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Database: PDB
Entry: 4KM9
LinkDB: 4KM9
Original site: 4KM9 
HEADER    PROTEIN BINDING                         08-MAY-13   4KM9              
TITLE     CRYSTAL STRUCTURE OF HUMAN SUPPRESSOR OF FUSED                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPPRESSOR OF FUSED HOMOLOG;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SUFUH;                                                      
COMPND   5 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: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL: HIGH FIVE;                                   
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_VECTOR: PFASTBAC HTB                               
KEYWDS    SUPPRESSOR OF FUSED, PROTEIN BINDING                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHANG,X.QI,Z.ZHANG,G.WU                                             
REVDAT   4   15-NOV-17 4KM9    1       REMARK                                   
REVDAT   3   12-FEB-14 4KM9    1       JRNL                                     
REVDAT   2   27-NOV-13 4KM9    1       REMARK                                   
REVDAT   1   20-NOV-13 4KM9    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.    3.19 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) : 3.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 8939                           
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) : 0.246                           
REMARK   3   R VALUE            (WORKING SET) : 0.243                           
REMARK   3   FREE R VALUE                     : 0.305                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 426                             
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) : 3.19                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 571                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.39                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 29                           
REMARK   3   BIN FREE R VALUE                    : 0.3130                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2981                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 7                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 109.4                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.13000                                              
REMARK   3    B22 (A**2) : 3.58000                                              
REMARK   3    B33 (A**2) : -3.71000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.589         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.471         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 59.121        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.918                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.849                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3063 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4173 ; 0.970 ; 1.948       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   379 ; 4.920 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   138 ;34.548 ;23.551       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   469 ;15.682 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;19.054 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   453 ; 0.064 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2372 ; 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):  1902 ; 1.008 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3057 ; 1.494 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1161 ; 0.367 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1116 ; 0.669 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
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    21        A   481                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.4460 -15.7760  -5.6310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2784 T22:   0.0306                                     
REMARK   3      T33:   0.0334 T12:   0.0403                                     
REMARK   3      T13:   0.0684 T23:  -0.0056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8689 L22:   0.8016                                     
REMARK   3      L33:   4.8377 L12:  -0.1928                                     
REMARK   3      L13:  -0.7737 L23:  -0.0039                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1376 S12:   0.0399 S13:  -0.0416                       
REMARK   3      S21:   0.1023 S22:  -0.0567 S23:   0.0054                       
REMARK   3      S31:   0.5009 S32:   0.2534 S33:   0.1943                       
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 4KM9 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_1000079515.                                   
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   : 8956                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 63.040                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 8.400                              
REMARK 200  R MERGE                    (I) : 0.12700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49200                            
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   (%): 49.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M POTASSIUM CHLORIDE,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 281K                     
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       58.82650            
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       58.82650            
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       36.93750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       60.47000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       36.93750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       60.47000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       58.82650            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       36.93750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       60.47000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       58.82650            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       36.93750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       60.47000            
REMARK 290   SMTRY3   8  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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 501  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -4                                                      
REMARK 465     ALA A    -3                                                      
REMARK 465     MET A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     GLN 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     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     GLU A   306                                                      
REMARK 465     GLN A   307                                                      
REMARK 465     ILE A   308                                                      
REMARK 465     ARG A   309                                                      
REMARK 465     GLU A   310                                                      
REMARK 465     THR A   311                                                      
REMARK 465     LEU A   312                                                      
REMARK 465     ARG A   313                                                      
REMARK 465     ARG A   314                                                      
REMARK 465     GLY A   315                                                      
REMARK 465     LEU A   316                                                      
REMARK 465     GLU A   317                                                      
REMARK 465     ILE A   318                                                      
REMARK 465     ASN A   319                                                      
REMARK 465     SER A   320                                                      
REMARK 465     LYS A   321                                                      
REMARK 465     PRO A   322                                                      
REMARK 465     VAL A   323                                                      
REMARK 465     LEU A   324                                                      
REMARK 465     PRO A   325                                                      
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     PRO A   453                                                      
REMARK 465     GLU A   454                                                      
REMARK 465     GLU A   455                                                      
REMARK 465     PHE A   456                                                      
REMARK 465     PRO A   482                                                      
REMARK 465     LEU A   483                                                      
REMARK 465     HIS A   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     THR A  21    OG1  CG2                                            
REMARK 470     PRO A  23    CG   CD                                             
REMARK 470     PRO A  24    CG   CD                                             
REMARK 470     GLU A  40    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  50    CG   OD1  ND2                                       
REMARK 470     GLU A 127    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 140    CG   CD1  CD2                                       
REMARK 470     GLU A 171    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 253    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 356    CG1  CG2  CD1                                       
REMARK 470     PRO A 357    CG   CD                                             
REMARK 470     GLU A 359    CG   CD   OE1  OE2                                  
REMARK 470     SER A 368    OG                                                  
REMARK 470     THR A 401    OG1  CG2                                            
REMARK 470     GLU A 420    CG   CD   OE1  OE2                                  
REMARK 470     SER A 452    OG                                                  
REMARK 470     LYS A 457    CG   CD   CE   NZ                                   
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   CD1  LEU A   431     CD1  ILE A   433              1.93            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 357   N   -  CA  -  CB  ANGL. DEV. =   8.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A 104      -28.72   -140.92                                   
REMARK 500    GLU A 152        9.31     56.69                                   
REMARK 500    ASN A 169       -3.09     77.23                                   
REMARK 500    PRO A 191        1.97    -68.38                                   
REMARK 500    ALA A 229      -71.69    -58.59                                   
REMARK 500    LYS A 272      106.28    -56.94                                   
REMARK 500    VAL A 477       -8.23    -59.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4KM8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KMA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KMD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KMH   RELATED DB: PDB                                   
DBREF  4KM9 A    1   484  UNP    Q9UMX1   SUFU_HUMAN       1    484             
SEQADV 4KM9 GLY A   -4  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM9 ALA A   -3  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM9 MET A   -2  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM9 GLY A   -1  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM9 GLN A    0  UNP  Q9UMX1              EXPRESSION TAG                 
SEQRES   1 A  489  GLY ALA MET GLY GLN MET ALA GLU LEU ARG PRO SER GLY          
SEQRES   2 A  489  ALA PRO GLY PRO THR ALA PRO PRO ALA PRO GLY PRO THR          
SEQRES   3 A  489  ALA PRO PRO ALA PHE ALA SER LEU PHE PRO PRO GLY LEU          
SEQRES   4 A  489  HIS ALA ILE TYR GLY GLU CYS ARG ARG LEU TYR PRO ASP          
SEQRES   5 A  489  GLN PRO ASN PRO LEU GLN VAL THR ALA ILE VAL LYS TYR          
SEQRES   6 A  489  TRP LEU GLY GLY PRO ASP PRO LEU ASP TYR VAL SER MET          
SEQRES   7 A  489  TYR ARG ASN VAL GLY SER PRO SER ALA ASN ILE PRO GLU          
SEQRES   8 A  489  HIS TRP HIS TYR ILE SER PHE GLY LEU SER ASP LEU TYR          
SEQRES   9 A  489  GLY ASP ASN ARG VAL HIS GLU PHE THR GLY THR ASP GLY          
SEQRES  10 A  489  PRO SER GLY PHE GLY PHE GLU LEU THR PHE ARG LEU LYS          
SEQRES  11 A  489  ARG GLU THR GLY GLU SER ALA PRO PRO THR TRP PRO ALA          
SEQRES  12 A  489  GLU LEU MET GLN GLY LEU ALA ARG TYR VAL PHE GLN SER          
SEQRES  13 A  489  GLU ASN THR PHE CYS SER GLY ASP HIS VAL SER TRP HIS          
SEQRES  14 A  489  SER PRO LEU ASP ASN SER GLU SER ARG ILE GLN HIS MET          
SEQRES  15 A  489  LEU LEU THR GLU ASP PRO GLN MET GLN PRO VAL GLN THR          
SEQRES  16 A  489  PRO PHE GLY VAL VAL THR PHE LEU GLN ILE VAL GLY VAL          
SEQRES  17 A  489  CYS THR GLU GLU LEU HIS SER ALA GLN GLN TRP ASN GLY          
SEQRES  18 A  489  GLN GLY ILE LEU GLU LEU LEU ARG THR VAL PRO ILE ALA          
SEQRES  19 A  489  GLY GLY PRO TRP LEU ILE THR ASP MET ARG ARG GLY GLU          
SEQRES  20 A  489  THR ILE PHE GLU ILE ASP PRO HIS LEU GLN GLU ARG VAL          
SEQRES  21 A  489  ASP LYS GLY ILE GLU THR ASP GLY SER ASN LEU SER GLY          
SEQRES  22 A  489  VAL SER ALA LYS CYS ALA TRP ASP ASP LEU SER ARG PRO          
SEQRES  23 A  489  PRO GLU ASP ASP GLU ASP SER ARG SER ILE CYS ILE GLY          
SEQRES  24 A  489  THR GLN PRO ARG ARG LEU SER GLY LYS ASP THR GLU GLN          
SEQRES  25 A  489  ILE ARG GLU THR LEU ARG ARG GLY LEU GLU ILE ASN SER          
SEQRES  26 A  489  LYS PRO VAL LEU PRO PRO ILE ASN PRO GLN ARG GLN ASN          
SEQRES  27 A  489  GLY LEU ALA HIS ASP ARG ALA PRO SER ARG LYS ASP SER          
SEQRES  28 A  489  LEU GLU SER ASP SER SER THR ALA ILE ILE PRO HIS GLU          
SEQRES  29 A  489  LEU ILE ARG THR ARG GLN LEU GLU SER VAL HIS LEU LYS          
SEQRES  30 A  489  PHE ASN GLN GLU SER GLY ALA LEU ILE PRO LEU CYS LEU          
SEQRES  31 A  489  ARG GLY ARG LEU LEU HIS GLY ARG HIS PHE THR TYR LYS          
SEQRES  32 A  489  SER ILE THR GLY ASP MET ALA ILE THR PHE VAL SER THR          
SEQRES  33 A  489  GLY VAL GLU GLY ALA PHE ALA THR GLU GLU HIS PRO TYR          
SEQRES  34 A  489  ALA ALA HIS GLY PRO TRP LEU GLN ILE LEU LEU THR GLU          
SEQRES  35 A  489  GLU PHE VAL GLU LYS MET LEU GLU ASP LEU GLU ASP LEU          
SEQRES  36 A  489  THR SER PRO GLU GLU PHE LYS LEU PRO LYS GLU TYR SER          
SEQRES  37 A  489  TRP PRO GLU LYS LYS LEU LYS VAL SER ILE LEU PRO ASP          
SEQRES  38 A  489  VAL VAL PHE ASP SER PRO LEU HIS                              
FORMUL   2  HOH   *7(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  GLU A  152  1                                  18    
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 PRO A  249  ASP A  262  1                                  14    
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  ASP A  446  1                                  11    
HELIX   14  14 PRO A  475  PHE A  479  5                                   5    
SHEET    1   A 7 GLN A  53  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  HIS A  87   N  ASN A  76           
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 GLN A  53  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  HIS A  87   N  ASN A  76           
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  SER A 270  0                                        
SHEET    2   C 6 PHE A 395  LYS A 398  1  O  THR A 396   N  VAL A 269           
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  ILE A 433   N  VAL A 409           
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  LEU A 366 -1  N  LEU A 366   O  TYR A 424           
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  SER A 472   N  LEU A 371           
SHEET    4   D 4 LYS A 460  TRP A 464 -1  N  LYS A 460   O  ILE A 473           
CISPEP   1 ALA A  229    GLY A  230          0         0.42                     
CISPEP   2 ILE A  356    PRO A  357          0        -2.87                     
CISPEP   3 HIS A  358    GLU A  359          0         0.52                     
CISPEP   4 LEU A  458    PRO A  459          0         4.00                     
CRYST1   73.875  120.940  117.653  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      0.013536  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008269  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008500        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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