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Database: PDB
Entry: 4KM8
LinkDB: 4KM8
Original site: 4KM8 
HEADER    PROTEIN BINDING                         08-MAY-13   4KM8              
TITLE     CRYSTAL STRUCTURE OF SUFUD60                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPPRESSOR OF FUSED HOMOLOG;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-285, 346-484;                               
COMPND   5 SYNONYM: SUFUH;                                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SUFU, UNQ650/PRO1280;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    PROTEIN BINDING                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHANG,X.QI,Z.ZHANG,G.WU                                             
REVDAT   5   15-NOV-17 4KM8    1       REMARK                                   
REVDAT   4   23-AUG-17 4KM8    1       SOURCE REMARK                            
REVDAT   3   12-FEB-14 4KM8    1       JRNL                                     
REVDAT   2   27-NOV-13 4KM8    1       REMARK                                   
REVDAT   1   20-NOV-13 4KM8    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.    2.26 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) : 2.26                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 24721                          
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) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1316                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.26                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.32                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1734                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.77                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2500                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 88                           
REMARK   3   BIN FREE R VALUE                    : 0.3210                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3044                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 127                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.79000                                              
REMARK   3    B22 (A**2) : 0.84000                                              
REMARK   3    B33 (A**2) : -2.63000                                             
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): 0.252         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.214         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.160         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.159        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3132 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4265 ; 1.337 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   382 ; 5.997 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   146 ;35.005 ;23.904       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   485 ;16.932 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;14.310 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   458 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2432 ; 0.007 ; 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):  1923 ; 0.746 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3105 ; 1.366 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1209 ; 1.809 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1160 ; 2.842 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -7        A   481                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.6539 -17.5257  -4.1872              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0687 T22:   0.0441                                     
REMARK   3      T33:   0.0165 T12:   0.0414                                     
REMARK   3      T13:   0.0158 T23:   0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1907 L22:   0.0325                                     
REMARK   3      L33:   0.2950 L12:   0.0379                                     
REMARK   3      L13:   0.0006 L23:  -0.0359                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0180 S12:  -0.0022 S13:  -0.0326                       
REMARK   3      S21:   0.0022 S22:  -0.0165 S23:  -0.0130                       
REMARK   3      S31:   0.1195 S32:   0.1028 S33:   0.0345                       
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 :   A   501        A   627                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.9117 -14.7742  -1.5234              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0619 T22:   0.0415                                     
REMARK   3      T33:   0.0219 T12:   0.0347                                     
REMARK   3      T13:   0.0122 T23:  -0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2198 L22:   0.1098                                     
REMARK   3      L33:   0.2740 L12:   0.0994                                     
REMARK   3      L13:   0.0488 L23:  -0.0639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0003 S12:  -0.0088 S13:  -0.0273                       
REMARK   3      S21:  -0.0002 S22:  -0.0399 S23:  -0.0156                       
REMARK   3      S31:   0.0781 S32:   0.0631 S33:   0.0403                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4KM8 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_1000079514.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUN-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   : 26211                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
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     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.13600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51700                            
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: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 3350, 0.15M AMMONIUM TARTRATE,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K                     
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       59.30550            
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       59.30550            
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       38.13800            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       61.22600            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       38.13800            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       61.22600            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       59.30550            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       38.13800            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       61.22600            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       59.30550            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       38.13800            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       61.22600            
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 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     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     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     GLU A   359                                                      
REMARK 465     LEU A   360                                                      
REMARK 465     ILE A   361                                                      
REMARK 465     THR A   451                                                      
REMARK 465     SER A   452                                                      
REMARK 465     PRO A   453                                                      
REMARK 465     GLU A   454                                                      
REMARK 465     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     SER A 279    OG                                                  
REMARK 470     ARG A 362    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 368    OG                                                  
REMARK 470     LYS A 457    CG   CD   CE   NZ                                   
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    LEU A 383   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    ARG A 388   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 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    SER A  79       81.01   -159.06                                   
REMARK 500    ASN A  83       30.14     71.79                                   
REMARK 500    VAL A 104      -43.97   -136.18                                   
REMARK 500    SER A 170     -151.03    -86.61                                   
REMARK 500    SER A 172      152.62    -44.95                                   
REMARK 500    TRP A 214     -105.01   -107.37                                   
REMARK 500    ARG A 388      -68.34   -121.52                                   
REMARK 500    ARG A 393     -163.66   -112.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    VAL A  58        -10.51                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4KM9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KMA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KMD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KMH   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 UNP RESIDUES 286-345 ARE DELETION.                                   
DBREF  4KM8 A    1   285  UNP    Q9UMX1   SUFU_HUMAN       1    285             
DBREF  4KM8 A  346   484  UNP    Q9UMX1   SUFU_HUMAN     346    484             
SEQADV 4KM8 MET A  -19  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 GLY A  -18  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 SER A  -17  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 SER A  -16  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 HIS A  -15  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 HIS A  -14  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 HIS A  -13  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 HIS A  -12  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 HIS A  -11  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 HIS A  -10  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 SER A   -9  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 SER A   -8  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 GLY A   -7  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 LEU A   -6  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 VAL A   -5  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 PRO A   -4  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 ARG A   -3  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 GLY A   -2  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 SER A   -1  UNP  Q9UMX1              EXPRESSION TAG                 
SEQADV 4KM8 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  MLY 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                                                      
MODRES 4KM8 MLY A   59  LYS  N-DIMETHYL-LYSINE                                  
HET    MLY  A  59      11                                                       
HETNAM     MLY N-DIMETHYL-LYSINE                                                
FORMUL   1  MLY    C8 H18 N2 O2                                                 
FORMUL   2  HOH   *127(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 MLY 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 HIS A  250  GLY A  263  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  LEU A  447  1                                  12    
HELIX   14  14 ASP A  476  SER A  481  1                                   6    
SHEET    1   A 7 LEU A  52  THR A  55  0                                        
SHEET    2   A 7 TYR A  70  ASN A  76 -1  O  MET A  73   N  LEU A  52           
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 LEU A  52  THR A  55  0                                        
SHEET    2   B 6 TYR A  70  ASN A  76 -1  O  MET A  73   N  LEU A  52           
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  VAL A 188   O  VAL A 195           
SHEET    1   C 6 GLY A 268  ALA A 271  0                                        
SHEET    2   C 6 HIS A 394  SER A 399  1  O  LYS A 398   N  ALA A 271           
SHEET    3   C 6 ALA A 405  VAL A 409 -1  O  ILE A 406   N  TYR A 397           
SHEET    4   C 6 TRP A 430  LEU A 434  1  O  LEU A 431   N  THR A 407           
SHEET    5   C 6 TYR A 424  HIS A 427 -1  N  ALA A 425   O  GLN A 432           
SHEET    6   C 6 ARG A 364  GLN A 365 -1  N  ARG A 364   O  ALA A 426           
SHEET    1   D 4 CYS A 273  ASP A 277  0                                        
SHEET    2   D 4 VAL A 369  PHE A 373 -1  O  LYS A 372   N  ALA A 274           
SHEET    3   D 4 LEU A 469  ILE A 473  1  O  LYS A 470   N  LEU A 371           
SHEET    4   D 4 LYS A 460  TRP A 464 -1  N  LYS A 460   O  ILE A 473           
LINK         C   VAL A  58                 N   MLY A  59     1555   1555  1.34  
LINK         C   MLY A  59                 N   TYR A  60     1555   1555  1.32  
CISPEP   1 ALA A  229    GLY A  230          0        -3.21                     
CISPEP   2 GLU A  448    ASP A  449          0         2.81                     
CISPEP   3 ASP A  449    LEU A  450          0         5.81                     
CISPEP   4 LEU A  458    PRO A  459          0         0.80                     
CRYST1   76.276  122.452  118.611  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      0.013110  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008166  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008431        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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