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Database: PDB
Entry: 2H2J
LinkDB: 2H2J
Original site: 2H2J 
HEADER    TRANSFERASE                             18-MAY-06   2H2J              
TITLE     STRUCTURE OF RUBISCO LSMT BOUND TO SINEFUNGIN AND MONOMETHYLLYSINE    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE-1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE LARGE      
COMPND   3 SUBUNIT N-METHYLTRANSFERASE;                                         
COMPND   4 CHAIN: A, B, C;                                                      
COMPND   5 FRAGMENT: RUBISCO LSMT (RESIDUES 49-482);                            
COMPND   6 SYNONYM: [RIBULOSE- BISPHOSPHATE CARBOXYLASE]-LYSINE N-              
COMPND   7 METHYLTRANSFERASE, RUBISCO METHYLTRANSFERASE, RUBISCO LSMT, RBCMT;   
COMPND   8 EC: 2.1.1.127;                                                       
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE   3 ORGANISM_COMMON: PEA;                                                
SOURCE   4 ORGANISM_TAXID: 3888;                                                
SOURCE   5 GENE: RBCMT;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST14                                   
KEYWDS    SET DOMAIN, PROTEIN LYSINE METHYLTRANSFERASE, TRANSFERASE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.F.COUTURE,G.HAUK,R.C.TRIEVEL                                        
REVDAT   5   18-OCT-17 2H2J    1       REMARK                                   
REVDAT   4   13-JUL-11 2H2J    1       VERSN                                    
REVDAT   3   24-FEB-09 2H2J    1       VERSN                                    
REVDAT   2   25-JUL-06 2H2J    1       JRNL                                     
REVDAT   1   30-MAY-06 2H2J    0                                                
JRNL        AUTH   J.F.COUTURE,G.HAUK,M.J.THOMPSON,G.M.BLACKBURN,R.C.TRIEVEL    
JRNL        TITL   CATALYTIC ROLES FOR CARBON-OXYGEN HYDROGEN BONDING IN SET    
JRNL        TITL 2 DOMAIN LYSINE METHYLTRANSFERASES.                            
JRNL        REF    J.BIOL.CHEM.                  V. 281 19280 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16682405                                                     
JRNL        DOI    10.1074/JBC.M602257200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 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) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 472996.700                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 96595                          
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) : 0.253                           
REMARK   3   FREE R VALUE                     : 0.292                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4883                            
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) : 2.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.60                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 14872                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4370                       
REMARK   3   BIN FREE R VALUE                    : 0.4540                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 804                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.016                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10464                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 114                                     
REMARK   3   SOLVENT ATOMS            : 450                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -15.71000                                            
REMARK   3    B22 (A**2) : 20.86000                                             
REMARK   3    B33 (A**2) : -5.16000                                             
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) : 0.42                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.69                            
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) : 0.48                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.74                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.810                           
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) : 1.340 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.330 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.770 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.770 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 52.61                                                
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  : SFG.PAR                                        
REMARK   3  PARAMETER FILE  4  : MMK.PAR                                        
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : SFG.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : MMK.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2H2J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAY-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000037848.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-AUG-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 32-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686                             
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR                                
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 108311                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.47                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
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   (%): 73.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NACITRATE PH 6.8, 1.29-1.59 M     
REMARK 280  NAACETATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K          
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       66.18500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       78.25000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      133.79500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       66.18500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       78.25000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      133.79500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       66.18500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       78.25000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      133.79500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       66.18500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       78.25000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      133.79500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7                                     
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 300 REMARK: THERE ARE THREE MOLECULES OF LSMT IN THE ASYMMETRIC UNIT.    
REMARK 300 LSMT IS A MONOMER IN SOLUTION.                                       
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11520 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 59890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 7                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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     SER A    49                                                      
REMARK 465     ARG A   228                                                      
REMARK 465     ASN A   229                                                      
REMARK 465     GLU A   230                                                      
REMARK 465     VAL A   256                                                      
REMARK 465     LYS A   257                                                      
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     PHE A   487                                                      
REMARK 465     GLN A   488                                                      
REMARK 465     GLN B   488                                                      
REMARK 465     SER C    49                                                      
REMARK 465     GLN C   488                                                      
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 C 236   C   -  N   -  CA  ANGL. DEV. =  10.4 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       44.24    -74.41                                   
REMARK 500    GLU A  64       -5.90   -153.51                                   
REMARK 500    THR A  68     -105.03    -98.53                                   
REMARK 500    ILE A 105       65.50   -153.92                                   
REMARK 500    ILE A 195      -35.95   -131.61                                   
REMARK 500    LYS A 200        4.10    -60.49                                   
REMARK 500    SER A 225      -83.40    -74.24                                   
REMARK 500    LEU A 232       69.73   -109.05                                   
REMARK 500    PRO A 236      -28.73    -35.16                                   
REMARK 500    MET A 237      -60.98    -93.35                                   
REMARK 500    GLU A 250       96.47     44.05                                   
REMARK 500    ASP A 251       89.68    161.22                                   
REMARK 500    ASP A 288      121.45   -172.09                                   
REMARK 500    ASN A 306      105.61    -50.85                                   
REMARK 500    ASN A 348        3.51     59.19                                   
REMARK 500    LEU A 364      -84.77    -22.57                                   
REMARK 500    ARG A 377      -16.04    -48.31                                   
REMARK 500    SER A 387      147.42    128.23                                   
REMARK 500    ASP A 471       74.62   -102.87                                   
REMARK 500    LEU B  50      -73.24    -67.83                                   
REMARK 500    ASN B  93        5.79     92.86                                   
REMARK 500    ILE B 195      -45.95   -132.17                                   
REMARK 500    LYS B 200       -2.11    -58.90                                   
REMARK 500    SER B 225     -118.78   -116.24                                   
REMARK 500    ARG B 226       91.08     12.34                                   
REMARK 500    LEU B 227     -158.20   -161.97                                   
REMARK 500    PRO B 236      -61.88    -29.43                                   
REMARK 500    ASP B 239        7.89    -69.10                                   
REMARK 500    LYS B 257     -149.79    -98.73                                   
REMARK 500    ASP B 288      108.96    179.59                                   
REMARK 500    PHE B 325      -71.72    -41.85                                   
REMARK 500    ASN B 348       -0.62     60.16                                   
REMARK 500    LEU B 364      -88.87    -22.39                                   
REMARK 500    ARG B 377      -17.38    -48.46                                   
REMARK 500    SER B 387      150.70    115.52                                   
REMARK 500    VAL B 388      -71.35    -95.16                                   
REMARK 500    ASP B 471       40.26   -104.87                                   
REMARK 500    ASP B 480      -81.71    -64.81                                   
REMARK 500    GLU B 483       41.86    -92.59                                   
REMARK 500    TYR B 486      -79.63    -67.34                                   
REMARK 500    ASN C  93       -6.81     75.88                                   
REMARK 500    GLN C 169      129.54    -39.01                                   
REMARK 500    ILE C 195      -37.20   -134.66                                   
REMARK 500    ASN C 199       50.29    -97.01                                   
REMARK 500    LYS C 200       -5.26    -51.44                                   
REMARK 500    LEU C 232       72.66   -179.40                                   
REMARK 500    PRO C 236      -62.19    -28.63                                   
REMARK 500    THR C 249      -40.93   -135.85                                   
REMARK 500    ASP C 251       39.10    -71.26                                   
REMARK 500    HIS C 252      109.58     52.31                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      60 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SFG A 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SFG B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SFG C 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLZ A 900                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLZ B 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLZ C 902                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MLV   RELATED DB: PDB                                   
REMARK 900 THE SAME ENZYME IN COMPLEX WITH ADOHCY AND HEPES.                    
REMARK 900 RELATED ID: 1OZV   RELATED DB: PDB                                   
REMARK 900 THE SAME ENZYME IN COMPLEX WITH ADOHCY AND LYSINE.                   
REMARK 900 RELATED ID: 1P0Y   RELATED DB: PDB                                   
REMARK 900 THE SAME ENZYME IN COMPLEX WITH ADOHCY AND MONOMETHYLLYSINE.         
REMARK 999                                                                      
REMARK 999 THE ENGINEERED CONSTRUCT POSSESSES AN ENLYFQ SEQUENCE ON ITS C-      
REMARK 999 TERMINUS DUE TO A TEV PROTEASE CLEAVAGE SITE.                        
DBREF  2H2J A   49   482  UNP    Q43088   RBCMT_PEA       49    482             
DBREF  2H2J B   49   482  UNP    Q43088   RBCMT_PEA       49    482             
DBREF  2H2J C   49   482  UNP    Q43088   RBCMT_PEA       49    482             
SEQADV 2H2J GLU A  483  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2J ASN A  484  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2J LEU A  485  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2J TYR A  486  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2J PHE A  487  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2J GLN A  488  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2J GLU B  483  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2J ASN B  484  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2J LEU B  485  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2J TYR B  486  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2J PHE B  487  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2J GLN B  488  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2J GLU C  483  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2J ASN C  484  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2J LEU C  485  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2J TYR C  486  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2J PHE C  487  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2J GLN C  488  UNP  Q43088              CLONING ARTIFACT               
SEQRES   1 A  440  SER LEU SER PRO ALA VAL GLN THR PHE TRP LYS TRP LEU          
SEQRES   2 A  440  GLN GLU GLU GLY VAL ILE THR ALA LYS THR PRO VAL LYS          
SEQRES   3 A  440  ALA SER VAL VAL THR GLU GLY LEU GLY LEU VAL ALA LEU          
SEQRES   4 A  440  LYS ASP ILE SER ARG ASN ASP VAL ILE LEU GLN VAL PRO          
SEQRES   5 A  440  LYS ARG LEU TRP ILE ASN PRO ASP ALA VAL ALA ALA SER          
SEQRES   6 A  440  GLU ILE GLY ARG VAL CYS SER GLU LEU LYS PRO TRP LEU          
SEQRES   7 A  440  SER VAL ILE LEU PHE LEU ILE ARG GLU ARG SER ARG GLU          
SEQRES   8 A  440  ASP SER VAL TRP LYS HIS TYR PHE GLY ILE LEU PRO GLN          
SEQRES   9 A  440  GLU THR ASP SER THR ILE TYR TRP SER GLU GLU GLU LEU          
SEQRES  10 A  440  GLN GLU LEU GLN GLY SER GLN LEU LEU LYS THR THR VAL          
SEQRES  11 A  440  SER VAL LYS GLU TYR VAL LYS ASN GLU CYS LEU LYS LEU          
SEQRES  12 A  440  GLU GLN GLU ILE ILE LEU PRO ASN LYS ARG LEU PHE PRO          
SEQRES  13 A  440  ASP PRO VAL THR LEU ASP ASP PHE PHE TRP ALA PHE GLY          
SEQRES  14 A  440  ILE LEU ARG SER ARG ALA PHE SER ARG LEU ARG ASN GLU          
SEQRES  15 A  440  ASN LEU VAL VAL VAL PRO MET ALA ASP LEU ILE ASN HIS          
SEQRES  16 A  440  SER ALA GLY VAL THR THR GLU ASP HIS ALA TYR GLU VAL          
SEQRES  17 A  440  LYS GLY ALA ALA GLY LEU PHE SER TRP ASP TYR LEU PHE          
SEQRES  18 A  440  SER LEU LYS SER PRO LEU SER VAL LYS ALA GLY GLU GLN          
SEQRES  19 A  440  VAL TYR ILE GLN TYR ASP LEU ASN LYS SER ASN ALA GLU          
SEQRES  20 A  440  LEU ALA LEU ASP TYR GLY PHE ILE GLU PRO ASN GLU ASN          
SEQRES  21 A  440  ARG HIS ALA TYR THR LEU THR LEU GLU ILE SER GLU SER          
SEQRES  22 A  440  ASP PRO PHE PHE ASP ASP LYS LEU ASP VAL ALA GLU SER          
SEQRES  23 A  440  ASN GLY PHE ALA GLN THR ALA TYR PHE ASP ILE PHE TYR          
SEQRES  24 A  440  ASN ARG THR LEU PRO PRO GLY LEU LEU PRO TYR LEU ARG          
SEQRES  25 A  440  LEU VAL ALA LEU GLY GLY THR ASP ALA PHE LEU LEU GLU          
SEQRES  26 A  440  SER LEU PHE ARG ASP THR ILE TRP GLY HIS LEU GLU LEU          
SEQRES  27 A  440  SER VAL SER ARG ASP ASN GLU GLU LEU LEU CYS LYS ALA          
SEQRES  28 A  440  VAL ARG GLU ALA CYS LYS SER ALA LEU ALA GLY TYR HIS          
SEQRES  29 A  440  THR THR ILE GLU GLN ASP ARG GLU LEU LYS GLU GLY ASN          
SEQRES  30 A  440  LEU ASP SER ARG LEU ALA ILE ALA VAL GLY ILE ARG GLU          
SEQRES  31 A  440  GLY GLU LYS MET VAL LEU GLN GLN ILE ASP GLY ILE PHE          
SEQRES  32 A  440  GLU GLN LYS GLU LEU GLU LEU ASP GLN LEU GLU TYR TYR          
SEQRES  33 A  440  GLN GLU ARG ARG LEU LYS ASP LEU GLY LEU CYS GLY GLU          
SEQRES  34 A  440  ASN GLY ASP ILE LEU GLU ASN LEU TYR PHE GLN                  
SEQRES   1 B  440  SER LEU SER PRO ALA VAL GLN THR PHE TRP LYS TRP LEU          
SEQRES   2 B  440  GLN GLU GLU GLY VAL ILE THR ALA LYS THR PRO VAL LYS          
SEQRES   3 B  440  ALA SER VAL VAL THR GLU GLY LEU GLY LEU VAL ALA LEU          
SEQRES   4 B  440  LYS ASP ILE SER ARG ASN ASP VAL ILE LEU GLN VAL PRO          
SEQRES   5 B  440  LYS ARG LEU TRP ILE ASN PRO ASP ALA VAL ALA ALA SER          
SEQRES   6 B  440  GLU ILE GLY ARG VAL CYS SER GLU LEU LYS PRO TRP LEU          
SEQRES   7 B  440  SER VAL ILE LEU PHE LEU ILE ARG GLU ARG SER ARG GLU          
SEQRES   8 B  440  ASP SER VAL TRP LYS HIS TYR PHE GLY ILE LEU PRO GLN          
SEQRES   9 B  440  GLU THR ASP SER THR ILE TYR TRP SER GLU GLU GLU LEU          
SEQRES  10 B  440  GLN GLU LEU GLN GLY SER GLN LEU LEU LYS THR THR VAL          
SEQRES  11 B  440  SER VAL LYS GLU TYR VAL LYS ASN GLU CYS LEU LYS LEU          
SEQRES  12 B  440  GLU GLN GLU ILE ILE LEU PRO ASN LYS ARG LEU PHE PRO          
SEQRES  13 B  440  ASP PRO VAL THR LEU ASP ASP PHE PHE TRP ALA PHE GLY          
SEQRES  14 B  440  ILE LEU ARG SER ARG ALA PHE SER ARG LEU ARG ASN GLU          
SEQRES  15 B  440  ASN LEU VAL VAL VAL PRO MET ALA ASP LEU ILE ASN HIS          
SEQRES  16 B  440  SER ALA GLY VAL THR THR GLU ASP HIS ALA TYR GLU VAL          
SEQRES  17 B  440  LYS GLY ALA ALA GLY LEU PHE SER TRP ASP TYR LEU PHE          
SEQRES  18 B  440  SER LEU LYS SER PRO LEU SER VAL LYS ALA GLY GLU GLN          
SEQRES  19 B  440  VAL TYR ILE GLN TYR ASP LEU ASN LYS SER ASN ALA GLU          
SEQRES  20 B  440  LEU ALA LEU ASP TYR GLY PHE ILE GLU PRO ASN GLU ASN          
SEQRES  21 B  440  ARG HIS ALA TYR THR LEU THR LEU GLU ILE SER GLU SER          
SEQRES  22 B  440  ASP PRO PHE PHE ASP ASP LYS LEU ASP VAL ALA GLU SER          
SEQRES  23 B  440  ASN GLY PHE ALA GLN THR ALA TYR PHE ASP ILE PHE TYR          
SEQRES  24 B  440  ASN ARG THR LEU PRO PRO GLY LEU LEU PRO TYR LEU ARG          
SEQRES  25 B  440  LEU VAL ALA LEU GLY GLY THR ASP ALA PHE LEU LEU GLU          
SEQRES  26 B  440  SER LEU PHE ARG ASP THR ILE TRP GLY HIS LEU GLU LEU          
SEQRES  27 B  440  SER VAL SER ARG ASP ASN GLU GLU LEU LEU CYS LYS ALA          
SEQRES  28 B  440  VAL ARG GLU ALA CYS LYS SER ALA LEU ALA GLY TYR HIS          
SEQRES  29 B  440  THR THR ILE GLU GLN ASP ARG GLU LEU LYS GLU GLY ASN          
SEQRES  30 B  440  LEU ASP SER ARG LEU ALA ILE ALA VAL GLY ILE ARG GLU          
SEQRES  31 B  440  GLY GLU LYS MET VAL LEU GLN GLN ILE ASP GLY ILE PHE          
SEQRES  32 B  440  GLU GLN LYS GLU LEU GLU LEU ASP GLN LEU GLU TYR TYR          
SEQRES  33 B  440  GLN GLU ARG ARG LEU LYS ASP LEU GLY LEU CYS GLY GLU          
SEQRES  34 B  440  ASN GLY ASP ILE LEU GLU ASN LEU TYR PHE GLN                  
SEQRES   1 C  440  SER LEU SER PRO ALA VAL GLN THR PHE TRP LYS TRP LEU          
SEQRES   2 C  440  GLN GLU GLU GLY VAL ILE THR ALA LYS THR PRO VAL LYS          
SEQRES   3 C  440  ALA SER VAL VAL THR GLU GLY LEU GLY LEU VAL ALA LEU          
SEQRES   4 C  440  LYS ASP ILE SER ARG ASN ASP VAL ILE LEU GLN VAL PRO          
SEQRES   5 C  440  LYS ARG LEU TRP ILE ASN PRO ASP ALA VAL ALA ALA SER          
SEQRES   6 C  440  GLU ILE GLY ARG VAL CYS SER GLU LEU LYS PRO TRP LEU          
SEQRES   7 C  440  SER VAL ILE LEU PHE LEU ILE ARG GLU ARG SER ARG GLU          
SEQRES   8 C  440  ASP SER VAL TRP LYS HIS TYR PHE GLY ILE LEU PRO GLN          
SEQRES   9 C  440  GLU THR ASP SER THR ILE TYR TRP SER GLU GLU GLU LEU          
SEQRES  10 C  440  GLN GLU LEU GLN GLY SER GLN LEU LEU LYS THR THR VAL          
SEQRES  11 C  440  SER VAL LYS GLU TYR VAL LYS ASN GLU CYS LEU LYS LEU          
SEQRES  12 C  440  GLU GLN GLU ILE ILE LEU PRO ASN LYS ARG LEU PHE PRO          
SEQRES  13 C  440  ASP PRO VAL THR LEU ASP ASP PHE PHE TRP ALA PHE GLY          
SEQRES  14 C  440  ILE LEU ARG SER ARG ALA PHE SER ARG LEU ARG ASN GLU          
SEQRES  15 C  440  ASN LEU VAL VAL VAL PRO MET ALA ASP LEU ILE ASN HIS          
SEQRES  16 C  440  SER ALA GLY VAL THR THR GLU ASP HIS ALA TYR GLU VAL          
SEQRES  17 C  440  LYS GLY ALA ALA GLY LEU PHE SER TRP ASP TYR LEU PHE          
SEQRES  18 C  440  SER LEU LYS SER PRO LEU SER VAL LYS ALA GLY GLU GLN          
SEQRES  19 C  440  VAL TYR ILE GLN TYR ASP LEU ASN LYS SER ASN ALA GLU          
SEQRES  20 C  440  LEU ALA LEU ASP TYR GLY PHE ILE GLU PRO ASN GLU ASN          
SEQRES  21 C  440  ARG HIS ALA TYR THR LEU THR LEU GLU ILE SER GLU SER          
SEQRES  22 C  440  ASP PRO PHE PHE ASP ASP LYS LEU ASP VAL ALA GLU SER          
SEQRES  23 C  440  ASN GLY PHE ALA GLN THR ALA TYR PHE ASP ILE PHE TYR          
SEQRES  24 C  440  ASN ARG THR LEU PRO PRO GLY LEU LEU PRO TYR LEU ARG          
SEQRES  25 C  440  LEU VAL ALA LEU GLY GLY THR ASP ALA PHE LEU LEU GLU          
SEQRES  26 C  440  SER LEU PHE ARG ASP THR ILE TRP GLY HIS LEU GLU LEU          
SEQRES  27 C  440  SER VAL SER ARG ASP ASN GLU GLU LEU LEU CYS LYS ALA          
SEQRES  28 C  440  VAL ARG GLU ALA CYS LYS SER ALA LEU ALA GLY TYR HIS          
SEQRES  29 C  440  THR THR ILE GLU GLN ASP ARG GLU LEU LYS GLU GLY ASN          
SEQRES  30 C  440  LEU ASP SER ARG LEU ALA ILE ALA VAL GLY ILE ARG GLU          
SEQRES  31 C  440  GLY GLU LYS MET VAL LEU GLN GLN ILE ASP GLY ILE PHE          
SEQRES  32 C  440  GLU GLN LYS GLU LEU GLU LEU ASP GLN LEU GLU TYR TYR          
SEQRES  33 C  440  GLN GLU ARG ARG LEU LYS ASP LEU GLY LEU CYS GLY GLU          
SEQRES  34 C  440  ASN GLY ASP ILE LEU GLU ASN LEU TYR PHE GLN                  
HET    SFG  A 800      27                                                       
HET    MLZ  A 900      11                                                       
HET    SFG  B 801      27                                                       
HET    MLZ  B 901      11                                                       
HET    SFG  C 802      27                                                       
HET    MLZ  C 902      11                                                       
HETNAM     SFG SINEFUNGIN                                                       
HETNAM     MLZ N-METHYL-LYSINE                                                  
HETSYN     SFG ADENOSYL-ORNITHINE                                               
FORMUL   4  SFG    3(C15 H23 N7 O5)                                             
FORMUL   5  MLZ    3(C7 H16 N2 O2)                                              
FORMUL  10  HOH   *450(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  138  1                                  16    
HELIX    6   6 TRP A  143  GLY A  148  1                                   6    
HELIX    7   7 SER A  156  TRP A  160  5                                   5    
HELIX    8   8 SER A  161  GLU A  167  1                                   7    
HELIX    9   9 SER A  171  ILE A  195  1                                  25    
HELIX   10  10 THR A  208  ALA A  223  1                                  16    
HELIX   11  11 MET A  237  ILE A  241  5                                   5    
HELIX   12  12 SER A  292  TYR A  300  1                                   9    
HELIX   13  13 ASN A  306  ARG A  309  5                                   4    
HELIX   14  14 PHE A  324  SER A  334  1                                  11    
HELIX   15  15 GLY A  354  LEU A  364  1                                  11    
HELIX   16  16 GLY A  365  ARG A  377  5                                  13    
HELIX   17  17 THR A  379  SER A  387  1                                   9    
HELIX   18  18 SER A  389  ALA A  409  1                                  21    
HELIX   19  19 THR A  414  LYS A  422  1                                   9    
HELIX   20  20 ASP A  427  GLU A  457  1                                  31    
HELIX   21  21 LEU A  458  GLN A  460  5                                   3    
HELIX   22  22 TYR A  463  LYS A  470  1                                   8    
HELIX   23  23 GLY A  479  ASN A  484  1                                   6    
HELIX   24  24 SER B   49  GLU B   64  1                                  16    
HELIX   25  25 ARG B  102  TRP B  104  5                                   3    
HELIX   26  26 ASN B  106  ALA B  112  1                                   7    
HELIX   27  27 LYS B  123  ARG B  138  1                                  16    
HELIX   28  28 TRP B  143  GLY B  148  1                                   6    
HELIX   29  29 SER B  156  TRP B  160  5                                   5    
HELIX   30  30 SER B  161  GLU B  167  1                                   7    
HELIX   31  31 SER B  171  ILE B  195  1                                  25    
HELIX   32  32 THR B  208  ALA B  223  1                                  16    
HELIX   33  33 MET B  237  ILE B  241  5                                   5    
HELIX   34  34 LYS B  257  GLY B  261  5                                   5    
HELIX   35  35 PHE B  263  ASP B  266  5                                   4    
HELIX   36  36 SER B  292  TYR B  300  1                                   9    
HELIX   37  37 ASN B  306  ARG B  309  5                                   4    
HELIX   38  38 PHE B  324  SER B  334  1                                  11    
HELIX   39  39 GLY B  354  LEU B  364  1                                  11    
HELIX   40  40 GLY B  366  GLU B  373  5                                   8    
HELIX   41  41 THR B  379  SER B  387  1                                   9    
HELIX   42  42 SER B  389  ALA B  409  1                                  21    
HELIX   43  43 THR B  414  GLY B  424  1                                  11    
HELIX   44  44 ASP B  427  GLU B  457  1                                  31    
HELIX   45  45 TYR B  463  LEU B  469  1                                   7    
HELIX   46  46 ASN B  478  GLU B  483  1                                   6    
HELIX   47  47 SER C   51  GLU C   64  1                                  14    
HELIX   48  48 ARG C  102  TRP C  104  5                                   3    
HELIX   49  49 ASN C  106  ALA C  112  1                                   7    
HELIX   50  50 SER C  113  ARG C  117  5                                   5    
HELIX   51  51 LYS C  123  ARG C  138  1                                  16    
HELIX   52  52 TRP C  143  GLY C  148  1                                   6    
HELIX   53  53 SER C  156  TRP C  160  5                                   5    
HELIX   54  54 SER C  161  GLU C  167  1                                   7    
HELIX   55  55 SER C  171  GLN C  193  1                                  23    
HELIX   56  56 THR C  208  ALA C  223  1                                  16    
HELIX   57  57 MET C  237  ILE C  241  5                                   5    
HELIX   58  58 PHE C  263  ASP C  266  5                                   4    
HELIX   59  59 SER C  292  TYR C  300  1                                   9    
HELIX   60  60 ASN C  306  ARG C  309  5                                   4    
HELIX   61  61 PHE C  324  SER C  334  1                                  11    
HELIX   62  62 GLY C  354  LEU C  364  1                                  11    
HELIX   63  63 ASP C  368  GLU C  373  5                                   6    
HELIX   64  64 THR C  379  SER C  387  1                                   9    
HELIX   65  65 SER C  389  ALA C  409  1                                  21    
HELIX   66  66 THR C  414  GLU C  423  1                                  10    
HELIX   67  67 ASP C  427  GLU C  457  1                                  31    
HELIX   68  68 TYR C  463  LEU C  469  1                                   7    
HELIX   69  69 GLY C  479  ASN C  484  1                                   6    
SHEET    1   A 2 LYS A  74  VAL A  78  0                                        
SHEET    2   A 2 GLY A  81  VAL A  85 -1  O  VAL A  85   N  LYS A  74           
SHEET    1   B 2 VAL A  95  PRO A 100  0                                        
SHEET    2   B 2 LEU A 268  LYS A 272 -1  O  PHE A 269   N  VAL A  99           
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  LEU B 271   N  ILE B  96           
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  GLY C  81   N  VAL C  78           
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  ILE C 345   N  TYR C 312           
SITE     1 AC1 16 GLU A  80  GLY A  81  LEU A  82  PRO A 151                    
SITE     2 AC1 16 THR A 154  SER A 221  ARG A 222  ASP A 239                    
SITE     3 AC1 16 LEU A 240  ASN A 242  HIS A 243  TYR A 287                    
SITE     4 AC1 16 PHE A 302  MLZ A 900  HOH A 901  HOH A1012                    
SITE     1 AC2 16 GLU B  80  GLY B  81  LEU B  82  SER B 221                    
SITE     2 AC2 16 ARG B 222  ASP B 239  ASN B 242  HIS B 243                    
SITE     3 AC2 16 TYR B 287  PHE B 302  MLZ B 901  HOH B 903                    
SITE     4 AC2 16 HOH B 916  HOH B 918  HOH B 985  PHE C 263                    
SITE     1 AC3 14 GLU C  80  GLY C  81  LEU C  82  THR C 154                    
SITE     2 AC3 14 SER C 221  ARG C 222  ASP C 239  ASN C 242                    
SITE     3 AC3 14 HIS C 243  TYR C 287  MLZ C 902  HOH C 913                    
SITE     4 AC3 14 HOH C 935  HOH C 961                                          
SITE     1 AC4  9 ARG A 222  ALA A 223  SER A 225  ARG A 226                    
SITE     2 AC4  9 ALA A 238  TYR A 287  TYR A 300  SFG A 800                    
SITE     3 AC4  9 HOH A 955                                                     
SITE     1 AC5  9 ARG B 222  PHE B 224  SER B 225  ASP B 239                    
SITE     2 AC5  9 ILE B 241  HIS B 252  TYR B 287  SFG B 801                    
SITE     3 AC5  9 HOH B 913                                                     
SITE     1 AC6 12 ARG C 222  SER C 225  ARG C 226  ASP C 239                    
SITE     2 AC6 12 ILE C 241  TYR C 254  TYR C 287  TYR C 300                    
SITE     3 AC6 12 SFG C 802  HOH C 915  HOH C 918  HOH C 975                    
CRYST1  132.370  156.500  267.590  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      0.007555  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006390  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003737        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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