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Database: PDB
Entry: 1OZV
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HEADER    TRANSFERASE                             09-APR-03   1OZV              
TITLE     CRYSTAL STRUCTURE OF THE SET DOMAIN OF LSMT BOUND TO LYSINE AND ADOHCY
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE-1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE LARGE      
COMPND   3 SUBUNIT N-METHYLTRANSFERASE, CHLOROPLAST;                            
COMPND   4 CHAIN: A, B, C;                                                      
COMPND   5 SYNONYM: [RIBULOSE-BISPHOSPHATE-CARBOXYLASE]-LYSINE N-               
COMPND   6 METHYLTRANSFERASE, RUBISCO METHYLTRANSFERASE, RUBISCO LSMT, RBCMT;   
COMPND   7 EC: 2.1.1.127;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE   3 ORGANISM_COMMON: PEA;                                                
SOURCE   4 ORGANISM_TAXID: 3888;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PDEST14                                   
KEYWDS    SET DOMAIN, LYSINE N-METHYLATION, MULTIPLE METHYLATION,               
KEYWDS   2 PHOTOSYNTHESIS, POST-TRANSLATIONAL MODIFICATION, TRANSFERASE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.C.TRIEVEL,E.M.FLYNN,R.L.HOUTZ,J.H.HURLEY                            
REVDAT   3   13-JUL-11 1OZV    1       VERSN                                    
REVDAT   2   24-FEB-09 1OZV    1       VERSN                                    
REVDAT   1   01-JUL-03 1OZV    0                                                
JRNL        AUTH   R.C.TRIEVEL,E.M.FLYNN,R.L.HOUTZ,J.H.HURLEY                   
JRNL        TITL   MECHANISM OF MULTIPLE LYSINE METHYLATION BY THE SET DOMAIN   
JRNL        TITL 2 ENZYME RUBISCO LSMT                                          
JRNL        REF    NAT.STRUCT.BIOL.              V.  10   545 2003              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   12819771                                                     
JRNL        DOI    10.1038/NSB946                                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 29.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 612033.970                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 72448                          
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) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3664                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
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) : 2.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 9920                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3690                       
REMARK   3   BIN FREE R VALUE                    : 0.4120                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 504                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.018                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10552                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 108                                     
REMARK   3   SOLVENT ATOMS            : 644                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 67.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -15.72000                                            
REMARK   3    B22 (A**2) : 23.29000                                             
REMARK   3    B33 (A**2) : -7.57000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.38                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.58                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.44                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.64                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.83                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.370 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.410 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.770 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.820 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 49.22                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
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  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : SAH.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : SAH.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1OZV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-APR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018851.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC CONFOCAL MIRRORS             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79741                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
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     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.49400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.510                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS 1.1                                               
REMARK 200 STARTING MODEL: PDB ENTRY 1MLV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.95-1.10 M SODIUM ACETATE, 100 MM       
REMARK 280  LYSINE ACETATE, 1 MM TCEP, 400 UM S-ADENOSYLHOMOCYSTEINE, PH 6.8,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       65.98000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       78.45000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      133.77500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       65.98000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       78.45000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      133.77500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       65.98000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       78.45000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      133.77500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       65.98000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       78.45000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      133.77500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 9020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 60250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    45                                                      
REMARK 465     THR A    46                                                      
REMARK 465     GLU A    47                                                      
REMARK 465     PRO A    48                                                      
REMARK 465     SER A    49                                                      
REMARK 465     GLY A   258                                                      
REMARK 465     ALA A   259                                                      
REMARK 465     ALA A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     LEU A   262                                                      
REMARK 465     PHE A   263                                                      
REMARK 465     SER A   264                                                      
REMARK 465     TRP A   265                                                      
REMARK 465     ASP A   266                                                      
REMARK 465     GLN A   488                                                      
REMARK 465     MET B    45                                                      
REMARK 465     THR B    46                                                      
REMARK 465     GLU B    47                                                      
REMARK 465     MET C    45                                                      
REMARK 465     THR C    46                                                      
REMARK 465     GLU C    47                                                      
REMARK 465     PRO C    48                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  72   C   -  N   -  CA  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    PRO A  72   C   -  N   -  CD  ANGL. DEV. = -12.7 DEGREES          
REMARK 500    PRO B 236   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    PRO C 236   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    ASP C 251   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    GLU A  63       49.37    -75.94                                   
REMARK 500    GLU A  64       -1.94   -158.54                                   
REMARK 500    VAL A  66      -77.90    -77.75                                   
REMARK 500    THR A  68      -83.52    -99.33                                   
REMARK 500    ALA A  69      -26.20   -161.08                                   
REMARK 500    PRO A  72       24.24    -63.70                                   
REMARK 500    ASP A  89      123.41    -28.03                                   
REMARK 500    TRP A 104     -170.96    -61.26                                   
REMARK 500    ILE A 105       65.34   -161.61                                   
REMARK 500    PRO A 107      -36.93    -39.28                                   
REMARK 500    ILE A 195      -43.70   -132.35                                   
REMARK 500    LYS A 200       -7.54    -57.27                                   
REMARK 500    PHE A 203       78.25   -112.33                                   
REMARK 500    PRO A 236      -32.82    -33.23                                   
REMARK 500    GLU A 250       15.52    -67.33                                   
REMARK 500    HIS A 252      109.75     45.82                                   
REMARK 500    ASP A 288      114.76   -179.21                                   
REMARK 500    ASN A 306      108.82    -50.04                                   
REMARK 500    PRO A 323       -9.29    -57.45                                   
REMARK 500    LEU A 364      -73.72    -23.24                                   
REMARK 500    LEU A 386      -79.58    -71.95                                   
REMARK 500    SER A 387      151.55    174.21                                   
REMARK 500    VAL A 388      -63.23    -90.92                                   
REMARK 500    SER A 428      -68.94    -28.31                                   
REMARK 500    LEU B  50      -70.14    -88.26                                   
REMARK 500    ASN B  93       -2.47     87.52                                   
REMARK 500    SER B 120      -32.10    -37.63                                   
REMARK 500    ILE B 195      -54.40   -130.67                                   
REMARK 500    ASN B 199       56.91    -93.87                                   
REMARK 500    SER B 225      -89.31   -117.17                                   
REMARK 500    ARG B 226       94.87    -13.65                                   
REMARK 500    LEU B 227     -160.08   -161.18                                   
REMARK 500    ASN B 229       19.72     56.59                                   
REMARK 500    ASN B 231       -1.61   -144.10                                   
REMARK 500    ASP B 239        1.43    -64.55                                   
REMARK 500    LYS B 257     -145.49    -84.34                                   
REMARK 500    ASP B 288      102.47    175.28                                   
REMARK 500    PRO B 323       -2.15    -57.51                                   
REMARK 500    LEU B 364      -83.16    -16.31                                   
REMARK 500    LEU B 386      -77.32    -67.58                                   
REMARK 500    SER B 387      148.34    166.16                                   
REMARK 500    VAL B 388      -70.54    -85.72                                   
REMARK 500    SER B 428      -69.94    -29.40                                   
REMARK 500    ASP B 471       54.03   -108.07                                   
REMARK 500    THR C  71      104.58    -40.49                                   
REMARK 500    ILE C 195      -45.83   -135.68                                   
REMARK 500    ASN C 199       48.39    -95.69                                   
REMARK 500    PRO C 236      -65.80    -20.96                                   
REMARK 500    HIS C 252      104.68     36.18                                   
REMARK 500    ALA C 260     -126.29     51.90                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      61 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASP C 251        18.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1101        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH A1170        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH B1183        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH B1185        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH B1193        DISTANCE =  5.57 ANGSTROMS                       
REMARK 525    HOH C1195        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH C1196        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH C1233        DISTANCE =  5.05 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LYS A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LYS A 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LYS A 900                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH C 1002                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MLV   RELATED DB: PDB                                   
REMARK 900 STRUCTURE AND CATALYTIC MECHANISM OF A SET DOMAIN PROTEIN            
REMARK 900 METHYLTRANSFERASE                                                    
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AUTHORS INFORMED THAT RESIDUES 483-488 RESULT FROM                   
REMARK 999 A C-TERMINAL TEV PROTEASE CLEAVAGE SITE THAT WAS                     
REMARK 999 ENGINEERED INTO THE ENZYME AFTER LEU 482. AFTER                      
REMARK 999 CLEAVAGE, THESE SIX RESIDUES WERE LEFT ON THE                        
REMARK 999 C-TERMINUS OF THIS CONSTRUCT.                                        
DBREF  1OZV A   46   482  UNP    Q43088   RBCMT_PEA       46    482             
DBREF  1OZV B   46   482  UNP    Q43088   RBCMT_PEA       46    482             
DBREF  1OZV C   46   482  UNP    Q43088   RBCMT_PEA       46    482             
SEQADV 1OZV MET A   45  UNP  Q43088              INITIATING MET                 
SEQADV 1OZV GLU A  483  UNP  Q43088              ENGINEERED                     
SEQADV 1OZV ASN A  484  UNP  Q43088              ENGINEERED                     
SEQADV 1OZV LEU A  485  UNP  Q43088              ENGINEERED                     
SEQADV 1OZV TYR A  486  UNP  Q43088              ENGINEERED                     
SEQADV 1OZV PHE A  487  UNP  Q43088              ENGINEERED                     
SEQADV 1OZV GLN A  488  UNP  Q43088              ENGINEERED                     
SEQADV 1OZV MET B   45  UNP  Q43088              INITIATING MET                 
SEQADV 1OZV GLU B  483  UNP  Q43088              ENGINEERED                     
SEQADV 1OZV ASN B  484  UNP  Q43088              ENGINEERED                     
SEQADV 1OZV LEU B  485  UNP  Q43088              ENGINEERED                     
SEQADV 1OZV TYR B  486  UNP  Q43088              ENGINEERED                     
SEQADV 1OZV PHE B  487  UNP  Q43088              ENGINEERED                     
SEQADV 1OZV GLN B  488  UNP  Q43088              ENGINEERED                     
SEQADV 1OZV MET C   45  UNP  Q43088              INITIATING MET                 
SEQADV 1OZV GLU C  483  UNP  Q43088              ENGINEERED                     
SEQADV 1OZV ASN C  484  UNP  Q43088              ENGINEERED                     
SEQADV 1OZV LEU C  485  UNP  Q43088              ENGINEERED                     
SEQADV 1OZV TYR C  486  UNP  Q43088              ENGINEERED                     
SEQADV 1OZV PHE C  487  UNP  Q43088              ENGINEERED                     
SEQADV 1OZV GLN C  488  UNP  Q43088              ENGINEERED                     
SEQRES   1 A  444  MET THR GLU PRO SER LEU SER PRO ALA VAL GLN THR PHE          
SEQRES   2 A  444  TRP LYS TRP LEU GLN GLU GLU GLY VAL ILE THR ALA LYS          
SEQRES   3 A  444  THR PRO VAL LYS ALA SER VAL VAL THR GLU GLY LEU GLY          
SEQRES   4 A  444  LEU VAL ALA LEU LYS ASP ILE SER ARG ASN ASP VAL ILE          
SEQRES   5 A  444  LEU GLN VAL PRO LYS ARG LEU TRP ILE ASN PRO ASP ALA          
SEQRES   6 A  444  VAL ALA ALA SER GLU ILE GLY ARG VAL CYS SER GLU LEU          
SEQRES   7 A  444  LYS PRO TRP LEU SER VAL ILE LEU PHE LEU ILE ARG GLU          
SEQRES   8 A  444  ARG SER ARG GLU ASP SER VAL TRP LYS HIS TYR PHE GLY          
SEQRES   9 A  444  ILE LEU PRO GLN GLU THR ASP SER THR ILE TYR TRP SER          
SEQRES  10 A  444  GLU GLU GLU LEU GLN GLU LEU GLN GLY SER GLN LEU LEU          
SEQRES  11 A  444  LYS THR THR VAL SER VAL LYS GLU TYR VAL LYS ASN GLU          
SEQRES  12 A  444  CYS LEU LYS LEU GLU GLN GLU ILE ILE LEU PRO ASN LYS          
SEQRES  13 A  444  ARG LEU PHE PRO ASP PRO VAL THR LEU ASP ASP PHE PHE          
SEQRES  14 A  444  TRP ALA PHE GLY ILE LEU ARG SER ARG ALA PHE SER ARG          
SEQRES  15 A  444  LEU ARG ASN GLU ASN LEU VAL VAL VAL PRO MET ALA ASP          
SEQRES  16 A  444  LEU ILE ASN HIS SER ALA GLY VAL THR THR GLU ASP HIS          
SEQRES  17 A  444  ALA TYR GLU VAL LYS GLY ALA ALA GLY LEU PHE SER TRP          
SEQRES  18 A  444  ASP TYR LEU PHE SER LEU LYS SER PRO LEU SER VAL LYS          
SEQRES  19 A  444  ALA GLY GLU GLN VAL TYR ILE GLN TYR ASP LEU ASN LYS          
SEQRES  20 A  444  SER ASN ALA GLU LEU ALA LEU ASP TYR GLY PHE ILE GLU          
SEQRES  21 A  444  PRO ASN GLU ASN ARG HIS ALA TYR THR LEU THR LEU GLU          
SEQRES  22 A  444  ILE SER GLU SER ASP PRO PHE PHE ASP ASP LYS LEU ASP          
SEQRES  23 A  444  VAL ALA GLU SER ASN GLY PHE ALA GLN THR ALA TYR PHE          
SEQRES  24 A  444  ASP ILE PHE TYR ASN ARG THR LEU PRO PRO GLY LEU LEU          
SEQRES  25 A  444  PRO TYR LEU ARG LEU VAL ALA LEU GLY GLY THR ASP ALA          
SEQRES  26 A  444  PHE LEU LEU GLU SER LEU PHE ARG ASP THR ILE TRP GLY          
SEQRES  27 A  444  HIS LEU GLU LEU SER VAL SER ARG ASP ASN GLU GLU LEU          
SEQRES  28 A  444  LEU CYS LYS ALA VAL ARG GLU ALA CYS LYS SER ALA LEU          
SEQRES  29 A  444  ALA GLY TYR HIS THR THR ILE GLU GLN ASP ARG GLU LEU          
SEQRES  30 A  444  LYS GLU GLY ASN LEU ASP SER ARG LEU ALA ILE ALA VAL          
SEQRES  31 A  444  GLY ILE ARG GLU GLY GLU LYS MET VAL LEU GLN GLN ILE          
SEQRES  32 A  444  ASP GLY ILE PHE GLU GLN LYS GLU LEU GLU LEU ASP GLN          
SEQRES  33 A  444  LEU GLU TYR TYR GLN GLU ARG ARG LEU LYS ASP LEU GLY          
SEQRES  34 A  444  LEU CYS GLY GLU ASN GLY ASP ILE LEU GLU ASN LEU TYR          
SEQRES  35 A  444  PHE GLN                                                      
SEQRES   1 B  444  MET THR GLU PRO SER LEU SER PRO ALA VAL GLN THR PHE          
SEQRES   2 B  444  TRP LYS TRP LEU GLN GLU GLU GLY VAL ILE THR ALA LYS          
SEQRES   3 B  444  THR PRO VAL LYS ALA SER VAL VAL THR GLU GLY LEU GLY          
SEQRES   4 B  444  LEU VAL ALA LEU LYS ASP ILE SER ARG ASN ASP VAL ILE          
SEQRES   5 B  444  LEU GLN VAL PRO LYS ARG LEU TRP ILE ASN PRO ASP ALA          
SEQRES   6 B  444  VAL ALA ALA SER GLU ILE GLY ARG VAL CYS SER GLU LEU          
SEQRES   7 B  444  LYS PRO TRP LEU SER VAL ILE LEU PHE LEU ILE ARG GLU          
SEQRES   8 B  444  ARG SER ARG GLU ASP SER VAL TRP LYS HIS TYR PHE GLY          
SEQRES   9 B  444  ILE LEU PRO GLN GLU THR ASP SER THR ILE TYR TRP SER          
SEQRES  10 B  444  GLU GLU GLU LEU GLN GLU LEU GLN GLY SER GLN LEU LEU          
SEQRES  11 B  444  LYS THR THR VAL SER VAL LYS GLU TYR VAL LYS ASN GLU          
SEQRES  12 B  444  CYS LEU LYS LEU GLU GLN GLU ILE ILE LEU PRO ASN LYS          
SEQRES  13 B  444  ARG LEU PHE PRO ASP PRO VAL THR LEU ASP ASP PHE PHE          
SEQRES  14 B  444  TRP ALA PHE GLY ILE LEU ARG SER ARG ALA PHE SER ARG          
SEQRES  15 B  444  LEU ARG ASN GLU ASN LEU VAL VAL VAL PRO MET ALA ASP          
SEQRES  16 B  444  LEU ILE ASN HIS SER ALA GLY VAL THR THR GLU ASP HIS          
SEQRES  17 B  444  ALA TYR GLU VAL LYS GLY ALA ALA GLY LEU PHE SER TRP          
SEQRES  18 B  444  ASP TYR LEU PHE SER LEU LYS SER PRO LEU SER VAL LYS          
SEQRES  19 B  444  ALA GLY GLU GLN VAL TYR ILE GLN TYR ASP LEU ASN LYS          
SEQRES  20 B  444  SER ASN ALA GLU LEU ALA LEU ASP TYR GLY PHE ILE GLU          
SEQRES  21 B  444  PRO ASN GLU ASN ARG HIS ALA TYR THR LEU THR LEU GLU          
SEQRES  22 B  444  ILE SER GLU SER ASP PRO PHE PHE ASP ASP LYS LEU ASP          
SEQRES  23 B  444  VAL ALA GLU SER ASN GLY PHE ALA GLN THR ALA TYR PHE          
SEQRES  24 B  444  ASP ILE PHE TYR ASN ARG THR LEU PRO PRO GLY LEU LEU          
SEQRES  25 B  444  PRO TYR LEU ARG LEU VAL ALA LEU GLY GLY THR ASP ALA          
SEQRES  26 B  444  PHE LEU LEU GLU SER LEU PHE ARG ASP THR ILE TRP GLY          
SEQRES  27 B  444  HIS LEU GLU LEU SER VAL SER ARG ASP ASN GLU GLU LEU          
SEQRES  28 B  444  LEU CYS LYS ALA VAL ARG GLU ALA CYS LYS SER ALA LEU          
SEQRES  29 B  444  ALA GLY TYR HIS THR THR ILE GLU GLN ASP ARG GLU LEU          
SEQRES  30 B  444  LYS GLU GLY ASN LEU ASP SER ARG LEU ALA ILE ALA VAL          
SEQRES  31 B  444  GLY ILE ARG GLU GLY GLU LYS MET VAL LEU GLN GLN ILE          
SEQRES  32 B  444  ASP GLY ILE PHE GLU GLN LYS GLU LEU GLU LEU ASP GLN          
SEQRES  33 B  444  LEU GLU TYR TYR GLN GLU ARG ARG LEU LYS ASP LEU GLY          
SEQRES  34 B  444  LEU CYS GLY GLU ASN GLY ASP ILE LEU GLU ASN LEU TYR          
SEQRES  35 B  444  PHE GLN                                                      
SEQRES   1 C  444  MET THR GLU PRO SER LEU SER PRO ALA VAL GLN THR PHE          
SEQRES   2 C  444  TRP LYS TRP LEU GLN GLU GLU GLY VAL ILE THR ALA LYS          
SEQRES   3 C  444  THR PRO VAL LYS ALA SER VAL VAL THR GLU GLY LEU GLY          
SEQRES   4 C  444  LEU VAL ALA LEU LYS ASP ILE SER ARG ASN ASP VAL ILE          
SEQRES   5 C  444  LEU GLN VAL PRO LYS ARG LEU TRP ILE ASN PRO ASP ALA          
SEQRES   6 C  444  VAL ALA ALA SER GLU ILE GLY ARG VAL CYS SER GLU LEU          
SEQRES   7 C  444  LYS PRO TRP LEU SER VAL ILE LEU PHE LEU ILE ARG GLU          
SEQRES   8 C  444  ARG SER ARG GLU ASP SER VAL TRP LYS HIS TYR PHE GLY          
SEQRES   9 C  444  ILE LEU PRO GLN GLU THR ASP SER THR ILE TYR TRP SER          
SEQRES  10 C  444  GLU GLU GLU LEU GLN GLU LEU GLN GLY SER GLN LEU LEU          
SEQRES  11 C  444  LYS THR THR VAL SER VAL LYS GLU TYR VAL LYS ASN GLU          
SEQRES  12 C  444  CYS LEU LYS LEU GLU GLN GLU ILE ILE LEU PRO ASN LYS          
SEQRES  13 C  444  ARG LEU PHE PRO ASP PRO VAL THR LEU ASP ASP PHE PHE          
SEQRES  14 C  444  TRP ALA PHE GLY ILE LEU ARG SER ARG ALA PHE SER ARG          
SEQRES  15 C  444  LEU ARG ASN GLU ASN LEU VAL VAL VAL PRO MET ALA ASP          
SEQRES  16 C  444  LEU ILE ASN HIS SER ALA GLY VAL THR THR GLU ASP HIS          
SEQRES  17 C  444  ALA TYR GLU VAL LYS GLY ALA ALA GLY LEU PHE SER TRP          
SEQRES  18 C  444  ASP TYR LEU PHE SER LEU LYS SER PRO LEU SER VAL LYS          
SEQRES  19 C  444  ALA GLY GLU GLN VAL TYR ILE GLN TYR ASP LEU ASN LYS          
SEQRES  20 C  444  SER ASN ALA GLU LEU ALA LEU ASP TYR GLY PHE ILE GLU          
SEQRES  21 C  444  PRO ASN GLU ASN ARG HIS ALA TYR THR LEU THR LEU GLU          
SEQRES  22 C  444  ILE SER GLU SER ASP PRO PHE PHE ASP ASP LYS LEU ASP          
SEQRES  23 C  444  VAL ALA GLU SER ASN GLY PHE ALA GLN THR ALA TYR PHE          
SEQRES  24 C  444  ASP ILE PHE TYR ASN ARG THR LEU PRO PRO GLY LEU LEU          
SEQRES  25 C  444  PRO TYR LEU ARG LEU VAL ALA LEU GLY GLY THR ASP ALA          
SEQRES  26 C  444  PHE LEU LEU GLU SER LEU PHE ARG ASP THR ILE TRP GLY          
SEQRES  27 C  444  HIS LEU GLU LEU SER VAL SER ARG ASP ASN GLU GLU LEU          
SEQRES  28 C  444  LEU CYS LYS ALA VAL ARG GLU ALA CYS LYS SER ALA LEU          
SEQRES  29 C  444  ALA GLY TYR HIS THR THR ILE GLU GLN ASP ARG GLU LEU          
SEQRES  30 C  444  LYS GLU GLY ASN LEU ASP SER ARG LEU ALA ILE ALA VAL          
SEQRES  31 C  444  GLY ILE ARG GLU GLY GLU LYS MET VAL LEU GLN GLN ILE          
SEQRES  32 C  444  ASP GLY ILE PHE GLU GLN LYS GLU LEU GLU LEU ASP GLN          
SEQRES  33 C  444  LEU GLU TYR TYR GLN GLU ARG ARG LEU LYS ASP LEU GLY          
SEQRES  34 C  444  LEU CYS GLY GLU ASN GLY ASP ILE LEU GLU ASN LEU TYR          
SEQRES  35 C  444  PHE GLN                                                      
HET    LYS  A 700      10                                                       
HET    LYS  A 800      10                                                       
HET    LYS  A 900      10                                                       
HET    SAH  A1000      26                                                       
HET    SAH  B1001      26                                                       
HET    SAH  C1002      26                                                       
HETNAM     LYS LYSINE                                                           
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   4  LYS    3(C6 H15 N2 O2 1+)                                           
FORMUL   5  SAH    3(C14 H20 N6 O5 S)                                           
FORMUL   8  HOH   *644(H2 O)                                                    
HELIX    1   1 SER A   51  GLU A   63  1                                  13    
HELIX    2   2 ARG A  102  TRP A  104  5                                   3    
HELIX    3   3 ASN A  106  ALA A  112  1                                   7    
HELIX    4   4 SER A  113  ARG A  117  5                                   5    
HELIX    5   5 LYS A  123  ARG A  136  1                                  14    
HELIX    6   6 TRP A  143  GLY A  148  1                                   6    
HELIX    7   7 SER A  161  GLU A  167  1                                   7    
HELIX    8   8 SER A  171  ILE A  195  1                                  25    
HELIX    9   9 THR A  208  ALA A  223  1                                  16    
HELIX   10  10 SER A  292  TYR A  300  1                                   9    
HELIX   11  11 ASN A  306  ARG A  309  5                                   4    
HELIX   12  12 PHE A  324  SER A  334  1                                  11    
HELIX   13  13 GLY A  354  LEU A  364  1                                  11    
HELIX   14  14 GLY A  365  ARG A  377  5                                  13    
HELIX   15  15 THR A  379  SER A  387  1                                   9    
HELIX   16  16 SER A  389  GLY A  410  1                                  22    
HELIX   17  17 THR A  414  LYS A  422  1                                   9    
HELIX   18  18 ASP A  427  GLU A  457  1                                  31    
HELIX   19  19 TYR A  463  LYS A  470  1                                   8    
HELIX   20  20 GLY A  479  PHE A  487  1                                   9    
HELIX   21  21 SER B   49  GLU B   64  1                                  16    
HELIX   22  22 ARG B  102  TRP B  104  5                                   3    
HELIX   23  23 ASN B  106  ALA B  112  1                                   7    
HELIX   24  24 SER B  113  ARG B  117  5                                   5    
HELIX   25  25 LYS B  123  ARG B  136  1                                  14    
HELIX   26  26 TRP B  143  GLY B  148  1                                   6    
HELIX   27  27 SER B  156  TRP B  160  5                                   5    
HELIX   28  28 SER B  161  GLU B  167  1                                   7    
HELIX   29  29 SER B  171  ILE B  195  1                                  25    
HELIX   30  30 THR B  208  ALA B  223  1                                  16    
HELIX   31  31 MET B  237  ILE B  241  5                                   5    
HELIX   32  32 LYS B  257  GLY B  261  5                                   5    
HELIX   33  33 PHE B  263  ASP B  266  5                                   4    
HELIX   34  34 SER B  292  TYR B  300  1                                   9    
HELIX   35  35 ASN B  306  ARG B  309  5                                   4    
HELIX   36  36 PHE B  324  ASN B  335  1                                  12    
HELIX   37  37 GLY B  354  LEU B  364  1                                  11    
HELIX   38  38 ASP B  368  GLU B  373  5                                   6    
HELIX   39  39 THR B  379  SER B  387  1                                   9    
HELIX   40  40 SER B  389  GLY B  410  1                                  22    
HELIX   41  41 THR B  414  GLU B  423  1                                  10    
HELIX   42  42 ASP B  427  GLU B  457  1                                  31    
HELIX   43  43 TYR B  463  LEU B  469  1                                   7    
HELIX   44  44 ASN B  478  PHE B  487  1                                  10    
HELIX   45  45 SER C   51  GLU C   64  1                                  14    
HELIX   46  46 ARG C  102  TRP C  104  5                                   3    
HELIX   47  47 ASN C  106  ALA C  112  1                                   7    
HELIX   48  48 SER C  113  ARG C  117  5                                   5    
HELIX   49  49 LYS C  123  ARG C  136  1                                  14    
HELIX   50  50 TRP C  143  GLY C  148  1                                   6    
HELIX   51  51 SER C  156  TRP C  160  5                                   5    
HELIX   52  52 SER C  161  GLU C  167  1                                   7    
HELIX   53  53 SER C  171  ILE C  195  1                                  25    
HELIX   54  54 THR C  208  ALA C  223  1                                  16    
HELIX   55  55 MET C  237  ILE C  241  5                                   5    
HELIX   56  56 PHE C  263  ASP C  266  5                                   4    
HELIX   57  57 SER C  292  TYR C  300  1                                   9    
HELIX   58  58 ASN C  306  ARG C  309  5                                   4    
HELIX   59  59 PHE C  324  SER C  334  1                                  11    
HELIX   60  60 GLY C  354  LEU C  364  1                                  11    
HELIX   61  61 LEU C  364  ALA C  369  1                                   6    
HELIX   62  62 PHE C  370  GLU C  373  5                                   4    
HELIX   63  63 THR C  379  SER C  387  1                                   9    
HELIX   64  64 SER C  389  GLY C  410  1                                  22    
HELIX   65  65 THR C  414  GLU C  423  1                                  10    
HELIX   66  66 ASP C  427  GLU C  457  1                                  31    
HELIX   67  67 TYR C  463  LEU C  469  1                                   7    
HELIX   68  68 ASN C  478  GLN C  488  1                                  11    
SHEET    1   A 2 VAL A  73  VAL A  78  0                                        
SHEET    2   A 2 GLY A  81  ALA A  86 -1  O  VAL A  85   N  LYS A  74           
SHEET    1   B 3 ASP A  94  PRO A 100  0                                        
SHEET    2   B 3 LEU A 268  SER A 273 -1  O  LEU A 271   N  LEU A  97           
SHEET    3   B 3 TYR A 254  VAL A 256 -1  N  GLU A 255   O  SER A 270           
SHEET    1   C 2 ASN A 242  HIS A 243  0                                        
SHEET    2   C 2 TYR A 284  ILE A 285  1  O  ILE A 285   N  ASN A 242           
SHEET    1   D 2 ALA A 311  GLU A 317  0                                        
SHEET    2   D 2 THR A 340  PHE A 346 -1  O  PHE A 343   N  LEU A 314           
SHEET    1   E 2 VAL B  73  VAL B  78  0                                        
SHEET    2   E 2 GLY B  81  ALA B  86 -1  O  GLY B  81   N  VAL B  78           
SHEET    1   F 3 VAL B  95  PRO B 100  0                                        
SHEET    2   F 3 LEU B 268  LYS B 272 -1  O  PHE B 269   N  VAL B  99           
SHEET    3   F 3 ALA B 253  VAL B 256 -1  N  TYR B 254   O  SER B 270           
SHEET    1   G 2 ASN B 242  HIS B 243  0                                        
SHEET    2   G 2 TYR B 284  ILE B 285  1  O  ILE B 285   N  ASN B 242           
SHEET    1   H 2 ALA B 311  GLU B 317  0                                        
SHEET    2   H 2 THR B 340  PHE B 346 -1  O  ALA B 341   N  LEU B 316           
SHEET    1   I 2 VAL C  73  VAL C  78  0                                        
SHEET    2   I 2 GLY C  81  ALA C  86 -1  O  VAL C  85   N  LYS C  74           
SHEET    1   J 3 VAL C  95  PRO C 100  0                                        
SHEET    2   J 3 LEU C 268  LYS C 272 -1  O  PHE C 269   N  VAL C  99           
SHEET    3   J 3 TYR C 254  LYS C 257 -1  N  GLU C 255   O  SER C 270           
SHEET    1   K 2 ASN C 242  HIS C 243  0                                        
SHEET    2   K 2 TYR C 284  ILE C 285  1  O  ILE C 285   N  ASN C 242           
SHEET    1   L 2 ALA C 311  GLU C 317  0                                        
SHEET    2   L 2 THR C 340  PHE C 346 -1  O  ALA C 341   N  LEU C 316           
SITE     1 AC1 11 SER A 221  ARG A 222  ALA A 223  SER A 225                    
SITE     2 AC1 11 ARG A 226  ASP A 239  ILE A 241  TYR A 254                    
SITE     3 AC1 11 TYR A 287  TYR A 300  SAH A1000                               
SITE     1 AC2  7 HOH A1002  HOH A1023  SER B 221  ARG B 222                    
SITE     2 AC2  7 PHE B 224  SER B 225  TYR B 287                               
SITE     1 AC3 12 HOH A1003  HOH A1036  SER C 221  ARG C 222                    
SITE     2 AC3 12 PHE C 224  SER C 225  ARG C 226  ASP C 239                    
SITE     3 AC3 12 TYR C 254  TYR C 287  TYR C 300  SAH C1002                    
SITE     1 AC4 18 GLU A  80  GLY A  81  LEU A  82  PRO A 151                    
SITE     2 AC4 18 SER A 221  ARG A 222  ASP A 239  ASN A 242                    
SITE     3 AC4 18 HIS A 243  TYR A 287  TYR A 300  LYS A 700                    
SITE     4 AC4 18 HOH A1006  HOH A1035  HOH A1067  HOH A1071                    
SITE     5 AC4 18 HOH A1099  HOH A1105                                          
SITE     1 AC5 17 GLU B  80  GLY B  81  LEU B  82  SER B 221                    
SITE     2 AC5 17 ARG B 222  ASP B 239  ASN B 242  HIS B 243                    
SITE     3 AC5 17 TYR B 287  TYR B 300  PHE B 302  HOH B1006                    
SITE     4 AC5 17 HOH B1012  HOH B1013  HOH B1021  HOH B1176                    
SITE     5 AC5 17 PHE C 263                                                     
SITE     1 AC6 16 LYS A 900  GLU C  80  LEU C  82  SER C 221                    
SITE     2 AC6 16 ARG C 222  ASP C 239  LEU C 240  ILE C 241                    
SITE     3 AC6 16 ASN C 242  HIS C 243  TYR C 287  TYR C 300                    
SITE     4 AC6 16 GLY C 301  PHE C 302  HOH C1013  HOH C1039                    
CRYST1  131.960  156.900  267.550  90.00  90.00  90.00 I 2 2 2      24          
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      0.007578  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006373  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003738        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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