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Database: PDB
Entry: 1LWS
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Original site: 1LWS 
HEADER    HYDROLASE/DNA                           03-JUN-02   1LWS              
TITLE     CRYSTAL STRUCTURE OF THE INTEIN HOMING ENDONUCLEASE PI-SCEI           
TITLE    2 BOUND TO ITS RECOGNITION SEQUENCE                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PI-SCEI DNA RECOGNITION REGION TOP STRAND;                 
COMPND   3 CHAIN: B;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: PI-SCEI DNA RECOGNITION REGION BOTTOM STRAND;              
COMPND   7 CHAIN: C;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: ENDONUCLEASE PI-SCEI;                                      
COMPND  11 CHAIN: A;                                                            
COMPND  12 SYNONYM: PI-SCEI, VMA-DERIVED ENDONUCLEASE, VDE, SCE VMA             
COMPND  13 INTEIN;                                                              
COMPND  14 EC: 3.1.-.-;                                                         
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 MOL_ID: 2;                                                           
SOURCE   4 SYNTHETIC: YES;                                                      
SOURCE   5 MOL_ID: 3;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   7 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   8 ORGANISM_TAXID: 4932;                                                
SOURCE   9 GENE: VMA1;                                                          
SOURCE  10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  12 EXPRESSION_SYSTEM_STRAIN: DL41 (DE3);                                
SOURCE  13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PT7PI-SCEI                                
KEYWDS    HOMING ENDONUCLEASE, INTEIN, PROTEIN-DNA COMPLEX,                     
KEYWDS   2 ENDONUCLEASE, HYDROLASE/DNA COMPLEX                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.M.MOURE,F.S.GIMBLE,F.A.QUIOCHO                                      
REVDAT   2   24-FEB-09 1LWS    1       VERSN                                    
REVDAT   1   27-SEP-02 1LWS    0                                                
JRNL        AUTH   C.M.MOURE,F.S.GIMBLE,F.A.QUIOCHO                             
JRNL        TITL   CRYSTAL STRUCTURE OF THE INTEIN HOMING                       
JRNL        TITL 2 ENDONUCLEASE PI-SCEI BOUND TO ITS RECOGNITION                
JRNL        TITL 3 SEQUENCE.                                                    
JRNL        REF    NAT.STRUCT.BIOL.              V.   9   764 2002              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   12219083                                                     
JRNL        DOI    10.1038/NSB840                                               
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   X.DUAN,F.S.GIMBLE,F.A.QUIOCHO                                
REMARK   1  TITL   CRYSTAL STRUCTURE OF PI-SCEI, A HOMING                       
REMARK   1  TITL 2 ENDONUCLEASE WITH PROTEIN SPLICING ACTIVITY                  
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V.  89   555 1997              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   1  DOI    10.1016/S0092-8674(00)80237-8                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 11584                          
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 SET) : 0.287                           
REMARK   3   FREE R VALUE                     : 0.310                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 622                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.012                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1881                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3719                       
REMARK   3   BIN FREE R VALUE                    : 0.3945                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 124                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.043                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3360                                    
REMARK   3   NUCLEIC ACID ATOMS       : 1394                                    
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 69.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 10.91000                                             
REMARK   3    B22 (A**2) : 10.91000                                             
REMARK   3    B33 (A**2) : -21.83000                                            
REMARK   3    B12 (A**2) : 11.77000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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) : 0.63                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.89                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.25                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : GROUP FOR PROTEIN ATOMS, OVERALL FOR      
REMARK   3                            DNA                                       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 8.580 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 13.300; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 7.640 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 11.130; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.21                                                 
REMARK   3   BSOL        : 28.14                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 1LWS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB016357.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL; NULL                         
REMARK 200  TEMPERATURE           (KELVIN) : 200; NULL                          
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : APS; APS                           
REMARK 200  BEAMLINE                       : 14-BM-D; 14-BM-C                   
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792, 0.9789, 0.9611; 1.0        
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; NULL                          
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4; NULL               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12539                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 9.000                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : 0.05900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.20100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD; NULL                                      
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 200, NA HEPES, CALCIUM               
REMARK 280  CHLORIDE, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE        
REMARK 280  291K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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      141.13333            
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       70.56667            
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      105.85000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       35.28333            
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      176.41667            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      141.13333            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       70.56667            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       35.28333            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      105.85000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      176.41667            
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, 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      DC B     1                                                      
REMARK 465      DG B    36                                                      
REMARK 465      DG B    37                                                      
REMARK 465      DG C     1                                                      
REMARK 465      DC C     2                                                      
REMARK 465      DC C     3                                                      
REMARK 465     GLU A   100                                                      
REMARK 465     TYR A   101                                                      
REMARK 465     GLU A   134                                                      
REMARK 465     GLY A   135                                                      
REMARK 465     GLU A   251                                                      
REMARK 465     TYR A   252                                                      
REMARK 465     LYS A   253                                                      
REMARK 465     ASP A   254                                                      
REMARK 465     ARG A   255                                                      
REMARK 465     LYS A   256                                                      
REMARK 465     GLU A   257                                                      
REMARK 465     PRO A   258                                                      
REMARK 465     GLN A   259                                                      
REMARK 465     LYS A   269                                                      
REMARK 465     VAL A   270                                                      
REMARK 465     VAL A   271                                                      
REMARK 465     ARG A   272                                                      
REMARK 465     GLY A   273                                                      
REMARK 465     ASN A   274                                                      
REMARK 465     GLY A   275                                                      
REMARK 465     ILE A   276                                                      
REMARK 465     ARG A   277                                                      
REMARK 465     ASN A   278                                                      
REMARK 465     ASN A   279                                                      
REMARK 465     LEU A   280                                                      
REMARK 465     ASN A   281                                                      
REMARK 465     THR A   282                                                      
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     DC B   3   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DT C   6   N1  -  C1' -  C2' ANGL. DEV. =   8.5 DEGREES          
REMARK 500     DC C  14   O4' -  C1' -  N1  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DT C  21   O4' -  C1' -  N1  ANGL. DEV. =   2.6 DEGREES          
REMARK 500     DC C  22   O4' -  C1' -  N1  ANGL. DEV. =   3.2 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    PHE A   2     -156.99   -104.44                                   
REMARK 500    SER A  14     -166.15    -57.10                                   
REMARK 500    GLU A  19       30.22    -67.76                                   
REMARK 500    ASN A  20      -14.91   -150.48                                   
REMARK 500    ILE A  38      -43.17   -135.98                                   
REMARK 500    LEU A  40       76.61   -118.95                                   
REMARK 500    GLU A  45      168.82    170.27                                   
REMARK 500    GLN A  55       26.25    -67.32                                   
REMARK 500    SER A  64        7.11     92.40                                   
REMARK 500    LEU A  70       15.62   -149.79                                   
REMARK 500    LEU A  71      104.61     77.95                                   
REMARK 500    ILE A  96     -150.55    -98.56                                   
REMARK 500    LYS A  97       -0.43    -42.93                                   
REMARK 500    GLU A 103      165.12    176.86                                   
REMARK 500    ARG A 118      124.74    -28.95                                   
REMARK 500    LEU A 122     -178.20    172.50                                   
REMARK 500    LYS A 128      108.23   -170.96                                   
REMARK 500    ARG A 138      -79.56    -55.52                                   
REMARK 500    LEU A 142       -5.73    -54.27                                   
REMARK 500    SER A 150      163.43    171.94                                   
REMARK 500    ASN A 151      -60.44   -102.00                                   
REMARK 500    LYS A 152      140.33    -34.32                                   
REMARK 500    ARG A 162      -15.05    -46.24                                   
REMARK 500    GLN A 177     -166.64   -104.80                                   
REMARK 500    SER A 196     -155.84   -152.16                                   
REMARK 500    LYS A 197      147.81     -0.00                                   
REMARK 500    PHE A 198       74.46    -67.64                                   
REMARK 500    ILE A 202      -21.24     98.00                                   
REMARK 500    GLU A 203        2.22   -158.64                                   
REMARK 500    LYS A 206      -80.31    -70.97                                   
REMARK 500    SER A 221       24.81    -71.24                                   
REMARK 500    ASP A 222       -6.90   -144.02                                   
REMARK 500    ALA A 224       65.11    -63.47                                   
REMARK 500    ASN A 247       46.86     79.38                                   
REMARK 500    ASP A 288       43.63    -74.75                                   
REMARK 500    ALA A 289      -55.27   -151.51                                   
REMARK 500    VAL A 291      -61.68   -102.33                                   
REMARK 500    ASN A 302      129.24    179.23                                   
REMARK 500    PHE A 306      -44.22    -21.76                                   
REMARK 500    ASN A 311      121.80    -22.73                                   
REMARK 500    ILE A 312      -70.18    -49.46                                   
REMARK 500    HIS A 333       44.80   -107.67                                   
REMARK 500    THR A 341      154.41    149.40                                   
REMARK 500    ARG A 347      -79.59    -43.52                                   
REMARK 500    ALA A 409      -78.64    -48.84                                   
REMARK 500    ALA A 410     -152.54    -99.18                                   
REMARK 500    SER A 437      135.41    -13.47                                   
REMARK 500    ASP A 438       41.86    -64.24                                   
REMARK 500    ASP A 439       64.57   -177.84                                   
REMARK 500    GLN A 449       11.56     84.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500     DA B  24         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 326   OD2                                                    
REMARK 620 2 ASP A 326   OD1  51.5                                              
REMARK 620 3 ASP A 218   OD1  70.5  65.9                                        
REMARK 620 4 GLY A 217   O    69.2 118.8  83.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 325   O                                                      
REMARK 620 2 ASP A 218   OD1 100.8                                              
REMARK 620 3 ASP A 218   OD2  62.2  47.9                                        
REMARK 620 4 ASP A 326   OD1  73.6  68.9  85.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1VDE   RELATED DB: PDB                                   
REMARK 900 PI-SCEI, A HOMING ENDONUCLEASE WITH PROTEIN SPLICING                 
REMARK 900 ACTIVITY                                                             
REMARK 900 RELATED ID: 1LWT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE INTEIN HOMING ENDONUCLEASE PI_SCEI          
REMARK 900 BOUND TO ITS SUBSTRATE DNA (CA2+ FREE)                               
DBREF  1LWS A    1   454  UNP    P17255   VATA_YEAST     284    737             
DBREF  1LWS B    1    37  PDB    1LWS     1LWS             1     37             
DBREF  1LWS C    1    37  PDB    1LWS     1LWS             1     37             
SEQADV 1LWS MSE A   10  UNP  P17255    MET   293 MODIFIED RESIDUE               
SEQADV 1LWS MSE A   28  UNP  P17255    MET   311 MODIFIED RESIDUE               
SEQADV 1LWS MSE A   47  UNP  P17255    MET   330 MODIFIED RESIDUE               
SEQADV 1LWS MSE A  109  UNP  P17255    MET   392 MODIFIED RESIDUE               
SEQADV 1LWS MSE A  193  UNP  P17255    MET   476 MODIFIED RESIDUE               
SEQADV 1LWS MSE A  236  UNP  P17255    MET   519 MODIFIED RESIDUE               
SEQADV 1LWS MSE A  372  UNP  P17255    MET   655 MODIFIED RESIDUE               
SEQADV 1LWS MSE A  385  UNP  P17255    MET   668 MODIFIED RESIDUE               
SEQRES   1 B   37   DC  DT  DC  DT  DA  DT  DG  DT  DC  DG  DG  DG  DT          
SEQRES   2 B   37   DG  DC  DG  DG  DA  DG  DA  DA  DA  DG  DA  DG  DG          
SEQRES   3 B   37   DT  DA  DA  DT  DG  DA  DA  DA  DT  DG  DG                  
SEQRES   1 C   37   DG  DC  DC  DA  DT  DT  DT  DC  DA  DT  DT  DA  DC          
SEQRES   2 C   37   DC  DT  DC  DT  DT  DT  DC  DT  DC  DC  DG  DC  DA          
SEQRES   3 C   37   DC  DC  DC  DG  DA  DC  DA  DT  DA  DG  DA                  
SEQRES   1 A  454  CYS PHE ALA LYS GLY THR ASN VAL LEU MSE ALA ASP GLY          
SEQRES   2 A  454  SER ILE GLU CYS ILE GLU ASN ILE GLU VAL GLY ASN LYS          
SEQRES   3 A  454  VAL MSE GLY LYS ASP GLY ARG PRO ARG GLU VAL ILE LYS          
SEQRES   4 A  454  LEU PRO ARG GLY ARG GLU THR MSE TYR SER VAL VAL GLN          
SEQRES   5 A  454  LYS SER GLN HIS ARG ALA HIS LYS SER ASP SER SER ARG          
SEQRES   6 A  454  GLU VAL PRO GLU LEU LEU LYS PHE THR CYS ASN ALA THR          
SEQRES   7 A  454  HIS GLU LEU VAL VAL ARG THR PRO ARG SER VAL ARG ARG          
SEQRES   8 A  454  LEU SER ARG THR ILE LYS GLY VAL GLU TYR PHE GLU VAL          
SEQRES   9 A  454  ILE THR PHE GLU MSE GLY GLN LYS LYS ALA PRO ASP GLY          
SEQRES  10 A  454  ARG ILE VAL GLU LEU VAL LYS GLU VAL SER LYS SER TYR          
SEQRES  11 A  454  PRO ILE SER GLU GLY PRO GLU ARG ALA ASN GLU LEU VAL          
SEQRES  12 A  454  GLU SER TYR ARG LYS ALA SER ASN LYS ALA TYR PHE GLU          
SEQRES  13 A  454  TRP THR ILE GLU ALA ARG ASP LEU SER LEU LEU GLY SER          
SEQRES  14 A  454  HIS VAL ARG LYS ALA THR TYR GLN THR TYR ALA PRO ILE          
SEQRES  15 A  454  LEU TYR GLU ASN ASP HIS PHE PHE ASP TYR MSE GLN LYS          
SEQRES  16 A  454  SER LYS PHE HIS LEU THR ILE GLU GLY PRO LYS VAL LEU          
SEQRES  17 A  454  ALA TYR LEU LEU GLY LEU TRP ILE GLY ASP GLY LEU SER          
SEQRES  18 A  454  ASP ARG ALA THR PHE SER VAL ASP SER ARG ASP THR SER          
SEQRES  19 A  454  LEU MSE GLU ARG VAL THR GLU TYR ALA GLU LYS LEU ASN          
SEQRES  20 A  454  LEU CYS ALA GLU TYR LYS ASP ARG LYS GLU PRO GLN VAL          
SEQRES  21 A  454  ALA LYS THR VAL ASN LEU TYR SER LYS VAL VAL ARG GLY          
SEQRES  22 A  454  ASN GLY ILE ARG ASN ASN LEU ASN THR GLU ASN PRO LEU          
SEQRES  23 A  454  TRP ASP ALA ILE VAL GLY LEU GLY PHE LEU LYS ASP GLY          
SEQRES  24 A  454  VAL LYS ASN ILE PRO SER PHE LEU SER THR ASP ASN ILE          
SEQRES  25 A  454  GLY THR ARG GLU THR PHE LEU ALA GLY LEU ILE ASP SER          
SEQRES  26 A  454  ASP GLY TYR VAL THR ASP GLU HIS GLY ILE LYS ALA THR          
SEQRES  27 A  454  ILE LYS THR ILE HIS THR SER VAL ARG ASP GLY LEU VAL          
SEQRES  28 A  454  SER LEU ALA ARG SER LEU GLY LEU VAL VAL SER VAL ASN          
SEQRES  29 A  454  ALA GLU PRO ALA LYS VAL ASP MSE ASN GLY THR LYS HIS          
SEQRES  30 A  454  LYS ILE SER TYR ALA ILE TYR MSE SER GLY GLY ASP VAL          
SEQRES  31 A  454  LEU LEU ASN VAL LEU SER LYS CYS ALA GLY SER LYS LYS          
SEQRES  32 A  454  PHE ARG PRO ALA PRO ALA ALA ALA PHE ALA ARG GLU CYS          
SEQRES  33 A  454  ARG GLY PHE TYR PHE GLU LEU GLN GLU LEU LYS GLU ASP          
SEQRES  34 A  454  ASP TYR TYR GLY ILE THR LEU SER ASP ASP SER ASP HIS          
SEQRES  35 A  454  GLN PHE LEU LEU ALA ASN GLN VAL VAL VAL HIS ASN              
MODRES 1LWS MSE A   10  MET  SELENOMETHIONINE                                   
MODRES 1LWS MSE A   28  MET  SELENOMETHIONINE                                   
MODRES 1LWS MSE A   47  MET  SELENOMETHIONINE                                   
MODRES 1LWS MSE A  109  MET  SELENOMETHIONINE                                   
MODRES 1LWS MSE A  193  MET  SELENOMETHIONINE                                   
MODRES 1LWS MSE A  236  MET  SELENOMETHIONINE                                   
MODRES 1LWS MSE A  372  MET  SELENOMETHIONINE                                   
MODRES 1LWS MSE A  385  MET  SELENOMETHIONINE                                   
HET    MSE  A  10       8                                                       
HET    MSE  A  28       8                                                       
HET    MSE  A  47       8                                                       
HET    MSE  A 109       8                                                       
HET    MSE  A 193       8                                                       
HET    MSE  A 236       8                                                       
HET    MSE  A 372       8                                                       
HET    MSE  A 385       8                                                       
HET     CA  A 501       1                                                       
HET     CA  A 502       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  MSE    8(C5 H11 N O2 SE)                                            
FORMUL   4   CA    2(CA 2+)                                                     
HELIX    1   1 GLU A   19  ILE A   21  5                                   3    
HELIX    2   2 ARG A   57  ASP A   62  1                                   6    
HELIX    3   3 PRO A  136  LYS A  148  1                                  13    
HELIX    4   4 ARG A  162  LEU A  167  5                                   6    
HELIX    5   5 SER A  169  THR A  175  1                                   7    
HELIX    6   6 PHE A  189  LYS A  195  1                                   7    
HELIX    7   7 GLU A  203  ASP A  218  1                                  16    
HELIX    8   8 ASP A  232  ASN A  247  1                                  16    
HELIX    9   9 LEU A  286  VAL A  291  1                                   6    
HELIX   10  10 SER A  305  ASP A  310  5                                   6    
HELIX   11  11 ASN A  311  ASP A  326  1                                  16    
HELIX   12  12 HIS A  343  LEU A  357  1                                  15    
HELIX   13  13 GLY A  388  SER A  396  1                                   9    
SHEET    1   A 2 ASN A   7  VAL A   8  0                                        
SHEET    2   A 2 GLU A  16  CYS A  17 -1  O  GLU A  16   N  VAL A   8           
SHEET    1   B 3 LYS A  26  MSE A  28  0                                        
SHEET    2   B 3 PRO A  34  LYS A  39 -1  O  ARG A  35   N  VAL A  27           
SHEET    3   B 3 THR A 435  LEU A 436 -1  O  THR A 435   N  LYS A  39           
SHEET    1   C 3 LYS A  72  ASN A  76  0                                        
SHEET    2   C 3 ARG A  42  GLN A  52 -1  N  VAL A  50   O  PHE A  73           
SHEET    3   C 3 PHE A 421  TYR A 432 -1  O  TYR A 431   N  GLY A  43           
SHEET    1   D 2 GLU A  80  PRO A  86  0                                        
SHEET    2   D 2 TYR A 154  GLU A 160 -1  O  ILE A 159   N  LEU A  81           
SHEET    1   E 3 VAL A  89  ARG A  90  0                                        
SHEET    2   E 3 ILE A 105  LYS A 113 -1  O  ILE A 105   N  ARG A  90           
SHEET    3   E 3 ILE A 119  VAL A 126 -1  O  VAL A 126   N  THR A 106           
SHEET    1   F 2 GLN A 177  TYR A 179  0                                        
SHEET    2   F 2 ARG A 417  PHE A 419 -1  O  PHE A 419   N  GLN A 177           
SHEET    1   G 2 THR A 225  ASP A 229  0                                        
SHEET    2   G 2 ALA A 261  ASN A 265 -1  O  LYS A 262   N  VAL A 228           
SHEET    1   H 2 LEU A 296  LYS A 297  0                                        
SHEET    2   H 2 VAL A 300  LYS A 301 -1  O  VAL A 300   N  LYS A 297           
SHEET    1   I 4 GLY A 327  THR A 330  0                                        
SHEET    2   I 4 LYS A 336  ILE A 339 -1  O  THR A 338   N  TYR A 328           
SHEET    3   I 4 SER A 380  SER A 386 -1  O  ILE A 383   N  ILE A 339           
SHEET    4   I 4 VAL A 360  GLU A 366 -1  N  GLU A 366   O  SER A 380           
SHEET    1   J 2 VAL A 370  ASP A 371  0                                        
SHEET    2   J 2 THR A 375  LYS A 376 -1  O  THR A 375   N  ASP A 371           
SHEET    1   K 2 GLN A 443  LEU A 445  0                                        
SHEET    2   K 2 VAL A 451  HIS A 453 -1  O  VAL A 452   N  PHE A 444           
LINK         C   LEU A   9                 N   MSE A  10     1555   1555  1.33  
LINK         C   MSE A  10                 N   ALA A  11     1555   1555  1.34  
LINK         C   VAL A  27                 N   MSE A  28     1555   1555  1.34  
LINK         C   MSE A  28                 N   GLY A  29     1555   1555  1.34  
LINK         C   THR A  46                 N   MSE A  47     1555   1555  1.33  
LINK         C   MSE A  47                 N   TYR A  48     1555   1555  1.33  
LINK         C   GLU A 108                 N   MSE A 109     1555   1555  1.32  
LINK         C   MSE A 109                 N   GLY A 110     1555   1555  1.33  
LINK         C   TYR A 192                 N   MSE A 193     1555   1555  1.33  
LINK         C   MSE A 193                 N   GLN A 194     1555   1555  1.34  
LINK         C   LEU A 235                 N   MSE A 236     1555   1555  1.33  
LINK         C   MSE A 236                 N   GLU A 237     1555   1555  1.33  
LINK         C   ASP A 371                 N   MSE A 372     1555   1555  1.33  
LINK         C   MSE A 372                 N   ASN A 373     1555   1555  1.33  
LINK         C   TYR A 384                 N   MSE A 385     1555   1555  1.33  
LINK         C   MSE A 385                 N   SER A 386     1555   1555  1.33  
LINK        CA    CA A 501                 OD2 ASP A 326     1555   1555  2.06  
LINK        CA    CA A 501                 OD1 ASP A 326     1555   1555  2.74  
LINK        CA    CA A 501                 OD1 ASP A 218     1555   1555  2.65  
LINK        CA    CA A 501                 O   GLY A 217     1555   1555  2.78  
LINK        CA    CA A 502                 O   SER A 325     1555   1555  2.85  
LINK        CA    CA A 502                 OD1 ASP A 218     1555   1555  2.85  
LINK        CA    CA A 502                 OD2 ASP A 218     1555   1555  2.61  
LINK        CA    CA A 502                 OD1 ASP A 326     1555   1555  2.26  
SITE     1 AC1  3 GLY A 217  ASP A 218  ASP A 326                               
SITE     1 AC2  3 ASP A 218  SER A 325  ASP A 326                               
CRYST1  123.000  123.000  211.700  90.00  90.00 120.00 P 65 2 2     12          
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      0.008130  0.004694  0.000000        0.00000                         
SCALE2      0.000000  0.009388  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004724        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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