR GLU GLU HIS PRO TYR ALA ALA HIS GLY PRO          
SEQRES  34 A  484  TRP LEU GLN ILE LEU LEU THR GLU GLU PHE VAL GLU LYS          
SEQRES  35 A  484  MET LEU GLU ASP LEU GLU ASP LEU THR SER PRO GLU GLU          
SEQRES  36 A  484  PHE LYS LEU PRO LYS GLU TYR SER TRP PRO GLU LYS LYS          
SEQRES  37 A  484  LEU LYS VAL SER ILE LEU PRO ASP VAL VAL PHE ASP SER          
SEQRES  38 A  484  PRO LEU HIS                                                  
SEQRES   1 B  484  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  484  LEU VAL PRO ARG GLY SER HIS MET ALA GLU LEU ARG PRO          
SEQRES   3 B  484  SER GLY ALA PRO GLY PRO THR ALA PRO PRO ALA PRO GLY          
SEQRES   4 B  484  PRO THR ALA PRO PRO ALA PHE ALA SER LEU PHE PRO PRO          
SEQRES   5 B  484  GLY LEU HIS ALA ILE TYR GLY GLU CYS ARG ARG LEU TYR          
SEQRES   6 B  484  PRO ASP GLN PRO ASN PRO LEU GLN VAL THR ALA ILE VAL          
SEQRES   7 B  484  LYS TYR TRP LEU GLY GLY PRO ASP PRO LEU ASP TYR VAL          
SEQRES   8 B  484  SER MET TYR ARG ASN VAL GLY SER PRO SER ALA ASN ILE          
SEQRES   9 B  484  PRO GLU HIS TRP HIS TYR ILE SER PHE GLY LEU SER ASP          
SEQRES  10 B  484  LEU TYR GLY ASP ASN ARG VAL HIS GLU PHE THR GLY THR          
SEQRES  11 B  484  ASP GLY PRO SER GLY PHE GLY PHE GLU LEU THR PHE ARG          
SEQRES  12 B  484  LEU LYS ARG GLU THR GLY GLU SER ALA PRO PRO THR TRP          
SEQRES  13 B  484  PRO ALA GLU LEU MET GLN GLY LEU ALA ARG TYR VAL PHE          
SEQRES  14 B  484  GLN SER GLU ASN THR PHE CYS SER GLY ASP HIS VAL SER          
SEQRES  15 B  484  TRP HIS SER PRO LEU ASP ASN SER GLU SER ARG ILE GLN          
SEQRES  16 B  484  HIS MET LEU LEU THR GLU ASP PRO GLN MET GLN PRO VAL          
SEQRES  17 B  484  GLN THR PRO PHE GLY VAL VAL THR PHE LEU GLN ILE VAL          
SEQRES  18 B  484  GLY VAL CYS THR GLU GLU LEU HIS SER ALA GLN GLN TRP          
SEQRES  19 B  484  ASN GLY GLN GLY ILE LEU GLU LEU LEU ARG THR VAL PRO          
SEQRES  20 B  484  ILE ALA GLY GLY PRO TRP LEU ILE THR ASP MET ARG ARG          
SEQRES  21 B  484  GLY GLU THR ILE PHE GLU ILE ASP PRO HIS LEU GLN GLU          
SEQRES  22 B  484  ARG VAL ASP LYS GLY ILE GLU THR ASP GLY SER ASN LEU          
SEQRES  23 B  484  SER GLY VAL SER ALA LYS CYS ALA TRP ASP ASP LEU SER          
SEQRES  24 B  484  ARG PRO PRO GLU ASP ASP GLU ASP SER ARG SER ILE CYS          
SEQRES  25 B  484  ILE GLY THR GLN PRO ARG ARG LEU SER GLY LYS ASP THR          
SEQRES  26 B  484  PRO ILE ASN PRO GLN ARG GLN ASN GLY LEU ALA HIS ASP          
SEQRES  27 B  484  ARG ALA PRO SER ARG LYS ASP SER LEU GLU SER ASP SER          
SEQRES  28 B  484  SER THR ALA ILE ILE PRO HIS GLU LEU ILE ARG THR ARG          
SEQRES  29 B  484  GLN LEU GLU SER VAL HIS LEU LYS PHE ASN GLN GLU SER          
SEQRES  30 B  484  GLY ALA LEU ILE PRO LEU CYS LEU ARG GLY ARG LEU LEU          
SEQRES  31 B  484  HIS GLY ARG HIS PHE THR TYR LYS SER ILE THR GLY ASP          
SEQRES  32 B  484  MET ALA ILE THR PHE VAL SER THR GLY VAL GLU GLY ALA          
SEQRES  33 B  484  PHE ALA THR GLU GLU HIS PRO TYR ALA ALA HIS GLY PRO          
SEQRES  34 B  484  TRP LEU GLN ILE LEU LEU THR GLU GLU PHE VAL GLU LYS          
SEQRES  35 B  484  MET LEU GLU ASP LEU GLU ASP LEU THR SER PRO GLU GLU          
SEQRES  36 B  484  PHE LYS LEU PRO LYS GLU TYR SER TRP PRO GLU LYS LYS          
SEQRES  37 B  484  LEU LYS VAL SER ILE LEU PRO ASP VAL VAL PHE ASP SER          
SEQRES  38 B  484  PRO LEU HIS                                                  
FORMUL   3  HOH   *12(H2 O)                                                     
HELIX    1   1 PHE A   26  PHE A   30  5                                   5    
HELIX    2   2 PRO A   31  TYR A   45  1                                  15    
HELIX    3   3 LYS A   59  GLY A   63  5                                   5    
HELIX    4   4 SER A   79  ASN A   83  5                                   5    
HELIX    5   5 THR A  135  SER A  151  1                                  17    
HELIX    6   6 CYS A  204  TRP A  214  1                                  11    
HELIX    7   7 ASN A  215  ARG A  224  1                                  10    
HELIX    8   8 THR A  243  ASP A  248  1                                   6    
HELIX    9   9 HIS A  250  ASP A  262  1                                  13    
HELIX   10  10 ASN A  374  ALA A  379  1                                   6    
HELIX   11  11 LEU A  380  GLY A  387  1                                   8    
HELIX   12  12 ARG A  388  GLY A  392  5                                   5    
HELIX   13  13 THR A  436  LEU A  447  1                                  12    
HELIX   14  14 PRO B   31  TYR B   45  1                                  15    
HELIX   15  15 LYS B   59  GLY B   63  5                                   5    
HELIX   16  16 SER B   79  ASN B   83  5                                   5    
HELIX   17  17 THR B  135  SER B  151  1                                  17    
HELIX   18  18 CYS B  204  TRP B  214  1                                  11    
HELIX   19  19 ASN B  215  ARG B  224  1                                  10    
HELIX   20  20 THR B  243  ASP B  248  1                                   6    
HELIX   21  21 HIS B  250  ASP B  262  1                                  13    
HELIX   22  22 ASN B  374  ALA B  379  1                                   6    
HELIX   23  23 LEU B  380  GLY B  387  1                                   8    
HELIX   24  24 ARG B  388  GLY B  392  5                                   5    
HELIX   25  25 THR B  436  LEU B  447  1                                  12    
HELIX   26  26 PRO B  475  PHE B  479  5                                   5    
SHEET    1   A 7 LEU A  52  THR A  55  0                                        
SHEET    2   A 7 TYR A  70  ASN A  76 -1  O  VAL A  71   N  VAL A  54           
SHEET    3   A 7 HIS A  87  PHE A  93 -1  O  ILE A  91   N  SER A  72           
SHEET    4   A 7 PRO A 113  LYS A 125 -1  O  LEU A 124   N  TRP A  88           
SHEET    5   A 7 GLY A 193  VAL A 203  1  O  ILE A 200   N  THR A 121           
SHEET    6   A 7 HIS A 176  GLU A 181 -1  N  THR A 180   O  GLN A 199           
SHEET    7   A 7 HIS A 160  VAL A 161 -1  N  VAL A 161   O  MET A 177           
SHEET    1   B 6 LEU A  52  THR A  55  0                                        
SHEET    2   B 6 TYR A  70  ASN A  76 -1  O  VAL A  71   N  VAL A  54           
SHEET    3   B 6 HIS A  87  PHE A  93 -1  O  ILE A  91   N  SER A  72           
SHEET    4   B 6 PRO A 113  LYS A 125 -1  O  LEU A 124   N  TRP A  88           
SHEET    5   B 6 GLY A 193  VAL A 203  1  O  ILE A 200   N  THR A 121           
SHEET    6   B 6 VAL A 188  THR A 190 -1  N  THR A 190   O  GLY A 193           
SHEET    1   C 6 GLY A 268  ALA A 271  0                                        
SHEET    2   C 6 PHE A 395  SER A 399  1  O  LYS A 398   N  ALA A 271           
SHEET    3   C 6 ALA A 405  VAL A 409 -1  O  ILE A 406   N  TYR A 397           
SHEET    4   C 6 TRP A 430  LEU A 434  1  O  LEU A 431   N  THR A 407           
SHEET    5   C 6 TYR A 424  HIS A 427 -1  N  ALA A 425   O  GLN A 432           
SHEET    6   C 6 ARG A 364  GLN A 365 -1  N  ARG A 364   O  ALA A 426           
SHEET    1   D 4 CYS A 273  ASP A 277  0                                        
SHEET    2   D 4 VAL A 369  PHE A 373 -1  O  LYS A 372   N  ALA A 274           
SHEET    3   D 4 LEU A 469  ILE A 473  1  O  LYS A 470   N  LEU A 371           
SHEET    4   D 4 LYS A 460  TRP A 464 -1  N  LYS A 460   O  ILE A 473           
SHEET    1   E 7 LEU B  52  THR B  55  0                                        
SHEET    2   E 7 TYR B  70  ASN B  76 -1  O  MET B  73   N  LEU B  52           
SHEET    3   E 7 HIS B  87  PHE B  93 -1  O  HIS B  89   N  TYR B  74           
SHEET    4   E 7 PRO B 113  LYS B 125 -1  O  LEU B 124   N  TRP B  88           
SHEET    5   E 7 GLY B 193  VAL B 203  1  O  ILE B 200   N  THR B 121           
SHEET    6   E 7 HIS B 176  GLU B 181 -1  N  THR B 180   O  GLN B 199           
SHEET    7   E 7 HIS B 160  VAL B 161 -1  N  VAL B 161   O  MET B 177           
SHEET    1   F 6 LEU B  52  THR B  55  0                                        
SHEET    2   F 6 TYR B  70  ASN B  76 -1  O  MET B  73   N  LEU B  52           
SHEET    3   F 6 HIS B  87  PHE B  93 -1  O  HIS B  89   N  TYR B  74           
SHEET    4   F 6 PRO B 113  LYS B 125 -1  O  LEU B 124   N  TRP B  88           
SHEET    5   F 6 GLY B 193  VAL B 203  1  O  ILE B 200   N  THR B 121           
SHEET    6   F 6 VAL B 188  THR B 190 -1  N  THR B 190   O  GLY B 193           
SHEET    1   G 6 GLY B 268  ALA B 271  0                                        
SHEET    2   G 6 PHE B 395  SER B 399  1  O  LYS B 398   N  VAL B 269           
SHEET    3   G 6 ALA B 405  VAL B 409 -1  O  ILE B 406   N  TYR B 397           
SHEET    4   G 6 TRP B 430  LEU B 434  1  O  LEU B 431   N  THR B 407           
SHEET    5   G 6 TYR B 424  HIS B 427 -1  N  ALA B 425   O  GLN B 432           
SHEET    6   G 6 THR B 363  GLN B 365 -1  N  ARG B 364   O  ALA B 426           
SHEET    1   H 4 CYS B 273  ASP B 277  0                                        
SHEET    2   H 4 VAL B 369  PHE B 373 -1  O  LYS B 372   N  ALA B 274           
SHEET    3   H 4 LEU B 469  ILE B 473  1  O  LYS B 470   N  LEU B 371           
SHEET    4   H 4 LYS B 460  TRP B 464 -1  N  TRP B 464   O  LEU B 469           
CISPEP   1 ALA A  229    GLY A  230          0        -3.45                     
CISPEP   2 ASP A  449    LEU A  450          0        -9.47                     
CISPEP   3 GLU A  455    PHE A  456          0        -1.15                     
CISPEP   4 LEU A  458    PRO A  459          0         5.26                     
CISPEP   5 ALA B  229    GLY B  230          0         1.74                     
CISPEP   6 ASP B  449    LEU B  450          0        -5.31                     
CISPEP   7 LEU B  458    PRO B  459          0         6.16                     
CRYST1   73.634  122.329  118.751  90.00  90.41  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013581  0.000000  0.000098        0.00000                         
SCALE2      0.000000  0.008175  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008421        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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