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Database: PDB
Entry: 1M1L
LinkDB: 1M1L
Original site: 1M1L 
HEADER    SIGNALING PROTEIN                       19-JUN-02   1M1L              
TITLE     HUMAN SUPPRESSOR OF FUSED (N-TERMINAL DOMAIN)                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPPRESSOR OF FUSED;                                       
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN (RESIDUES 27-262);                       
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PST-239                                   
KEYWDS    GENE REGULATION, HEDGEHOG SIGNALING, SIGNAL TRANSDUCTION,             
KEYWDS   2 FUSED, SIGNALING PROTEIN                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MERCHANT,F.F.VAJDOS,M.ULTSCH,H.R.MAUN,U.WENDT,J.CANNON,             
AUTHOR   2 R.A.LAZARUS,A.M.DE VOS,F.J.DE SAUVAGE                                
REVDAT   3   24-FEB-09 1M1L    1       VERSN                                    
REVDAT   2   29-MAR-05 1M1L    1       JRNL                                     
REVDAT   1   03-FEB-04 1M1L    0                                                
JRNL        AUTH   M.MERCHANT,F.F.VAJDOS,M.ULTSCH,H.R.MAUN,U.WENDT,             
JRNL        AUTH 2 J.CANNON,W.DESMARAIS,R.A.LAZARUS,A.M.DE VOS,                 
JRNL        AUTH 3 F.J.DE SAUVAGE                                               
JRNL        TITL   SUPPRESSOR OF FUSED REGULATES GLI ACTIVITY THROUGH           
JRNL        TITL 2 A DUAL BINDING MECHANISM                                     
JRNL        REF    MOL.CELL.BIOL.                V.  24  8627 2004              
JRNL        REFN                   ISSN 0270-7306                               
JRNL        PMID   15367681                                                     
JRNL        DOI    10.1128/MCB.24.19.8627-8641.2004                             
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.81                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 48273                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : THIN SHELLS                     
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7486                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 346                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1M1L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB016484.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48643                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.810                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: SAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M LICL, 0.1 M NACITRATE PH 5.0-        
REMARK 280  6.0, 10% W/V PEG 6000, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 279K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       86.51250            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       49.94802            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       96.94433            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       86.51250            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       49.94802            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       96.94433            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       86.51250            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       49.94802            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       96.94433            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       86.51250            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       49.94802            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       96.94433            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       86.51250            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       49.94802            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       96.94433            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       86.51250            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       49.94802            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       96.94433            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       99.89603            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      193.88867            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       99.89603            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      193.88867            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       99.89603            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      193.88867            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       99.89603            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      193.88867            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       99.89603            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      193.88867            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       99.89603            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      193.88867            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). AUTHOR STATES               
REMARK 300 THAT BIOLOGICAL UNIT IS UNKNOWN.                                     
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA C    27                                                      
REMARK 465     SER C    28                                                      
REMARK 465     ALA D    27                                                      
REMARK 465     SER D    28                                                      
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   OH   TYR A   147     OE1  GLN B   150              2.11            
REMARK 500   N    ALA B    27     O    HOH B   314              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU C 139   CB    GLU C 139   CG     -0.116                       
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    GLU A 253   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    PRO B  80   N   -  CA  -  C   ANGL. DEV. = -16.5 DEGREES          
REMARK 500    GLU C 139   CA  -  CB  -  CG  ANGL. DEV. = -16.5 DEGREES          
REMARK 500    GLU C 139   OE1 -  CD  -  OE2 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ARG D  42   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    GLU D 152   N   -  CA  -  C   ANGL. DEV. = -25.0 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  28       74.30    172.99                                   
REMARK 500    TRP A  61        2.30    -68.41                                   
REMARK 500    VAL A 104      -51.02   -132.67                                   
REMARK 500    ASP A 111      -70.49    -85.92                                   
REMARK 500    SER A 165      141.08   -171.77                                   
REMARK 500    SER A 170     -146.39   -102.63                                   
REMARK 500    SER A 172      151.68    -42.73                                   
REMARK 500    TRP A 214     -105.05   -104.67                                   
REMARK 500    PRO A 249       -8.23    -50.09                                   
REMARK 500    SER B  28       75.75   -159.99                                   
REMARK 500    TRP B  61        5.39    -66.83                                   
REMARK 500    SER B  81      -61.30    129.05                                   
REMARK 500    VAL B 104      -50.52   -132.36                                   
REMARK 500    ASP B 111      -70.90    -87.16                                   
REMARK 500    SER B 170     -148.00   -103.51                                   
REMARK 500    SER B 172      149.80    -39.79                                   
REMARK 500    TRP B 214     -104.50   -104.08                                   
REMARK 500    PRO B 249       -6.38    -46.93                                   
REMARK 500    PRO C  31      113.87    -37.75                                   
REMARK 500    VAL C 104      -49.16   -134.60                                   
REMARK 500    ASP C 111      -73.15    -86.30                                   
REMARK 500    SER C 170     -146.42   -100.64                                   
REMARK 500    SER C 172      148.86    -39.51                                   
REMARK 500    TRP C 214     -107.01   -102.62                                   
REMARK 500    PRO C 249       -7.41    -50.07                                   
REMARK 500    GLU C 260      -72.28    -53.42                                   
REMARK 500    PRO D  31      106.37    -38.18                                   
REMARK 500    VAL D 104      -48.22   -136.00                                   
REMARK 500    SER D 151      156.48     70.76                                   
REMARK 500    GLU D 152      -14.77    166.50                                   
REMARK 500    ASN D 153     -168.78     81.59                                   
REMARK 500    SER D 165      140.37   -170.80                                   
REMARK 500    SER D 170     -149.22   -101.49                                   
REMARK 500    SER D 172      147.27    -39.92                                   
REMARK 500    TRP D 214     -106.56   -104.61                                   
REMARK 500    PRO D 249       -8.10    -50.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1M1L A   27   262  UNP    Q9UMX1   SUFU_HUMAN      27    262             
DBREF  1M1L B   27   262  UNP    Q9UMX1   SUFU_HUMAN      27    262             
DBREF  1M1L C   27   262  UNP    Q9UMX1   SUFU_HUMAN      27    262             
DBREF  1M1L D   27   262  UNP    Q9UMX1   SUFU_HUMAN      27    262             
SEQRES   1 A  236  ALA SER LEU PHE PRO PRO GLY LEU HIS ALA ILE TYR GLY          
SEQRES   2 A  236  GLU CYS ARG ARG LEU TYR PRO ASP GLN PRO ASN PRO LEU          
SEQRES   3 A  236  GLN VAL THR ALA ILE VAL LYS TYR TRP LEU GLY GLY PRO          
SEQRES   4 A  236  ASP PRO LEU ASP TYR VAL SER MET TYR ARG ASN VAL GLY          
SEQRES   5 A  236  SER PRO SER ALA ASN ILE PRO GLU HIS TRP HIS TYR ILE          
SEQRES   6 A  236  SER PHE GLY LEU SER ASP LEU TYR GLY ASP ASN ARG VAL          
SEQRES   7 A  236  HIS GLU PHE THR GLY THR ASP GLY PRO SER GLY PHE GLY          
SEQRES   8 A  236  PHE GLU LEU THR PHE ARG LEU LYS ARG GLU THR GLY GLU          
SEQRES   9 A  236  SER ALA PRO PRO THR TRP PRO ALA GLU LEU MET GLN GLY          
SEQRES  10 A  236  LEU ALA ARG TYR VAL PHE GLN SER GLU ASN THR PHE CYS          
SEQRES  11 A  236  SER GLY ASP HIS VAL SER TRP HIS SER PRO LEU ASP ASN          
SEQRES  12 A  236  SER GLU SER ARG ILE GLN HIS MET LEU LEU THR GLU ASP          
SEQRES  13 A  236  PRO GLN MET GLN PRO VAL GLN THR PRO PHE GLY VAL VAL          
SEQRES  14 A  236  THR PHE LEU GLN ILE VAL GLY VAL CYS THR GLU GLU LEU          
SEQRES  15 A  236  HIS SER ALA GLN GLN TRP ASN GLY GLN GLY ILE LEU GLU          
SEQRES  16 A  236  LEU LEU ARG THR VAL PRO ILE ALA GLY GLY PRO TRP LEU          
SEQRES  17 A  236  ILE THR ASP MET ARG ARG GLY GLU THR ILE PHE GLU ILE          
SEQRES  18 A  236  ASP PRO HIS LEU GLN GLU ARG VAL ASP LYS GLY ILE GLU          
SEQRES  19 A  236  THR ASP                                                      
SEQRES   1 B  236  ALA SER LEU PHE PRO PRO GLY LEU HIS ALA ILE TYR GLY          
SEQRES   2 B  236  GLU CYS ARG ARG LEU TYR PRO ASP GLN PRO ASN PRO LEU          
SEQRES   3 B  236  GLN VAL THR ALA ILE VAL LYS TYR TRP LEU GLY GLY PRO          
SEQRES   4 B  236  ASP PRO LEU ASP TYR VAL SER MET TYR ARG ASN VAL GLY          
SEQRES   5 B  236  SER PRO SER ALA ASN ILE PRO GLU HIS TRP HIS TYR ILE          
SEQRES   6 B  236  SER PHE GLY LEU SER ASP LEU TYR GLY ASP ASN ARG VAL          
SEQRES   7 B  236  HIS GLU PHE THR GLY THR ASP GLY PRO SER GLY PHE GLY          
SEQRES   8 B  236  PHE GLU LEU THR PHE ARG LEU LYS ARG GLU THR GLY GLU          
SEQRES   9 B  236  SER ALA PRO PRO THR TRP PRO ALA GLU LEU MET GLN GLY          
SEQRES  10 B  236  LEU ALA ARG TYR VAL PHE GLN SER GLU ASN THR PHE CYS          
SEQRES  11 B  236  SER GLY ASP HIS VAL SER TRP HIS SER PRO LEU ASP ASN          
SEQRES  12 B  236  SER GLU SER ARG ILE GLN HIS MET LEU LEU THR GLU ASP          
SEQRES  13 B  236  PRO GLN MET GLN PRO VAL GLN THR PRO PHE GLY VAL VAL          
SEQRES  14 B  236  THR PHE LEU GLN ILE VAL GLY VAL CYS THR GLU GLU LEU          
SEQRES  15 B  236  HIS SER ALA GLN GLN TRP ASN GLY GLN GLY ILE LEU GLU          
SEQRES  16 B  236  LEU LEU ARG THR VAL PRO ILE ALA GLY GLY PRO TRP LEU          
SEQRES  17 B  236  ILE THR ASP MET ARG ARG GLY GLU THR ILE PHE GLU ILE          
SEQRES  18 B  236  ASP PRO HIS LEU GLN GLU ARG VAL ASP LYS GLY ILE GLU          
SEQRES  19 B  236  THR ASP                                                      
SEQRES   1 C  236  ALA SER LEU PHE PRO PRO GLY LEU HIS ALA ILE TYR GLY          
SEQRES   2 C  236  GLU CYS ARG ARG LEU TYR PRO ASP GLN PRO ASN PRO LEU          
SEQRES   3 C  236  GLN VAL THR ALA ILE VAL LYS TYR TRP LEU GLY GLY PRO          
SEQRES   4 C  236  ASP PRO LEU ASP TYR VAL SER MET TYR ARG ASN VAL GLY          
SEQRES   5 C  236  SER PRO SER ALA ASN ILE PRO GLU HIS TRP HIS TYR ILE          
SEQRES   6 C  236  SER PHE GLY LEU SER ASP LEU TYR GLY ASP ASN ARG VAL          
SEQRES   7 C  236  HIS GLU PHE THR GLY THR ASP GLY PRO SER GLY PHE GLY          
SEQRES   8 C  236  PHE GLU LEU THR PHE ARG LEU LYS ARG GLU THR GLY GLU          
SEQRES   9 C  236  SER ALA PRO PRO THR TRP PRO ALA GLU LEU MET GLN GLY          
SEQRES  10 C  236  LEU ALA ARG TYR VAL PHE GLN SER GLU ASN THR PHE CYS          
SEQRES  11 C  236  SER GLY ASP HIS VAL SER TRP HIS SER PRO LEU ASP ASN          
SEQRES  12 C  236  SER GLU SER ARG ILE GLN HIS MET LEU LEU THR GLU ASP          
SEQRES  13 C  236  PRO GLN MET GLN PRO VAL GLN THR PRO PHE GLY VAL VAL          
SEQRES  14 C  236  THR PHE LEU GLN ILE VAL GLY VAL CYS THR GLU GLU LEU          
SEQRES  15 C  236  HIS SER ALA GLN GLN TRP ASN GLY GLN GLY ILE LEU GLU          
SEQRES  16 C  236  LEU LEU ARG THR VAL PRO ILE ALA GLY GLY PRO TRP LEU          
SEQRES  17 C  236  ILE THR ASP MET ARG ARG GLY GLU THR ILE PHE GLU ILE          
SEQRES  18 C  236  ASP PRO HIS LEU GLN GLU ARG VAL ASP LYS GLY ILE GLU          
SEQRES  19 C  236  THR ASP                                                      
SEQRES   1 D  236  ALA SER LEU PHE PRO PRO GLY LEU HIS ALA ILE TYR GLY          
SEQRES   2 D  236  GLU CYS ARG ARG LEU TYR PRO ASP GLN PRO ASN PRO LEU          
SEQRES   3 D  236  GLN VAL THR ALA ILE VAL LYS TYR TRP LEU GLY GLY PRO          
SEQRES   4 D  236  ASP PRO LEU ASP TYR VAL SER MET TYR ARG ASN VAL GLY          
SEQRES   5 D  236  SER PRO SER ALA ASN ILE PRO GLU HIS TRP HIS TYR ILE          
SEQRES   6 D  236  SER PHE GLY LEU SER ASP LEU TYR GLY ASP ASN ARG VAL          
SEQRES   7 D  236  HIS GLU PHE THR GLY THR ASP GLY PRO SER GLY PHE GLY          
SEQRES   8 D  236  PHE GLU LEU THR PHE ARG LEU LYS ARG GLU THR GLY GLU          
SEQRES   9 D  236  SER ALA PRO PRO THR TRP PRO ALA GLU LEU MET GLN GLY          
SEQRES  10 D  236  LEU ALA ARG TYR VAL PHE GLN SER GLU ASN THR PHE CYS          
SEQRES  11 D  236  SER GLY ASP HIS VAL SER TRP HIS SER PRO LEU ASP ASN          
SEQRES  12 D  236  SER GLU SER ARG ILE GLN HIS MET LEU LEU THR GLU ASP          
SEQRES  13 D  236  PRO GLN MET GLN PRO VAL GLN THR PRO PHE GLY VAL VAL          
SEQRES  14 D  236  THR PHE LEU GLN ILE VAL GLY VAL CYS THR GLU GLU LEU          
SEQRES  15 D  236  HIS SER ALA GLN GLN TRP ASN GLY GLN GLY ILE LEU GLU          
SEQRES  16 D  236  LEU LEU ARG THR VAL PRO ILE ALA GLY GLY PRO TRP LEU          
SEQRES  17 D  236  ILE THR ASP MET ARG ARG GLY GLU THR ILE PHE GLU ILE          
SEQRES  18 D  236  ASP PRO HIS LEU GLN GLU ARG VAL ASP LYS GLY ILE GLU          
SEQRES  19 D  236  THR ASP                                                      
FORMUL   5  HOH   *346(H2 O)                                                    
HELIX    1   1 PRO A   31  TYR A   45  1                                  15    
HELIX    2   2 LYS A   59  GLY A   63  5                                   5    
HELIX    3   3 THR A  135  GLU A  152  1                                  18    
HELIX    4   4 CYS A  204  TRP A  214  1                                  11    
HELIX    5   5 ASN A  215  VAL A  226  1                                  12    
HELIX    6   6 PRO A  227  GLY A  230  5                                   4    
HELIX    7   7 THR A  243  ASP A  248  1                                   6    
HELIX    8   8 HIS A  250  THR A  261  1                                  12    
HELIX    9   9 PRO B   31  TYR B   45  1                                  15    
HELIX   10  10 LYS B   59  GLY B   63  5                                   5    
HELIX   11  11 THR B  135  GLU B  152  1                                  18    
HELIX   12  12 CYS B  204  TRP B  214  1                                  11    
HELIX   13  13 ASN B  215  VAL B  226  1                                  12    
HELIX   14  14 PRO B  227  GLY B  230  5                                   4    
HELIX   15  15 THR B  243  ASP B  248  1                                   6    
HELIX   16  16 HIS B  250  THR B  261  1                                  12    
HELIX   17  17 PRO C   31  TYR C   45  1                                  15    
HELIX   18  18 LYS C   59  GLY C   63  5                                   5    
HELIX   19  19 THR C  135  SER C  151  1                                  17    
HELIX   20  20 CYS C  204  TRP C  214  1                                  11    
HELIX   21  21 ASN C  215  VAL C  226  1                                  12    
HELIX   22  22 PRO C  227  GLY C  230  5                                   4    
HELIX   23  23 THR C  243  ASP C  248  1                                   6    
HELIX   24  24 HIS C  250  THR C  261  1                                  12    
HELIX   25  25 PRO D   31  TYR D   45  1                                  15    
HELIX   26  26 LYS D   59  GLY D   63  5                                   5    
HELIX   27  27 THR D  135  GLN D  150  1                                  16    
HELIX   28  28 CYS D  204  TRP D  214  1                                  11    
HELIX   29  29 ASN D  215  VAL D  226  1                                  12    
HELIX   30  30 PRO D  227  GLY D  230  5                                   4    
HELIX   31  31 THR D  243  ASP D  248  1                                   6    
HELIX   32  32 HIS D  250  THR D  261  1                                  12    
SHEET    1   A14 HIS A 160  VAL A 161  0                                        
SHEET    2   A14 HIS A 176  GLU A 181 -1  O  MET A 177   N  VAL A 161           
SHEET    3   A14 GLY A 193  VAL A 203 -1  O  GLN A 199   N  THR A 180           
SHEET    4   A14 PRO A 113  LYS A 125  1  N  THR A 121   O  ILE A 200           
SHEET    5   A14 HIS A  87  PHE A  93 -1  N  TRP A  88   O  LEU A 124           
SHEET    6   A14 TYR A  70  ASN A  76 -1  N  ASN A  76   O  HIS A  87           
SHEET    7   A14 LEU A  52  THR A  55 -1  N  VAL A  54   O  VAL A  71           
SHEET    8   A14 LEU D  52  THR D  55 -1  O  GLN D  53   N  THR A  55           
SHEET    9   A14 TYR D  70  ASN D  76 -1  O  MET D  73   N  LEU D  52           
SHEET   10   A14 HIS D  87  PHE D  93 -1  O  HIS D  87   N  ASN D  76           
SHEET   11   A14 PRO D 113  LYS D 125 -1  O  LEU D 124   N  TRP D  88           
SHEET   12   A14 GLY D 193  VAL D 203  1  O  ILE D 200   N  THR D 121           
SHEET   13   A14 HIS D 176  GLU D 181 -1  N  THR D 180   O  GLN D 199           
SHEET   14   A14 HIS D 160  VAL D 161 -1  N  VAL D 161   O  MET D 177           
SHEET    1   B12 VAL A 188  THR A 190  0                                        
SHEET    2   B12 GLY A 193  VAL A 203 -1  O  VAL A 195   N  VAL A 188           
SHEET    3   B12 PRO A 113  LYS A 125  1  N  THR A 121   O  ILE A 200           
SHEET    4   B12 HIS A  87  PHE A  93 -1  N  TRP A  88   O  LEU A 124           
SHEET    5   B12 TYR A  70  ASN A  76 -1  N  ASN A  76   O  HIS A  87           
SHEET    6   B12 LEU A  52  THR A  55 -1  N  VAL A  54   O  VAL A  71           
SHEET    7   B12 LEU D  52  THR D  55 -1  O  GLN D  53   N  THR A  55           
SHEET    8   B12 TYR D  70  ASN D  76 -1  O  MET D  73   N  LEU D  52           
SHEET    9   B12 HIS D  87  PHE D  93 -1  O  HIS D  87   N  ASN D  76           
SHEET   10   B12 PRO D 113  LYS D 125 -1  O  LEU D 124   N  TRP D  88           
SHEET   11   B12 GLY D 193  VAL D 203  1  O  ILE D 200   N  THR D 121           
SHEET   12   B12 VAL D 188  THR D 190 -1  N  VAL D 188   O  VAL D 195           
SHEET    1   C14 HIS B 160  VAL B 161  0                                        
SHEET    2   C14 HIS B 176  GLU B 181 -1  O  MET B 177   N  VAL B 161           
SHEET    3   C14 GLY B 193  VAL B 203 -1  O  GLN B 199   N  THR B 180           
SHEET    4   C14 PRO B 113  LYS B 125  1  N  THR B 121   O  ILE B 200           
SHEET    5   C14 HIS B  87  PHE B  93 -1  N  TRP B  88   O  LEU B 124           
SHEET    6   C14 TYR B  70  ASN B  76 -1  N  ASN B  76   O  HIS B  87           
SHEET    7   C14 LEU B  52  THR B  55 -1  N  VAL B  54   O  VAL B  71           
SHEET    8   C14 LEU C  52  THR C  55 -1  O  GLN C  53   N  THR B  55           
SHEET    9   C14 TYR C  70  ASN C  76 -1  O  VAL C  71   N  VAL C  54           
SHEET   10   C14 HIS C  87  PHE C  93 -1  O  HIS C  87   N  ASN C  76           
SHEET   11   C14 PRO C 113  LYS C 125 -1  O  LEU C 124   N  TRP C  88           
SHEET   12   C14 GLY C 193  VAL C 203  1  O  ILE C 200   N  THR C 121           
SHEET   13   C14 HIS C 176  GLU C 181 -1  N  THR C 180   O  GLN C 199           
SHEET   14   C14 HIS C 160  VAL C 161 -1  N  VAL C 161   O  MET C 177           
SHEET    1   D12 VAL B 188  THR B 190  0                                        
SHEET    2   D12 GLY B 193  VAL B 203 -1  O  VAL B 195   N  VAL B 188           
SHEET    3   D12 PRO B 113  LYS B 125  1  N  THR B 121   O  ILE B 200           
SHEET    4   D12 HIS B  87  PHE B  93 -1  N  TRP B  88   O  LEU B 124           
SHEET    5   D12 TYR B  70  ASN B  76 -1  N  ASN B  76   O  HIS B  87           
SHEET    6   D12 LEU B  52  THR B  55 -1  N  VAL B  54   O  VAL B  71           
SHEET    7   D12 LEU C  52  THR C  55 -1  O  GLN C  53   N  THR B  55           
SHEET    8   D12 TYR C  70  ASN C  76 -1  O  VAL C  71   N  VAL C  54           
SHEET    9   D12 HIS C  87  PHE C  93 -1  O  HIS C  87   N  ASN C  76           
SHEET   10   D12 PRO C 113  LYS C 125 -1  O  LEU C 124   N  TRP C  88           
SHEET   11   D12 GLY C 193  VAL C 203  1  O  ILE C 200   N  THR C 121           
SHEET   12   D12 VAL C 188  THR C 190 -1  N  VAL C 188   O  VAL C 195           
CRYST1  173.025  173.025  290.833  90.00  90.00 120.00 H 3 2        72          
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      0.005780  0.003337  0.000000        0.00000                         
SCALE2      0.000000  0.006674  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003438        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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