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Database: PDB
Entry: 4KMD
LinkDB: 4KMD
Original site: 4KMD 
HEADER    PROTEIN BINDING/TRANSCRIPTION           08-MAY-13   4KMD              
TITLE     CRYSTAL STRUCTURE OF SUFUD60-GLI1P                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUFU;                                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-285, 346-484;                               
COMPND   5 SYNONYM: SUFUH;                                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: ZINC FINGER PROTEIN GLI1;                                  
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: UNP RESIDUES 112-128;                                      
COMPND  11 SYNONYM: GLIOMA-ASSOCIATED ONCOGENE, ONCOGENE GLI;                   
COMPND  12 ENGINEERED: 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;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 OTHER_DETAILS: CHEMICAL SYNTHESIS                                    
KEYWDS    PROTEIN PEPTIDE COMPLEX, PROTEIN BINDING-TRANSCRIPTION COMPLEX        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHANG,X.QI,Z.ZHANG,G.WU                                             
REVDAT   5   15-NOV-17 4KMD    1       REMARK                                   
REVDAT   4   23-AUG-17 4KMD    1       SOURCE REMARK                            
REVDAT   3   12-FEB-14 4KMD    1       JRNL                                     
REVDAT   2   27-NOV-13 4KMD    1       REMARK                                   
REVDAT   1   20-NOV-13 4KMD    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.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 47718                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2416                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3351                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2150                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 182                          
REMARK   3   BIN FREE R VALUE                    : 0.2510                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2987                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 223                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.95000                                              
REMARK   3    B22 (A**2) : 0.74000                                              
REMARK   3    B33 (A**2) : -1.69000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.107         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.063         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.130         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3114 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4227 ; 1.074 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   377 ; 5.496 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   145 ;35.076 ;24.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   495 ;14.549 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;18.655 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   451 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2384 ; 0.005 ; 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):  1879 ; 0.510 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3039 ; 0.978 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1235 ; 1.343 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1186 ; 2.199 ; 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  : 4                                          
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    28        A   480                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.3548  15.3384  15.9858              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0124 T22:   0.0458                                     
REMARK   3      T33:   0.0542 T12:   0.0037                                     
REMARK   3      T13:   0.0063 T23:   0.0040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4223 L22:   0.5231                                     
REMARK   3      L33:   1.4790 L12:   0.1738                                     
REMARK   3      L13:  -0.1521 L23:  -0.0256                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0376 S12:   0.0424 S13:   0.0180                       
REMARK   3      S21:   0.0094 S22:   0.0245 S23:   0.0060                       
REMARK   3      S31:  -0.0713 S32:   0.0936 S33:  -0.0621                       
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   119        B   128                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.2349  14.9505  12.4725              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0501 T22:   0.0517                                     
REMARK   3      T33:   0.0422 T12:  -0.0234                                     
REMARK   3      T13:   0.0173 T23:   0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.2211 L22:   5.5891                                     
REMARK   3      L33:   6.1879 L12:  -1.8123                                     
REMARK   3      L13:  -0.9272 L23:  -1.7631                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0443 S12:  -0.0643 S13:  -0.4471                       
REMARK   3      S21:  -0.0954 S22:   0.1239 S23:   0.2551                       
REMARK   3      S31:   0.2092 S32:  -0.0866 S33:  -0.0797                       
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   602        A   817                          
REMARK   3    RESIDUE RANGE :   B   201        B   206                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.6903  14.6143  18.0328              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0097 T22:   0.0273                                     
REMARK   3      T33:   0.0174 T12:   0.0000                                     
REMARK   3      T13:   0.0024 T23:  -0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5196 L22:   0.5268                                     
REMARK   3      L33:   1.6476 L12:   0.3315                                     
REMARK   3      L13:  -0.3944 L23:  -0.1427                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0105 S12:   0.0486 S13:  -0.0001                       
REMARK   3      S21:   0.0321 S22:   0.0148 S23:   0.0018                       
REMARK   3      S31:  -0.0728 S32:   0.0689 S33:  -0.0253                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   501        A   506                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.4316   2.9711  24.5234              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4725 T22:   0.1904                                     
REMARK   3      T33:   0.4338 T12:   0.0822                                     
REMARK   3      T13:   0.2770 T23:  -0.0469                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8401 L22:   7.3843                                     
REMARK   3      L33:   4.3024 L12:  -0.2693                                     
REMARK   3      L13:   2.2821 L23:  -4.4597                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1260 S12:   0.1663 S13:  -0.0570                       
REMARK   3      S21:  -1.1039 S22:  -0.3236 S23:  -0.6501                       
REMARK   3      S31:   0.5735 S32:   0.3615 S33:   0.4496                       
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 4KMD 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_1000079518.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-JAN-13                          
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   : 47766                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
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   (%): 42.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M MAGNESIUM CHLORIDE,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       74.87800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.87800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       35.41500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       41.05900            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       35.41500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       41.05900            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       74.87800            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       35.41500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       41.05900            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       74.87800            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       35.41500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       41.05900            
REMARK 290   SMTRY3   8  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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLU A     3                                                      
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     PRO A    20                                                      
REMARK 465     THR A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     PRO A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     PHE A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     SER A   279                                                      
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     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     THR A   451                                                      
REMARK 465     SER A   452                                                      
REMARK 465     PRO A   453                                                      
REMARK 465     GLU A   454                                                      
REMARK 465     GLU A   455                                                      
REMARK 465     PHE A   456                                                      
REMARK 465     SER A   481                                                      
REMARK 465     PRO A   482                                                      
REMARK 465     LEU A   483                                                      
REMARK 465     HIS A   484                                                      
REMARK 465     SER B   112                                                      
REMARK 465     ARG B   113                                                      
REMARK 465     CYS B   114                                                      
REMARK 465     THR B   115                                                      
REMARK 465     SER B   116                                                      
REMARK 465     PRO B   117                                                      
REMARK 465     GLY B   118                                                      
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     GLU A 359    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SG   CYS A   156     S1   DTT A   507              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  79       80.73   -150.45                                   
REMARK 500    VAL A 104      -41.52   -142.40                                   
REMARK 500    GLU A 152       17.41     54.65                                   
REMARK 500    TRP A 163      -42.35   -134.41                                   
REMARK 500    SER A 170     -150.11    -88.32                                   
REMARK 500    TRP A 214     -106.64   -111.54                                   
REMARK 500    ARG A 388      -67.72   -120.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A 507                 
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: 4KMH   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 UNP RESIDUES 286-345 ARE DELETION.                                   
DBREF  4KMD A    1   285  UNP    Q9UMX1   SUFU_HUMAN       1    285             
DBREF  4KMD A  346   484  UNP    Q9UMX1   SUFU_HUMAN     346    484             
DBREF  4KMD B  112   128  UNP    P08151   GLI1_HUMAN     112    128             
SEQADV 4KMD MET A  -19  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD GLY A  -18  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD SER A  -17  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD SER A  -16  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD HIS A  -15  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD HIS A  -14  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD HIS A  -13  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD HIS A  -12  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD HIS A  -11  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD HIS A  -10  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD SER A   -9  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD SER A   -8  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD GLY A   -7  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD LEU A   -6  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD VAL A   -5  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD PRO A   -4  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD ARG A   -3  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD GLY A   -2  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD SER A   -1  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KMD HIS A    0  UNP  Q9UMX1              EXPRESSION TAG                 
SEQRES   1 A  444  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  444  LEU VAL PRO ARG GLY SER HIS MET ALA GLU LEU ARG PRO          
SEQRES   3 A  444  SER GLY ALA PRO GLY PRO THR ALA PRO PRO ALA PRO GLY          
SEQRES   4 A  444  PRO THR ALA PRO PRO ALA PHE ALA SER LEU PHE PRO PRO          
SEQRES   5 A  444  GLY LEU HIS ALA ILE TYR GLY GLU CYS ARG ARG LEU TYR          
SEQRES   6 A  444  PRO ASP GLN PRO ASN PRO LEU GLN VAL THR ALA ILE VAL          
SEQRES   7 A  444  LYS TYR TRP LEU GLY GLY PRO ASP PRO LEU ASP TYR VAL          
SEQRES   8 A  444  SER MET TYR ARG ASN VAL GLY SER PRO SER ALA ASN ILE          
SEQRES   9 A  444  PRO GLU HIS TRP HIS TYR ILE SER PHE GLY LEU SER ASP          
SEQRES  10 A  444  LEU TYR GLY ASP ASN ARG VAL HIS GLU PHE THR GLY THR          
SEQRES  11 A  444  ASP GLY PRO SER GLY PHE GLY PHE GLU LEU THR PHE ARG          
SEQRES  12 A  444  LEU LYS ARG GLU THR GLY GLU SER ALA PRO PRO THR TRP          
SEQRES  13 A  444  PRO ALA GLU LEU MET GLN GLY LEU ALA ARG TYR VAL PHE          
SEQRES  14 A  444  GLN SER GLU ASN THR PHE CYS SER GLY ASP HIS VAL SER          
SEQRES  15 A  444  TRP HIS SER PRO LEU ASP ASN SER GLU SER ARG ILE GLN          
SEQRES  16 A  444  HIS MET LEU LEU THR GLU ASP PRO GLN MET GLN PRO VAL          
SEQRES  17 A  444  GLN THR PRO PHE GLY VAL VAL THR PHE LEU GLN ILE VAL          
SEQRES  18 A  444  GLY VAL CYS THR GLU GLU LEU HIS SER ALA GLN GLN TRP          
SEQRES  19 A  444  ASN GLY GLN GLY ILE LEU GLU LEU LEU ARG THR VAL PRO          
SEQRES  20 A  444  ILE ALA GLY GLY PRO TRP LEU ILE THR ASP MET ARG ARG          
SEQRES  21 A  444  GLY GLU THR ILE PHE GLU ILE ASP PRO HIS LEU GLN GLU          
SEQRES  22 A  444  ARG VAL ASP LYS GLY ILE GLU THR ASP GLY SER ASN LEU          
SEQRES  23 A  444  SER GLY VAL SER ALA LYS CYS ALA TRP ASP ASP LEU SER          
SEQRES  24 A  444  ARG PRO PRO GLU ASP ASP SER LEU GLU SER ASP SER SER          
SEQRES  25 A  444  THR ALA ILE ILE PRO HIS GLU LEU ILE ARG THR ARG GLN          
SEQRES  26 A  444  LEU GLU SER VAL HIS LEU LYS PHE ASN GLN GLU SER GLY          
SEQRES  27 A  444  ALA LEU ILE PRO LEU CYS LEU ARG GLY ARG LEU LEU HIS          
SEQRES  28 A  444  GLY ARG HIS PHE THR TYR LYS SER ILE THR GLY ASP MET          
SEQRES  29 A  444  ALA ILE THR PHE VAL SER THR GLY VAL GLU GLY ALA PHE          
SEQRES  30 A  444  ALA THR GLU GLU HIS PRO TYR ALA ALA HIS GLY PRO TRP          
SEQRES  31 A  444  LEU GLN ILE LEU LEU THR GLU GLU PHE VAL GLU LYS MET          
SEQRES  32 A  444  LEU GLU ASP LEU GLU ASP LEU THR SER PRO GLU GLU PHE          
SEQRES  33 A  444  LYS LEU PRO LYS GLU TYR SER TRP PRO GLU LYS LYS LEU          
SEQRES  34 A  444  LYS VAL SER ILE LEU PRO ASP VAL VAL PHE ASP SER PRO          
SEQRES  35 A  444  LEU HIS                                                      
SEQRES   1 B   17  SER ARG CYS THR SER PRO GLY GLY SER TYR GLY HIS LEU          
SEQRES   2 B   17  SER ILE GLY THR                                              
HET    GOL  A 501       6                                                       
HET    GOL  A 502       6                                                       
HET    GOL  A 503       6                                                       
HET    GOL  A 504       6                                                       
HET    GOL  A 505       6                                                       
HET    GOL  A 506       6                                                       
HET    DTT  A 507       8                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE                                   
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     DTT 1,4-DITHIOTHREITOL                                               
FORMUL   3  GOL    6(C3 H8 O3)                                                  
FORMUL   9  DTT    C4 H10 O2 S2                                                 
FORMUL  10  HOH   *223(H2 O)                                                    
HELIX    1   1 PRO A   31  TYR A   45  1                                  15    
HELIX    2   2 LYS A   59  GLY A   63  5                                   5    
HELIX    3   3 SER A   79  ASN A   83  5                                   5    
HELIX    4   4 THR A  135  GLU A  152  1                                  18    
HELIX    5   5 CYS A  204  TRP A  214  1                                  11    
HELIX    6   6 ASN A  215  THR A  225  1                                  11    
HELIX    7   7 VAL A  226  GLY A  230  5                                   5    
HELIX    8   8 THR A  243  ASP A  248  1                                   6    
HELIX    9   9 PRO A  249  GLY A  263  1                                  15    
HELIX   10  10 ASN A  374  ALA A  379  1                                   6    
HELIX   11  11 LEU A  380  ARG A  388  1                                   9    
HELIX   12  12 LEU A  389  GLY A  392  5                                   4    
HELIX   13  13 THR A  436  LEU A  447  1                                  12    
HELIX   14  14 PRO A  465  LYS A  467  5                                   3    
HELIX   15  15 PRO A  475  ASP A  480  5                                   6    
SHEET    1   A 6 LEU A  52  THR A  55  0                                        
SHEET    2   A 6 TYR A  70  ASN A  76 -1  O  MET A  73   N  LEU A  52           
SHEET    3   A 6 HIS A  87  PHE A  93 -1  O  HIS A  89   N  TYR A  74           
SHEET    4   A 6 PRO A 113  LYS A 125 -1  O  LEU A 124   N  TRP A  88           
SHEET    5   A 6 GLY A 193  VAL A 203  1  O  ILE A 200   N  THR A 121           
SHEET    6   A 6 VAL A 188  THR A 190 -1  N  VAL A 188   O  VAL A 195           
SHEET    1   B14 LEU A  52  THR A  55  0                                        
SHEET    2   B14 TYR A  70  ASN A  76 -1  O  MET A  73   N  LEU A  52           
SHEET    3   B14 HIS A  87  PHE A  93 -1  O  HIS A  89   N  TYR A  74           
SHEET    4   B14 PRO A 113  LYS A 125 -1  O  LEU A 124   N  TRP A  88           
SHEET    5   B14 GLY A 193  VAL A 203  1  O  ILE A 200   N  THR A 121           
SHEET    6   B14 HIS A 176  GLU A 181 -1  N  THR A 180   O  GLN A 199           
SHEET    7   B14 HIS A 160  VAL A 161 -1  N  VAL A 161   O  MET A 177           
SHEET    8   B14 SER B 120  HIS B 123  1  O  HIS B 123   N  HIS A 160           
SHEET    9   B14 LEU A 266  ALA A 271  1  N  SER A 270   O  GLY B 122           
SHEET   10   B14 PHE A 395  SER A 399  1  O  LYS A 398   N  VAL A 269           
SHEET   11   B14 ALA A 405  VAL A 409 -1  O  PHE A 408   N  PHE A 395           
SHEET   12   B14 TRP A 430  LEU A 434  1  O  LEU A 431   N  THR A 407           
SHEET   13   B14 TYR A 424  HIS A 427 -1  N  ALA A 425   O  GLN A 432           
SHEET   14   B14 ARG A 364  GLN A 365 -1  N  ARG A 364   O  ALA A 426           
SHEET    1   C 4 CYS A 273  ASP A 276  0                                        
SHEET    2   C 4 VAL A 369  PHE A 373 -1  O  LYS A 372   N  ALA A 274           
SHEET    3   C 4 LEU A 469  ILE A 473  1  O  LYS A 470   N  LEU A 371           
SHEET    4   C 4 LYS A 460  TRP A 464 -1  N  TYR A 462   O  VAL A 471           
CISPEP   1 LEU A  458    PRO A  459          0         2.33                     
SITE     1 AC1  3 GLU A 367  PRO A 423  HOH A 795                               
SITE     1 AC2  8 PHE A 116  GLY A 117  PHE A 118  THR A 154                    
SITE     2 AC2  8 PHE A 155  THR A 196  DTT A 507  HOH A 660                    
SITE     1 AC3  6 HIS A 105  PHE A 116  GLU A 367  HOH A 736                    
SITE     2 AC3  6 HOH A 750  HOH A 768                                          
SITE     1 AC4  8 LEU A  34  TYR A  38  GLN A  53  ILE A  57                    
SITE     2 AC4  8 LYS A  59  TYR A  70  HOH A 704  HOH A 814                    
SITE     1 AC5  6 TYR A  38  ARG A  42  GLN A  48  PRO A  49                    
SITE     2 AC5  6 TYR A  74  HOH A 790                                          
SITE     1 AC6  4 LEU A  29  PHE A  30  LEU A  62  PRO A 227                    
SITE     1 AC7  3 CYS A 156  GOL A 502  HOH A 649                               
CRYST1   70.830   82.118  149.756  90.00  90.00  90.00 C 2 2 21      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      0.014118  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012178  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006678        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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