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Database: PDB
Entry: 2QRV
LinkDB: 2QRV
Original site: 2QRV 
HEADER    TRANSFERASE/TRANSFERASE REGULATOR       29-JUL-07   2QRV              
TITLE     STRUCTURE OF DNMT3A-DNMT3L C-TERMINAL DOMAIN COMPLEX                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 3A;                     
COMPND   3 CHAIN: A, D, E, H;                                                   
COMPND   4 FRAGMENT: RESIDUES 623 TO 908;                                       
COMPND   5 SYNONYM: DNMT3A, DNA METHYLTRANSFERASE HSAIIIA, DNA MTASE            
COMPND   6 HSAIIIA, M.HSAIIIA;                                                  
COMPND   7 EC: 2.1.1.37;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 3-LIKE;                 
COMPND  11 CHAIN: B, C, F, G;                                                   
COMPND  12 FRAGMENT: RESIDUES 160 TO 386;                                       
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DNMT3A;                                                        
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_PLASMID: PXC528;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: DNMT3L;                                                        
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PXC510                                    
KEYWDS    DNA METHYLTRANSFERASE 3A (DNMT3A) AND ITS REGULATORY FACTOR,          
KEYWDS   2 DNA METHYLTRANSFERASE 3-LIKE PROTEIN (DNMT3L), NUCLEUS, S-           
KEYWDS   3 ADENOSYL-L-METHIONINE, TRANSFERASE/TRANSFERASE REGULATOR             
KEYWDS   4 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.JIA,X.CHENG                                                         
REVDAT   2   24-FEB-09 2QRV    1       VERSN                                    
REVDAT   1   04-DEC-07 2QRV    0                                                
JRNL        AUTH   D.JIA,R.Z.JURKOWSKA,X.ZHANG,A.JELTSCH,X.CHENG                
JRNL        TITL   STRUCTURE OF DNMT3A BOUND TO DNMT3L SUGGESTS A               
JRNL        TITL 2 MODEL FOR DE NOVO DNA METHYLATION.                           
JRNL        REF    NATURE                        V. 449   248 2007              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   17713477                                                     
JRNL        DOI    10.1038/NATURE06146                                          
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.89 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) : 2.89                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 332407.340                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 81.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 54424                          
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) : 0.259                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2756                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.89                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.99                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 38.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2410                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4670                       
REMARK   3   BIN FREE R VALUE                    : 0.4600                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 121                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.042                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14557                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 104                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 85.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 101.30                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 9.92000                                              
REMARK   3    B22 (A**2) : 9.92000                                              
REMARK   3    B33 (A**2) : -19.84000                                            
REMARK   3    B12 (A**2) : 24.85000                                             
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) : 0.49                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.58                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 40.00                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.55                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.64                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.04                            
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) : 4.840 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 7.650 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 6.400 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 9.070 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.28                                                 
REMARK   3   BSOL        : 36.80                                                
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  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : SAH.PAR                                        
REMARK   3  PARAMETER FILE  5  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA_REP.TOP                                
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : SAH.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE NON-CRYSTALLOGRAPHIC SYMMETRY         
REMARK   3  WAS USED AS RESTRAINS IN THE CNS REFINEMENT, AND WAS RELEASED       
REMARK   3  FOR THE SIDE CHAINS AT THE LATER CYCLES TO ACCOUNT FOR              
REMARK   3  DIFFERENT INTERACTION ENVIRONMENTS OF CRYSTAL PACKING WITH          
REMARK   3  EACH MOLECULE. THE GROUP B-FACTOR FOR EACH RESIDUE WAS REFINED      
REMARK   3  AT THE EARLIER STAGE OF REFINEMENT AND THE INDIVIDUAL B-FACTOR      
REMARK   3  FOR EACH ATOM WAS REFINED AT THE LATER CYCLES.                      
REMARK   4                                                                      
REMARK   4 2QRV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB043976.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-APR-06; NULL                    
REMARK 200  TEMPERATURE           (KELVIN) : 173.0; 173.0                       
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; NULL                            
REMARK 200  RADIATION SOURCE               : APS; NULL                          
REMARK 200  BEAMLINE                       : 22-ID; NULL                        
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0, 0.9792, 0.9785,0.9719;        
REMARK 200                                   NULL                               
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; NULL                          
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD; NULL         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 65264                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.890                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.99                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: 2PV0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THERE ARE TWO TETRAMER COMPLEXES PER ASYMMETRIC UNIT.        
REMARK 200  TETRAMER FORMED BY CHAINS A,B,C,D IS MORE STABLE THAN THE           
REMARK 200  TETRAMER FORMED BY CHAINS E,F,G,H. WITHIN EACH TETRAMER, THE        
REMARK 200  DNMT3L MOLECULES HAVE HIGHER B-FACTOR THAN THAT OF DNMT3A,          
REMARK 200  INDICATING DNMT3L MOLECULES - LOCATED IN THE OUTER SURFACES OF      
REMARK 200  TETRAMER - ARE MORE MOBILE.                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE FINAL PROTEIN SOLUTION               
REMARK 280  CONTAINED ~100 TO 133 MICRO M COMPLEX IN 20 MILLI M TRIS/HCL,       
REMARK 280  PH 8.0, 100 MILLI M NACL, 5 % GLYCEROL, AND 0.1 %                   
REMARK 280  MERCAPTOETHANOL. CRYSTALS WERE OBTAINED WITH THE MOTHER LIQUOR      
REMARK 280  CONTAINING 2~5 % PEG 3000, 100 MM TRIS/HCL, PH 8.0, 5 %             
REMARK 280  GLYCEROL AT 16C, VAPOR DIFFUSION, HANGING DROP                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      200.94050            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000      116.01305            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       16.56300            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000      200.94050            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000      116.01305            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       16.56300            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000      200.94050            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000      116.01305            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       16.56300            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      232.02610            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       33.12600            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000      232.02610            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       33.12600            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000      232.02610            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       33.12600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 WERE TWO TETRAMER COMPLEXES PER CRYSTALLOGRAPHIC       
REMARK 300 ASYMMETRIC UNIT. EACH TETRAMER CONTAINS TWO PAIRS OF DNMT3A-3L       
REMARK 300 HETERO-DIMERS (3L-3A-3A-3L) WITH TWO 3L-3A INTERFACES AND ONE 3A     
REMARK 300 -3A INTERFACE.                                                       
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
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   614                                                      
REMARK 465     GLY A   615                                                      
REMARK 465     HIS A   616                                                      
REMARK 465     HIS A   617                                                      
REMARK 465     HIS A   618                                                      
REMARK 465     HIS A   619                                                      
REMARK 465     HIS A   620                                                      
REMARK 465     HIS A   621                                                      
REMARK 465     MET A   622                                                      
REMARK 465     THR A   828                                                      
REMARK 465     ILE A   829                                                      
REMARK 465     THR A   830                                                      
REMARK 465     THR A   831                                                      
REMARK 465     ARG A   832                                                      
REMARK 465     SER A   833                                                      
REMARK 465     ASN A   834                                                      
REMARK 465     SER A   835                                                      
REMARK 465     ILE A   836                                                      
REMARK 465     LYS A   837                                                      
REMARK 465     GLN A   838                                                      
REMARK 465     GLY A   839                                                      
REMARK 465     LYS A   840                                                      
REMARK 465     ASP A   841                                                      
REMARK 465     GLY B   157                                                      
REMARK 465     SER B   158                                                      
REMARK 465     MET B   159                                                      
REMARK 465     TRP B   160                                                      
REMARK 465     ARG B   161                                                      
REMARK 465     SER B   162                                                      
REMARK 465     GLN B   163                                                      
REMARK 465     LEU B   164                                                      
REMARK 465     LYS B   165                                                      
REMARK 465     ALA B   166                                                      
REMARK 465     PHE B   167                                                      
REMARK 465     TYR B   168                                                      
REMARK 465     ASP B   169                                                      
REMARK 465     ARG B   170                                                      
REMARK 465     GLU B   171                                                      
REMARK 465     SER B   172                                                      
REMARK 465     GLU B   173                                                      
REMARK 465     ASN B   174                                                      
REMARK 465     PRO B   175                                                      
REMARK 465     LEU B   176                                                      
REMARK 465     GLU B   177                                                      
REMARK 465     SER B   211                                                      
REMARK 465     GLY B   212                                                      
REMARK 465     SER B   213                                                      
REMARK 465     ASP B   214                                                      
REMARK 465     PRO B   215                                                      
REMARK 465     LEU B   317                                                      
REMARK 465     GLN B   318                                                      
REMARK 465     ASN B   319                                                      
REMARK 465     ALA B   320                                                      
REMARK 465     LYS B   354                                                      
REMARK 465     LEU B   355                                                      
REMARK 465     ALA B   356                                                      
REMARK 465     ALA B   357                                                      
REMARK 465     LYS B   358                                                      
REMARK 465     TRP B   359                                                      
REMARK 465     PRO B   360                                                      
REMARK 465     THR B   380                                                      
REMARK 465     GLU B   381                                                      
REMARK 465     LEU B   382                                                      
REMARK 465     THR B   383                                                      
REMARK 465     SER B   384                                                      
REMARK 465     SER B   385                                                      
REMARK 465     LEU B   386                                                      
REMARK 465     GLY C   157                                                      
REMARK 465     SER C   158                                                      
REMARK 465     MET C   159                                                      
REMARK 465     TRP C   160                                                      
REMARK 465     ARG C   161                                                      
REMARK 465     SER C   162                                                      
REMARK 465     GLN C   163                                                      
REMARK 465     LEU C   164                                                      
REMARK 465     LYS C   165                                                      
REMARK 465     ALA C   166                                                      
REMARK 465     PHE C   167                                                      
REMARK 465     TYR C   168                                                      
REMARK 465     ASP C   169                                                      
REMARK 465     ARG C   170                                                      
REMARK 465     GLU C   171                                                      
REMARK 465     SER C   172                                                      
REMARK 465     GLU C   173                                                      
REMARK 465     ASN C   174                                                      
REMARK 465     PRO C   175                                                      
REMARK 465     LEU C   176                                                      
REMARK 465     GLU C   177                                                      
REMARK 465     SER C   211                                                      
REMARK 465     GLY C   212                                                      
REMARK 465     SER C   213                                                      
REMARK 465     ASP C   214                                                      
REMARK 465     PRO C   215                                                      
REMARK 465     LEU C   317                                                      
REMARK 465     GLN C   318                                                      
REMARK 465     ASN C   319                                                      
REMARK 465     ALA C   320                                                      
REMARK 465     LYS C   354                                                      
REMARK 465     LEU C   355                                                      
REMARK 465     ALA C   356                                                      
REMARK 465     ALA C   357                                                      
REMARK 465     LYS C   358                                                      
REMARK 465     TRP C   359                                                      
REMARK 465     PRO C   360                                                      
REMARK 465     THR C   380                                                      
REMARK 465     GLU C   381                                                      
REMARK 465     LEU C   382                                                      
REMARK 465     THR C   383                                                      
REMARK 465     SER C   384                                                      
REMARK 465     SER C   385                                                      
REMARK 465     LEU C   386                                                      
REMARK 465     MET D   614                                                      
REMARK 465     GLY D   615                                                      
REMARK 465     HIS D   616                                                      
REMARK 465     HIS D   617                                                      
REMARK 465     HIS D   618                                                      
REMARK 465     HIS D   619                                                      
REMARK 465     HIS D   620                                                      
REMARK 465     HIS D   621                                                      
REMARK 465     MET D   622                                                      
REMARK 465     PRO D   623                                                      
REMARK 465     ALA D   624                                                      
REMARK 465     GLU D   625                                                      
REMARK 465     THR D   828                                                      
REMARK 465     ILE D   829                                                      
REMARK 465     THR D   830                                                      
REMARK 465     THR D   831                                                      
REMARK 465     ARG D   832                                                      
REMARK 465     SER D   833                                                      
REMARK 465     ASN D   834                                                      
REMARK 465     SER D   835                                                      
REMARK 465     ILE D   836                                                      
REMARK 465     LYS D   837                                                      
REMARK 465     GLN D   838                                                      
REMARK 465     GLY D   839                                                      
REMARK 465     LYS D   840                                                      
REMARK 465     ASP D   841                                                      
REMARK 465     GLN D   842                                                      
REMARK 465     HIS D   843                                                      
REMARK 465     MET E   614                                                      
REMARK 465     GLY E   615                                                      
REMARK 465     HIS E   616                                                      
REMARK 465     HIS E   617                                                      
REMARK 465     HIS E   618                                                      
REMARK 465     HIS E   619                                                      
REMARK 465     HIS E   620                                                      
REMARK 465     HIS E   621                                                      
REMARK 465     MET E   622                                                      
REMARK 465     THR E   828                                                      
REMARK 465     ILE E   829                                                      
REMARK 465     THR E   830                                                      
REMARK 465     THR E   831                                                      
REMARK 465     ARG E   832                                                      
REMARK 465     SER E   833                                                      
REMARK 465     ASN E   834                                                      
REMARK 465     SER E   835                                                      
REMARK 465     ILE E   836                                                      
REMARK 465     LYS E   837                                                      
REMARK 465     GLN E   838                                                      
REMARK 465     GLY E   839                                                      
REMARK 465     LYS E   840                                                      
REMARK 465     ASP E   841                                                      
REMARK 465     GLN E   842                                                      
REMARK 465     HIS E   843                                                      
REMARK 465     GLY F   157                                                      
REMARK 465     SER F   158                                                      
REMARK 465     MET F   159                                                      
REMARK 465     TRP F   160                                                      
REMARK 465     ARG F   161                                                      
REMARK 465     SER F   162                                                      
REMARK 465     GLN F   163                                                      
REMARK 465     LEU F   164                                                      
REMARK 465     LYS F   165                                                      
REMARK 465     ALA F   166                                                      
REMARK 465     PHE F   167                                                      
REMARK 465     TYR F   168                                                      
REMARK 465     ASP F   169                                                      
REMARK 465     ARG F   170                                                      
REMARK 465     GLU F   171                                                      
REMARK 465     SER F   172                                                      
REMARK 465     GLU F   173                                                      
REMARK 465     ASN F   174                                                      
REMARK 465     PRO F   175                                                      
REMARK 465     LEU F   176                                                      
REMARK 465     GLU F   177                                                      
REMARK 465     SER F   211                                                      
REMARK 465     GLY F   212                                                      
REMARK 465     SER F   213                                                      
REMARK 465     ASP F   214                                                      
REMARK 465     PRO F   215                                                      
REMARK 465     LEU F   317                                                      
REMARK 465     GLN F   318                                                      
REMARK 465     ASN F   319                                                      
REMARK 465     ALA F   320                                                      
REMARK 465     LYS F   354                                                      
REMARK 465     LEU F   355                                                      
REMARK 465     ALA F   356                                                      
REMARK 465     ALA F   357                                                      
REMARK 465     LYS F   358                                                      
REMARK 465     TRP F   359                                                      
REMARK 465     PRO F   360                                                      
REMARK 465     THR F   380                                                      
REMARK 465     GLU F   381                                                      
REMARK 465     LEU F   382                                                      
REMARK 465     THR F   383                                                      
REMARK 465     SER F   384                                                      
REMARK 465     SER F   385                                                      
REMARK 465     LEU F   386                                                      
REMARK 465     GLY G   157                                                      
REMARK 465     SER G   158                                                      
REMARK 465     MET G   159                                                      
REMARK 465     TRP G   160                                                      
REMARK 465     ARG G   161                                                      
REMARK 465     SER G   162                                                      
REMARK 465     GLN G   163                                                      
REMARK 465     LEU G   164                                                      
REMARK 465     LYS G   165                                                      
REMARK 465     ALA G   166                                                      
REMARK 465     PHE G   167                                                      
REMARK 465     TYR G   168                                                      
REMARK 465     ASP G   169                                                      
REMARK 465     ARG G   170                                                      
REMARK 465     GLU G   171                                                      
REMARK 465     SER G   172                                                      
REMARK 465     GLU G   173                                                      
REMARK 465     ASN G   174                                                      
REMARK 465     PRO G   175                                                      
REMARK 465     LEU G   176                                                      
REMARK 465     GLU G   177                                                      
REMARK 465     SER G   211                                                      
REMARK 465     GLY G   212                                                      
REMARK 465     SER G   213                                                      
REMARK 465     ASP G   214                                                      
REMARK 465     PRO G   215                                                      
REMARK 465     LEU G   317                                                      
REMARK 465     GLN G   318                                                      
REMARK 465     ASN G   319                                                      
REMARK 465     ALA G   320                                                      
REMARK 465     LYS G   354                                                      
REMARK 465     LEU G   355                                                      
REMARK 465     ALA G   356                                                      
REMARK 465     ALA G   357                                                      
REMARK 465     LYS G   358                                                      
REMARK 465     TRP G   359                                                      
REMARK 465     PRO G   360                                                      
REMARK 465     THR G   380                                                      
REMARK 465     GLU G   381                                                      
REMARK 465     LEU G   382                                                      
REMARK 465     THR G   383                                                      
REMARK 465     SER G   384                                                      
REMARK 465     SER G   385                                                      
REMARK 465     LEU G   386                                                      
REMARK 465     MET H   614                                                      
REMARK 465     GLY H   615                                                      
REMARK 465     HIS H   616                                                      
REMARK 465     HIS H   617                                                      
REMARK 465     HIS H   618                                                      
REMARK 465     HIS H   619                                                      
REMARK 465     HIS H   620                                                      
REMARK 465     HIS H   621                                                      
REMARK 465     MET H   622                                                      
REMARK 465     PRO H   623                                                      
REMARK 465     ALA H   624                                                      
REMARK 465     GLU H   625                                                      
REMARK 465     THR H   828                                                      
REMARK 465     ILE H   829                                                      
REMARK 465     THR H   830                                                      
REMARK 465     THR H   831                                                      
REMARK 465     ARG H   832                                                      
REMARK 465     SER H   833                                                      
REMARK 465     ASN H   834                                                      
REMARK 465     SER H   835                                                      
REMARK 465     ILE H   836                                                      
REMARK 465     LYS H   837                                                      
REMARK 465     GLN H   838                                                      
REMARK 465     GLY H   839                                                      
REMARK 465     LYS H   840                                                      
REMARK 465     ASP H   841                                                      
REMARK 465     GLN H   842                                                      
REMARK 465     HIS H   843                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 625    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 626    CG   CD   CE   NZ                                   
REMARK 470     LYS A 628    CG   CD   CE   NZ                                   
REMARK 470     LYS A 689    CG   CD   CE   NZ                                   
REMARK 470     ASN A 713    CG   OD1  ND2                                       
REMARK 470     LYS A 762    CG   CD   CE   NZ                                   
REMARK 470     ARG A 767    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 779    CG   CD   CE   NZ                                   
REMARK 470     GLU A 813    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 820    CG1  CG2  CD1                                       
REMARK 470     ARG A 827    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 842    CG   CD   OE1  NE2                                  
REMARK 470     PHE A 847    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL A 908    CG1  CG2                                            
REMARK 470     HIS B 250    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR B 251    OG1  CG2                                            
REMARK 470     CYS B 252    SG                                                  
REMARK 470     ASP B 253    CG   OD1  OD2                                       
REMARK 470     ARG B 254    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 278    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     HIS C 250    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR C 251    OG1  CG2                                            
REMARK 470     CYS C 252    SG                                                  
REMARK 470     ASP C 253    CG   OD1  OD2                                       
REMARK 470     ARG C 254    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 278    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LYS D 626    CG   CD   CE   NZ                                   
REMARK 470     LYS D 628    CG   CD   CE   NZ                                   
REMARK 470     LYS D 689    CG   CD   CE   NZ                                   
REMARK 470     ASN D 713    CG   OD1  ND2                                       
REMARK 470     LYS D 762    CG   CD   CE   NZ                                   
REMARK 470     ARG D 767    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 779    CG   CD   CE   NZ                                   
REMARK 470     GLU D 813    CG   CD   OE1  OE2                                  
REMARK 470     ILE D 820    CG1  CG2  CD1                                       
REMARK 470     ARG D 827    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE D 847    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL D 908    CG1  CG2                                            
REMARK 470     GLU E 625    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 626    CG   CD   CE   NZ                                   
REMARK 470     LYS E 628    CG   CD   CE   NZ                                   
REMARK 470     LYS E 689    CG   CD   CE   NZ                                   
REMARK 470     ASN E 713    CG   OD1  ND2                                       
REMARK 470     LYS E 762    CG   CD   CE   NZ                                   
REMARK 470     ARG E 767    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E 779    CG   CD   CE   NZ                                   
REMARK 470     GLU E 813    CG   CD   OE1  OE2                                  
REMARK 470     ILE E 820    CG1  CG2  CD1                                       
REMARK 470     ARG E 827    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE E 847    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL E 908    CG1  CG2                                            
REMARK 470     HIS F 250    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR F 251    OG1  CG2                                            
REMARK 470     CYS F 252    SG                                                  
REMARK 470     ASP F 253    CG   OD1  OD2                                       
REMARK 470     ARG F 254    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG F 278    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     HIS G 250    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR G 251    OG1  CG2                                            
REMARK 470     CYS G 252    SG                                                  
REMARK 470     ASP G 253    CG   OD1  OD2                                       
REMARK 470     ARG G 254    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG G 278    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LYS H 626    CG   CD   CE   NZ                                   
REMARK 470     LYS H 628    CG   CD   CE   NZ                                   
REMARK 470     LYS H 689    CG   CD   CE   NZ                                   
REMARK 470     ASN H 713    CG   OD1  ND2                                       
REMARK 470     LYS H 762    CG   CD   CE   NZ                                   
REMARK 470     ARG H 767    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS H 779    CG   CD   CE   NZ                                   
REMARK 470     GLU H 813    CG   CD   OE1  OE2                                  
REMARK 470     ILE H 820    CG1  CG2  CD1                                       
REMARK 470     ARG H 827    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE H 847    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL H 908    CG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    VAL A   686     NH2  ARG A   732              2.07            
REMARK 500   OE1  GLU E   861     N    HIS E   869              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 644   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES          
REMARK 500    PRO A 845   C   -  N   -  CD  ANGL. DEV. = -29.6 DEGREES          
REMARK 500    ASN D 875   N   -  CA  -  C   ANGL. DEV. = -17.5 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    ALA A 624      118.46    172.52                                   
REMARK 500    LYS A 676      -38.59    -27.94                                   
REMARK 500    ARG A 684       43.97    -67.70                                   
REMARK 500    TRP A 694       25.72    -75.92                                   
REMARK 500    ASN A 707      -79.36    -19.56                                   
REMARK 500    ASP A 708       14.71    -66.01                                   
REMARK 500    GLU A 721     -167.46   -117.97                                   
REMARK 500    LEU A 726      -29.82    -37.86                                   
REMARK 500    ASN A 753      156.16    177.31                                   
REMARK 500    VAL A 781       18.83   -143.54                                   
REMARK 500    ALA A 783       33.68    -69.06                                   
REMARK 500    ASP A 807       88.31   -173.79                                   
REMARK 500    LYS A 808      103.74    -56.20                                   
REMARK 500    HIS A 843      -83.61    -87.95                                   
REMARK 500    PRO A 845      -10.50     45.28                                   
REMARK 500    ASN A 849       48.51     30.64                                   
REMARK 500    GLU A 850       10.64     84.48                                   
REMARK 500    SER A 874     -167.20     63.66                                   
REMARK 500    ALA A 880      -70.59    -63.73                                   
REMARK 500    LEU A 884      -88.92    -60.24                                   
REMARK 500    LEU A 885      -39.43    -37.02                                   
REMARK 500    ALA A 899      -59.62    -23.53                                   
REMARK 500    PRO A 900       19.05    -67.92                                   
REMARK 500    THR B 181      162.29    -48.34                                   
REMARK 500    PHE B 196      -13.54     76.32                                   
REMARK 500    VAL B 222      -74.02    -94.27                                   
REMARK 500    THR B 225      -64.60    -21.23                                   
REMARK 500    TRP B 235       25.48    -79.39                                   
REMARK 500    HIS B 250       34.14     80.96                                   
REMARK 500    ARG B 254      107.41    174.87                                   
REMARK 500    PRO B 255      128.24    -34.21                                   
REMARK 500    PRO B 256      -69.72    -26.99                                   
REMARK 500    ARG B 265      -72.39    -58.06                                   
REMARK 500    PRO B 272     -159.96    -80.93                                   
REMARK 500    SER B 276       97.51    -36.21                                   
REMARK 500    PRO B 277      -76.13    -56.37                                   
REMARK 500    ARG B 278     -169.47   -122.27                                   
REMARK 500    ASN B 291     -177.19    -56.44                                   
REMARK 500    MET B 304      148.02    170.42                                   
REMARK 500    ASP B 311      104.38   -163.31                                   
REMARK 500    HIS B 313      -29.40   -154.18                                   
REMARK 500    SER B 325      166.85    175.25                                   
REMARK 500    PRO B 328      144.27    -27.49                                   
REMARK 500    ALA B 336       50.60    -68.02                                   
REMARK 500    LEU B 337      -75.61   -116.54                                   
REMARK 500    VAL B 338      132.57    -38.15                                   
REMARK 500    LYS B 362      -29.26    -38.44                                   
REMARK 500    PHE C 196       -7.43     75.14                                   
REMARK 500    GLU C 197      140.73    178.80                                   
REMARK 500    VAL C 222      -69.97    -96.83                                   
REMARK 500    TRP C 235       24.90    -79.88                                   
REMARK 500    PRO C 237      150.84    -50.00                                   
REMARK 500    LEU C 248      104.89    -54.79                                   
REMARK 500    HIS C 250       36.76     78.89                                   
REMARK 500    ARG C 254      108.43    176.04                                   
REMARK 500    PRO C 255      125.37    -32.97                                   
REMARK 500    PRO C 272     -158.57    -79.53                                   
REMARK 500    SER C 276       95.99    -34.01                                   
REMARK 500    PRO C 277      -74.65    -57.71                                   
REMARK 500    ARG C 278     -165.27   -121.87                                   
REMARK 500    MET C 304      148.90    170.04                                   
REMARK 500    PRO C 310     -167.33    -78.83                                   
REMARK 500    ASP C 311      106.18   -165.12                                   
REMARK 500    HIS C 313      -28.82   -156.14                                   
REMARK 500    SER C 325      167.13    175.99                                   
REMARK 500    PRO C 328      147.89    -29.26                                   
REMARK 500    ALA C 336       47.91    -67.72                                   
REMARK 500    LEU C 337      -74.58   -116.61                                   
REMARK 500    VAL C 338      131.90    -37.13                                   
REMARK 500    SER C 352       76.30   -100.24                                   
REMARK 500    ARG D 627      159.92    -48.02                                   
REMARK 500    GLN D 674       46.35     40.00                                   
REMARK 500    TRP D 694       20.09    -75.50                                   
REMARK 500    GLU D 721     -169.56   -122.49                                   
REMARK 500    ASN D 753      158.80    175.33                                   
REMARK 500    SER D 771      168.27    178.10                                   
REMARK 500    PRO D 773     -177.00    -68.03                                   
REMARK 500    VAL D 781       14.13   -143.82                                   
REMARK 500    ALA D 783       30.66    -69.53                                   
REMARK 500    ASP D 807       90.33   -172.84                                   
REMARK 500    LYS D 808      104.23    -55.83                                   
REMARK 500    GLU D 813       14.11    -68.66                                   
REMARK 500    PRO D 845      -55.61    -17.76                                   
REMARK 500    ASN D 849       74.02     -6.47                                   
REMARK 500    LEU D 855      149.57    -37.58                                   
REMARK 500    SER D 874     -152.99    -73.98                                   
REMARK 500    ALA D 899      -63.53    -25.70                                   
REMARK 500    GLU D 903        6.88    -65.11                                   
REMARK 500    ALA E 624     -159.99   -136.91                                   
REMARK 500    GLU E 625       61.82   -151.40                                   
REMARK 500    VAL E 680     -166.09    -74.43                                   
REMARK 500    ARG E 684       43.69    -70.39                                   
REMARK 500    TRP E 694       22.44    -70.42                                   
REMARK 500    GLU E 721     -166.97   -124.98                                   
REMARK 500    LEU E 726      -33.69    -39.99                                   
REMARK 500    ASN E 753      161.56    170.21                                   
REMARK 500    PRO E 773     -179.44    -64.86                                   
REMARK 500    VAL E 781       10.70   -144.70                                   
REMARK 500    ALA E 783       36.00    -69.57                                   
REMARK 500    ASP E 807       87.53   -171.01                                   
REMARK 500    LYS E 808       99.65    -52.71                                   
REMARK 500    HIS E 817      130.76    -37.64                                   
REMARK 500    PRO E 845      -38.82    -13.10                                   
REMARK 500    HIS E 869       10.30     80.65                                   
REMARK 500    VAL E 873      -92.72   -119.82                                   
REMARK 500    ASN E 875       46.38    -72.97                                   
REMARK 500    SER E 888     -173.96    -66.45                                   
REMARK 500    LEU E 897       -4.51    -48.59                                   
REMARK 500    ALA E 899      -41.97    -20.56                                   
REMARK 500    ALA E 906      139.20    -39.90                                   
REMARK 500    PHE F 196      -15.55     77.66                                   
REMARK 500    GLU F 197      142.60   -171.06                                   
REMARK 500    VAL F 222      -75.58    -91.06                                   
REMARK 500    PRO F 237      152.29    -48.58                                   
REMARK 500    LEU F 248      105.85    -57.82                                   
REMARK 500    HIS F 250       36.15     77.73                                   
REMARK 500    ARG F 254      109.73    176.51                                   
REMARK 500    PRO F 255      125.65    -33.37                                   
REMARK 500    PRO F 256      -65.33    -29.27                                   
REMARK 500    PRO F 272     -158.39    -79.79                                   
REMARK 500    SER F 276       98.14    -37.38                                   
REMARK 500    PRO F 277      -77.52    -54.05                                   
REMARK 500    ARG F 278     -167.41   -122.53                                   
REMARK 500    ASN F 291      179.92    -58.94                                   
REMARK 500    MET F 304      149.61    169.61                                   
REMARK 500    PRO F 310     -167.09    -78.29                                   
REMARK 500    ASP F 311      104.52   -163.86                                   
REMARK 500    HIS F 313      -29.25   -154.80                                   
REMARK 500    SER F 325      169.27    173.25                                   
REMARK 500    PRO F 328      144.43    -26.88                                   
REMARK 500    ALA F 336       49.98    -67.64                                   
REMARK 500    LEU F 337      -76.48   -116.57                                   
REMARK 500    VAL F 338      133.95    -39.85                                   
REMARK 500    LYS F 362      -32.50    -38.78                                   
REMARK 500    THR G 181      159.13    -48.30                                   
REMARK 500    TRP G 185        8.88    -65.30                                   
REMARK 500    PHE G 196      -11.29     76.46                                   
REMARK 500    GLU G 197      141.53   -172.13                                   
REMARK 500    VAL G 222      -74.95    -93.00                                   
REMARK 500    THR G 225      -68.70    -21.64                                   
REMARK 500    TRP G 235       25.53    -79.40                                   
REMARK 500    LEU G 248      102.79    -56.65                                   
REMARK 500    HIS G 250       37.74     78.01                                   
REMARK 500    ARG G 254      109.09    176.94                                   
REMARK 500    PRO G 255      127.96    -33.55                                   
REMARK 500    PRO G 272     -160.98    -76.73                                   
REMARK 500    SER G 276       97.28    -35.24                                   
REMARK 500    PRO G 277      -80.82    -53.90                                   
REMARK 500    ARG G 278     -166.29   -121.89                                   
REMARK 500    ASN G 291      177.93    -58.76                                   
REMARK 500    MET G 304      149.31    171.94                                   
REMARK 500    PRO G 310     -166.03    -76.76                                   
REMARK 500    ASP G 311      102.37   -165.35                                   
REMARK 500    HIS G 313      -29.11   -154.75                                   
REMARK 500    SER G 325      166.66    176.45                                   
REMARK 500    PRO G 328      148.12    -28.21                                   
REMARK 500    ALA G 336       49.26    -68.24                                   
REMARK 500    LEU G 337      -72.49   -118.47                                   
REMARK 500    VAL G 338      131.02    -38.80                                   
REMARK 500    LYS G 362      -33.53    -38.92                                   
REMARK 500    ILE H 639       40.47   -107.85                                   
REMARK 500    LYS H 676      -37.95    -32.07                                   
REMARK 500    VAL H 680     -166.46    -79.22                                   
REMARK 500    ARG H 684       44.61    -77.39                                   
REMARK 500    ILE H 691      -71.40    -52.53                                   
REMARK 500    ASN H 707      -70.16    -22.29                                   
REMARK 500    ASP H 708       20.97    -77.97                                   
REMARK 500    LEU H 726      -29.91    -37.15                                   
REMARK 500    ASN H 753      161.53    179.46                                   
REMARK 500    SER H 771      168.99    178.90                                   
REMARK 500    VAL H 781       15.31   -145.15                                   
REMARK 500    ALA H 783       35.44    -73.44                                   
REMARK 500    ASP H 807       92.04   -170.25                                   
REMARK 500    LYS H 808      102.10    -59.23                                   
REMARK 500    GLU H 813        9.06    -66.76                                   
REMARK 500    VAL H 873     -125.87   -127.71                                   
REMARK 500    SER H 874      167.82    -42.11                                   
REMARK 500    ASN H 875       10.82    -68.51                                   
REMARK 500    SER H 888      142.31    -21.36                                   
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 SAH A 1                   
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH D 4                   
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH E 5                   
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH H 8                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2PV0   RELATED DB: PDB                                   
REMARK 900 DNMT3L                                                               
REMARK 900 RELATED ID: 2PVC   RELATED DB: PDB                                   
REMARK 900 DNMT3L-HISTONE H3 TAIL                                               
DBREF  2QRV A  623   908  UNP    Q9Y6K1   DNM3A_HUMAN    624    909             
DBREF  2QRV B  160   386  UNP    Q9UJW3   DNM3L_HUMAN    160    387             
DBREF  2QRV C  160   386  UNP    Q9UJW3   DNM3L_HUMAN    160    387             
DBREF  2QRV D  625   908  UNP    Q9Y6K1   DNM3A_HUMAN    624    909             
DBREF  2QRV E  623   908  UNP    Q9Y6K1   DNM3A_HUMAN    624    909             
DBREF  2QRV F  160   386  UNP    Q9UJW3   DNM3L_HUMAN    160    387             
DBREF  2QRV G  160   386  UNP    Q9UJW3   DNM3L_HUMAN    160    387             
DBREF  2QRV H  623   908  UNP    Q9Y6K1   DNM3A_HUMAN    624    909             
SEQADV 2QRV MET A  614  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV GLY A  615  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS A  616  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS A  617  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS A  618  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS A  619  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS A  620  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS A  621  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV MET A  622  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV GLY B  157  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 2QRV SER B  158  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 2QRV MET B  159  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 2QRV GLY C  157  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 2QRV SER C  158  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 2QRV MET C  159  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 2QRV MET D  614  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV GLY D  615  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS D  616  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS D  617  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS D  618  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS D  619  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS D  620  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS D  621  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV MET D  622  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV MET E  614  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV GLY E  615  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS E  616  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS E  617  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS E  618  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS E  619  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS E  620  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS E  621  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV MET E  622  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV GLY F  157  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 2QRV SER F  158  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 2QRV MET F  159  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 2QRV GLY G  157  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 2QRV SER G  158  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 2QRV MET G  159  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 2QRV MET H  614  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV GLY H  615  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS H  616  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS H  617  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS H  618  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS H  619  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS H  620  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV HIS H  621  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 2QRV MET H  622  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQRES   1 A  295  MET GLY HIS HIS HIS HIS HIS HIS MET PRO ALA GLU LYS          
SEQRES   2 A  295  ARG LYS PRO ILE ARG VAL LEU SER LEU PHE ASP GLY ILE          
SEQRES   3 A  295  ALA THR GLY LEU LEU VAL LEU LYS ASP LEU GLY ILE GLN          
SEQRES   4 A  295  VAL ASP ARG TYR ILE ALA SER GLU VAL CYS GLU ASP SER          
SEQRES   5 A  295  ILE THR VAL GLY MET VAL ARG HIS GLN GLY LYS ILE MET          
SEQRES   6 A  295  TYR VAL GLY ASP VAL ARG SER VAL THR GLN LYS HIS ILE          
SEQRES   7 A  295  GLN GLU TRP GLY PRO PHE ASP LEU VAL ILE GLY GLY SER          
SEQRES   8 A  295  PRO CYS ASN ASP LEU SER ILE VAL ASN PRO ALA ARG LYS          
SEQRES   9 A  295  GLY LEU TYR GLU GLY THR GLY ARG LEU PHE PHE GLU PHE          
SEQRES  10 A  295  TYR ARG LEU LEU HIS ASP ALA ARG PRO LYS GLU GLY ASP          
SEQRES  11 A  295  ASP ARG PRO PHE PHE TRP LEU PHE GLU ASN VAL VAL ALA          
SEQRES  12 A  295  MET GLY VAL SER ASP LYS ARG ASP ILE SER ARG PHE LEU          
SEQRES  13 A  295  GLU SER ASN PRO VAL MET ILE ASP ALA LYS GLU VAL SER          
SEQRES  14 A  295  ALA ALA HIS ARG ALA ARG TYR PHE TRP GLY ASN LEU PRO          
SEQRES  15 A  295  GLY MET ASN ARG PRO LEU ALA SER THR VAL ASN ASP LYS          
SEQRES  16 A  295  LEU GLU LEU GLN GLU CYS LEU GLU HIS GLY ARG ILE ALA          
SEQRES  17 A  295  LYS PHE SER LYS VAL ARG THR ILE THR THR ARG SER ASN          
SEQRES  18 A  295  SER ILE LYS GLN GLY LYS ASP GLN HIS PHE PRO VAL PHE          
SEQRES  19 A  295  MET ASN GLU LYS GLU ASP ILE LEU TRP CYS THR GLU MET          
SEQRES  20 A  295  GLU ARG VAL PHE GLY PHE PRO VAL HIS TYR THR ASP VAL          
SEQRES  21 A  295  SER ASN MET SER ARG LEU ALA ARG GLN ARG LEU LEU GLY          
SEQRES  22 A  295  ARG SER TRP SER VAL PRO VAL ILE ARG HIS LEU PHE ALA          
SEQRES  23 A  295  PRO LEU LYS GLU TYR PHE ALA CYS VAL                          
SEQRES   1 B  230  GLY SER MET TRP ARG SER GLN LEU LYS ALA PHE TYR ASP          
SEQRES   2 B  230  ARG GLU SER GLU ASN PRO LEU GLU MET PHE GLU THR VAL          
SEQRES   3 B  230  PRO VAL TRP ARG ARG GLN PRO VAL ARG VAL LEU SER LEU          
SEQRES   4 B  230  PHE GLU ASP ILE LYS LYS GLU LEU THR SER LEU GLY PHE          
SEQRES   5 B  230  LEU GLU SER GLY SER ASP PRO GLY GLN LEU LYS HIS VAL          
SEQRES   6 B  230  VAL ASP VAL THR ASP THR VAL ARG LYS ASP VAL GLU GLU          
SEQRES   7 B  230  TRP GLY PRO PHE ASP LEU VAL TYR GLY ALA THR PRO PRO          
SEQRES   8 B  230  LEU GLY HIS THR CYS ASP ARG PRO PRO SER TRP TYR LEU          
SEQRES   9 B  230  PHE GLN PHE HIS ARG LEU LEU GLN TYR ALA ARG PRO LYS          
SEQRES  10 B  230  PRO GLY SER PRO ARG PRO PHE PHE TRP MET PHE VAL ASP          
SEQRES  11 B  230  ASN LEU VAL LEU ASN LYS GLU ASP LEU ASP VAL ALA SER          
SEQRES  12 B  230  ARG PHE LEU GLU MET GLU PRO VAL THR ILE PRO ASP VAL          
SEQRES  13 B  230  HIS GLY GLY SER LEU GLN ASN ALA VAL ARG VAL TRP SER          
SEQRES  14 B  230  ASN ILE PRO ALA ILE ARG SER ARG HIS TRP ALA LEU VAL          
SEQRES  15 B  230  SER GLU GLU GLU LEU SER LEU LEU ALA GLN ASN LYS GLN          
SEQRES  16 B  230  SER SER LYS LEU ALA ALA LYS TRP PRO THR LYS LEU VAL          
SEQRES  17 B  230  LYS ASN CYS PHE LEU PRO LEU ARG GLU TYR PHE LYS TYR          
SEQRES  18 B  230  PHE SER THR GLU LEU THR SER SER LEU                          
SEQRES   1 C  230  GLY SER MET TRP ARG SER GLN LEU LYS ALA PHE TYR ASP          
SEQRES   2 C  230  ARG GLU SER GLU ASN PRO LEU GLU MET PHE GLU THR VAL          
SEQRES   3 C  230  PRO VAL TRP ARG ARG GLN PRO VAL ARG VAL LEU SER LEU          
SEQRES   4 C  230  PHE GLU ASP ILE LYS LYS GLU LEU THR SER LEU GLY PHE          
SEQRES   5 C  230  LEU GLU SER GLY SER ASP PRO GLY GLN LEU LYS HIS VAL          
SEQRES   6 C  230  VAL ASP VAL THR ASP THR VAL ARG LYS ASP VAL GLU GLU          
SEQRES   7 C  230  TRP GLY PRO PHE ASP LEU VAL TYR GLY ALA THR PRO PRO          
SEQRES   8 C  230  LEU GLY HIS THR CYS ASP ARG PRO PRO SER TRP TYR LEU          
SEQRES   9 C  230  PHE GLN PHE HIS ARG LEU LEU GLN TYR ALA ARG PRO LYS          
SEQRES  10 C  230  PRO GLY SER PRO ARG PRO PHE PHE TRP MET PHE VAL ASP          
SEQRES  11 C  230  ASN LEU VAL LEU ASN LYS GLU ASP LEU ASP VAL ALA SER          
SEQRES  12 C  230  ARG PHE LEU GLU MET GLU PRO VAL THR ILE PRO ASP VAL          
SEQRES  13 C  230  HIS GLY GLY SER LEU GLN ASN ALA VAL ARG VAL TRP SER          
SEQRES  14 C  230  ASN ILE PRO ALA ILE ARG SER ARG HIS TRP ALA LEU VAL          
SEQRES  15 C  230  SER GLU GLU GLU LEU SER LEU LEU ALA GLN ASN LYS GLN          
SEQRES  16 C  230  SER SER LYS LEU ALA ALA LYS TRP PRO THR LYS LEU VAL          
SEQRES  17 C  230  LYS ASN CYS PHE LEU PRO LEU ARG GLU TYR PHE LYS TYR          
SEQRES  18 C  230  PHE SER THR GLU LEU THR SER SER LEU                          
SEQRES   1 D  295  MET GLY HIS HIS HIS HIS HIS HIS MET PRO ALA GLU LYS          
SEQRES   2 D  295  ARG LYS PRO ILE ARG VAL LEU SER LEU PHE ASP GLY ILE          
SEQRES   3 D  295  ALA THR GLY LEU LEU VAL LEU LYS ASP LEU GLY ILE GLN          
SEQRES   4 D  295  VAL ASP ARG TYR ILE ALA SER GLU VAL CYS GLU ASP SER          
SEQRES   5 D  295  ILE THR VAL GLY MET VAL ARG HIS GLN GLY LYS ILE MET          
SEQRES   6 D  295  TYR VAL GLY ASP VAL ARG SER VAL THR GLN LYS HIS ILE          
SEQRES   7 D  295  GLN GLU TRP GLY PRO PHE ASP LEU VAL ILE GLY GLY SER          
SEQRES   8 D  295  PRO CYS ASN ASP LEU SER ILE VAL ASN PRO ALA ARG LYS          
SEQRES   9 D  295  GLY LEU TYR GLU GLY THR GLY ARG LEU PHE PHE GLU PHE          
SEQRES  10 D  295  TYR ARG LEU LEU HIS ASP ALA ARG PRO LYS GLU GLY ASP          
SEQRES  11 D  295  ASP ARG PRO PHE PHE TRP LEU PHE GLU ASN VAL VAL ALA          
SEQRES  12 D  295  MET GLY VAL SER ASP LYS ARG ASP ILE SER ARG PHE LEU          
SEQRES  13 D  295  GLU SER ASN PRO VAL MET ILE ASP ALA LYS GLU VAL SER          
SEQRES  14 D  295  ALA ALA HIS ARG ALA ARG TYR PHE TRP GLY ASN LEU PRO          
SEQRES  15 D  295  GLY MET ASN ARG PRO LEU ALA SER THR VAL ASN ASP LYS          
SEQRES  16 D  295  LEU GLU LEU GLN GLU CYS LEU GLU HIS GLY ARG ILE ALA          
SEQRES  17 D  295  LYS PHE SER LYS VAL ARG THR ILE THR THR ARG SER ASN          
SEQRES  18 D  295  SER ILE LYS GLN GLY LYS ASP GLN HIS PHE PRO VAL PHE          
SEQRES  19 D  295  MET ASN GLU LYS GLU ASP ILE LEU TRP CYS THR GLU MET          
SEQRES  20 D  295  GLU ARG VAL PHE GLY PHE PRO VAL HIS TYR THR ASP VAL          
SEQRES  21 D  295  SER ASN MET SER ARG LEU ALA ARG GLN ARG LEU LEU GLY          
SEQRES  22 D  295  ARG SER TRP SER VAL PRO VAL ILE ARG HIS LEU PHE ALA          
SEQRES  23 D  295  PRO LEU LYS GLU TYR PHE ALA CYS VAL                          
SEQRES   1 E  295  MET GLY HIS HIS HIS HIS HIS HIS MET PRO ALA GLU LYS          
SEQRES   2 E  295  ARG LYS PRO ILE ARG VAL LEU SER LEU PHE ASP GLY ILE          
SEQRES   3 E  295  ALA THR GLY LEU LEU VAL LEU LYS ASP LEU GLY ILE GLN          
SEQRES   4 E  295  VAL ASP ARG TYR ILE ALA SER GLU VAL CYS GLU ASP SER          
SEQRES   5 E  295  ILE THR VAL GLY MET VAL ARG HIS GLN GLY LYS ILE MET          
SEQRES   6 E  295  TYR VAL GLY ASP VAL ARG SER VAL THR GLN LYS HIS ILE          
SEQRES   7 E  295  GLN GLU TRP GLY PRO PHE ASP LEU VAL ILE GLY GLY SER          
SEQRES   8 E  295  PRO CYS ASN ASP LEU SER ILE VAL ASN PRO ALA ARG LYS          
SEQRES   9 E  295  GLY LEU TYR GLU GLY THR GLY ARG LEU PHE PHE GLU PHE          
SEQRES  10 E  295  TYR ARG LEU LEU HIS ASP ALA ARG PRO LYS GLU GLY ASP          
SEQRES  11 E  295  ASP ARG PRO PHE PHE TRP LEU PHE GLU ASN VAL VAL ALA          
SEQRES  12 E  295  MET GLY VAL SER ASP LYS ARG ASP ILE SER ARG PHE LEU          
SEQRES  13 E  295  GLU SER ASN PRO VAL MET ILE ASP ALA LYS GLU VAL SER          
SEQRES  14 E  295  ALA ALA HIS ARG ALA ARG TYR PHE TRP GLY ASN LEU PRO          
SEQRES  15 E  295  GLY MET ASN ARG PRO LEU ALA SER THR VAL ASN ASP LYS          
SEQRES  16 E  295  LEU GLU LEU GLN GLU CYS LEU GLU HIS GLY ARG ILE ALA          
SEQRES  17 E  295  LYS PHE SER LYS VAL ARG THR ILE THR THR ARG SER ASN          
SEQRES  18 E  295  SER ILE LYS GLN GLY LYS ASP GLN HIS PHE PRO VAL PHE          
SEQRES  19 E  295  MET ASN GLU LYS GLU ASP ILE LEU TRP CYS THR GLU MET          
SEQRES  20 E  295  GLU ARG VAL PHE GLY PHE PRO VAL HIS TYR THR ASP VAL          
SEQRES  21 E  295  SER ASN MET SER ARG LEU ALA ARG GLN ARG LEU LEU GLY          
SEQRES  22 E  295  ARG SER TRP SER VAL PRO VAL ILE ARG HIS LEU PHE ALA          
SEQRES  23 E  295  PRO LEU LYS GLU TYR PHE ALA CYS VAL                          
SEQRES   1 F  230  GLY SER MET TRP ARG SER GLN LEU LYS ALA PHE TYR ASP          
SEQRES   2 F  230  ARG GLU SER GLU ASN PRO LEU GLU MET PHE GLU THR VAL          
SEQRES   3 F  230  PRO VAL TRP ARG ARG GLN PRO VAL ARG VAL LEU SER LEU          
SEQRES   4 F  230  PHE GLU ASP ILE LYS LYS GLU LEU THR SER LEU GLY PHE          
SEQRES   5 F  230  LEU GLU SER GLY SER ASP PRO GLY GLN LEU LYS HIS VAL          
SEQRES   6 F  230  VAL ASP VAL THR ASP THR VAL ARG LYS ASP VAL GLU GLU          
SEQRES   7 F  230  TRP GLY PRO PHE ASP LEU VAL TYR GLY ALA THR PRO PRO          
SEQRES   8 F  230  LEU GLY HIS THR CYS ASP ARG PRO PRO SER TRP TYR LEU          
SEQRES   9 F  230  PHE GLN PHE HIS ARG LEU LEU GLN TYR ALA ARG PRO LYS          
SEQRES  10 F  230  PRO GLY SER PRO ARG PRO PHE PHE TRP MET PHE VAL ASP          
SEQRES  11 F  230  ASN LEU VAL LEU ASN LYS GLU ASP LEU ASP VAL ALA SER          
SEQRES  12 F  230  ARG PHE LEU GLU MET GLU PRO VAL THR ILE PRO ASP VAL          
SEQRES  13 F  230  HIS GLY GLY SER LEU GLN ASN ALA VAL ARG VAL TRP SER          
SEQRES  14 F  230  ASN ILE PRO ALA ILE ARG SER ARG HIS TRP ALA LEU VAL          
SEQRES  15 F  230  SER GLU GLU GLU LEU SER LEU LEU ALA GLN ASN LYS GLN          
SEQRES  16 F  230  SER SER LYS LEU ALA ALA LYS TRP PRO THR LYS LEU VAL          
SEQRES  17 F  230  LYS ASN CYS PHE LEU PRO LEU ARG GLU TYR PHE LYS TYR          
SEQRES  18 F  230  PHE SER THR GLU LEU THR SER SER LEU                          
SEQRES   1 G  230  GLY SER MET TRP ARG SER GLN LEU LYS ALA PHE TYR ASP          
SEQRES   2 G  230  ARG GLU SER GLU ASN PRO LEU GLU MET PHE GLU THR VAL          
SEQRES   3 G  230  PRO VAL TRP ARG ARG GLN PRO VAL ARG VAL LEU SER LEU          
SEQRES   4 G  230  PHE GLU ASP ILE LYS LYS GLU LEU THR SER LEU GLY PHE          
SEQRES   5 G  230  LEU GLU SER GLY SER ASP PRO GLY GLN LEU LYS HIS VAL          
SEQRES   6 G  230  VAL ASP VAL THR ASP THR VAL ARG LYS ASP VAL GLU GLU          
SEQRES   7 G  230  TRP GLY PRO PHE ASP LEU VAL TYR GLY ALA THR PRO PRO          
SEQRES   8 G  230  LEU GLY HIS THR CYS ASP ARG PRO PRO SER TRP TYR LEU          
SEQRES   9 G  230  PHE GLN PHE HIS ARG LEU LEU GLN TYR ALA ARG PRO LYS          
SEQRES  10 G  230  PRO GLY SER PRO ARG PRO PHE PHE TRP MET PHE VAL ASP          
SEQRES  11 G  230  ASN LEU VAL LEU ASN LYS GLU ASP LEU ASP VAL ALA SER          
SEQRES  12 G  230  ARG PHE LEU GLU MET GLU PRO VAL THR ILE PRO ASP VAL          
SEQRES  13 G  230  HIS GLY GLY SER LEU GLN ASN ALA VAL ARG VAL TRP SER          
SEQRES  14 G  230  ASN ILE PRO ALA ILE ARG SER ARG HIS TRP ALA LEU VAL          
SEQRES  15 G  230  SER GLU GLU GLU LEU SER LEU LEU ALA GLN ASN LYS GLN          
SEQRES  16 G  230  SER SER LYS LEU ALA ALA LYS TRP PRO THR LYS LEU VAL          
SEQRES  17 G  230  LYS ASN CYS PHE LEU PRO LEU ARG GLU TYR PHE LYS TYR          
SEQRES  18 G  230  PHE SER THR GLU LEU THR SER SER LEU                          
SEQRES   1 H  295  MET GLY HIS HIS HIS HIS HIS HIS MET PRO ALA GLU LYS          
SEQRES   2 H  295  ARG LYS PRO ILE ARG VAL LEU SER LEU PHE ASP GLY ILE          
SEQRES   3 H  295  ALA THR GLY LEU LEU VAL LEU LYS ASP LEU GLY ILE GLN          
SEQRES   4 H  295  VAL ASP ARG TYR ILE ALA SER GLU VAL CYS GLU ASP SER          
SEQRES   5 H  295  ILE THR VAL GLY MET VAL ARG HIS GLN GLY LYS ILE MET          
SEQRES   6 H  295  TYR VAL GLY ASP VAL ARG SER VAL THR GLN LYS HIS ILE          
SEQRES   7 H  295  GLN GLU TRP GLY PRO PHE ASP LEU VAL ILE GLY GLY SER          
SEQRES   8 H  295  PRO CYS ASN ASP LEU SER ILE VAL ASN PRO ALA ARG LYS          
SEQRES   9 H  295  GLY LEU TYR GLU GLY THR GLY ARG LEU PHE PHE GLU PHE          
SEQRES  10 H  295  TYR ARG LEU LEU HIS ASP ALA ARG PRO LYS GLU GLY ASP          
SEQRES  11 H  295  ASP ARG PRO PHE PHE TRP LEU PHE GLU ASN VAL VAL ALA          
SEQRES  12 H  295  MET GLY VAL SER ASP LYS ARG ASP ILE SER ARG PHE LEU          
SEQRES  13 H  295  GLU SER ASN PRO VAL MET ILE ASP ALA LYS GLU VAL SER          
SEQRES  14 H  295  ALA ALA HIS ARG ALA ARG TYR PHE TRP GLY ASN LEU PRO          
SEQRES  15 H  295  GLY MET ASN ARG PRO LEU ALA SER THR VAL ASN ASP LYS          
SEQRES  16 H  295  LEU GLU LEU GLN GLU CYS LEU GLU HIS GLY ARG ILE ALA          
SEQRES  17 H  295  LYS PHE SER LYS VAL ARG THR ILE THR THR ARG SER ASN          
SEQRES  18 H  295  SER ILE LYS GLN GLY LYS ASP GLN HIS PHE PRO VAL PHE          
SEQRES  19 H  295  MET ASN GLU LYS GLU ASP ILE LEU TRP CYS THR GLU MET          
SEQRES  20 H  295  GLU ARG VAL PHE GLY PHE PRO VAL HIS TYR THR ASP VAL          
SEQRES  21 H  295  SER ASN MET SER ARG LEU ALA ARG GLN ARG LEU LEU GLY          
SEQRES  22 H  295  ARG SER TRP SER VAL PRO VAL ILE ARG HIS LEU PHE ALA          
SEQRES  23 H  295  PRO LEU LYS GLU TYR PHE ALA CYS VAL                          
HET    SAH  A   1      26                                                       
HET    SAH  D   4      26                                                       
HET    SAH  E   5      26                                                       
HET    SAH  H   8      26                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   9  SAH    4(C14 H20 N6 O5 S)                                           
HELIX    1   1 ALA A  640  LEU A  649  1                                  10    
HELIX    2   2 CYS A  662  HIS A  673  1                                  12    
HELIX    3   3 ASP A  682  VAL A  686  5                                   5    
HELIX    4   4 THR A  687  TRP A  694  1                                   8    
HELIX    5   5 CYS A  706  SER A  710  5                                   5    
HELIX    6   6 ARG A  725  ARG A  738  1                                  14    
HELIX    7   7 GLY A  758  GLU A  770  1                                  13    
HELIX    8   8 LYS A  779  VAL A  781  5                                   3    
HELIX    9   9 GLU A  810  CYS A  814  5                                   5    
HELIX   10  10 TRP A  856  GLY A  865  1                                  10    
HELIX   11  11 SER A  877  ARG A  887  1                                  11    
HELIX   12  12 SER A  890  ALA A  899  1                                  10    
HELIX   13  13 PRO A  900  PHE A  905  5                                   6    
HELIX   14  14 PRO B  183  ARG B  187  5                                   5    
HELIX   15  15 VAL B  228  TRP B  235  1                                   8    
HELIX   16  16 PRO B  256  ARG B  271  1                                  16    
HELIX   17  17 ASN B  291  GLU B  303  1                                  13    
HELIX   18  18 SER B  339  SER B  352  1                                  14    
HELIX   19  19 THR B  361  ASN B  366  1                                   6    
HELIX   20  20 CYS B  367  TYR B  374  5                                   8    
HELIX   21  21 PRO C  183  ARG C  187  5                                   5    
HELIX   22  22 VAL C  228  TRP C  235  1                                   8    
HELIX   23  23 PRO C  256  ALA C  270  1                                  15    
HELIX   24  24 ASN C  291  GLU C  303  1                                  13    
HELIX   25  25 SER C  339  SER C  352  1                                  14    
HELIX   26  26 THR C  361  ASN C  366  1                                   6    
HELIX   27  27 CYS C  367  TYR C  374  5                                   8    
HELIX   28  28 ALA D  640  LEU D  649  1                                  10    
HELIX   29  29 CYS D  662  HIS D  673  1                                  12    
HELIX   30  30 ASP D  682  VAL D  686  5                                   5    
HELIX   31  31 THR D  687  TRP D  694  1                                   8    
HELIX   32  32 CYS D  706  SER D  710  5                                   5    
HELIX   33  33 ARG D  725  ARG D  738  1                                  14    
HELIX   34  34 GLY D  758  LEU D  769  1                                  12    
HELIX   35  35 LYS D  779  VAL D  781  5                                   3    
HELIX   36  36 GLU D  810  LEU D  815  5                                   6    
HELIX   37  37 TRP D  856  GLY D  865  1                                  10    
HELIX   38  38 SER D  877  ARG D  887  1                                  11    
HELIX   39  39 SER D  890  ALA D  899  1                                  10    
HELIX   40  40 PRO D  900  PHE D  905  5                                   6    
HELIX   41  41 ALA E  640  LEU E  649  1                                  10    
HELIX   42  42 CYS E  662  HIS E  673  1                                  12    
HELIX   43  43 ASP E  682  VAL E  686  5                                   5    
HELIX   44  44 THR E  687  TRP E  694  1                                   8    
HELIX   45  45 CYS E  706  SER E  710  5                                   5    
HELIX   46  46 ARG E  725  ARG E  738  1                                  14    
HELIX   47  47 GLY E  758  GLU E  770  1                                  13    
HELIX   48  48 LYS E  779  VAL E  781  5                                   3    
HELIX   49  49 GLU E  810  LEU E  815  5                                   6    
HELIX   50  50 TRP E  856  PHE E  864  1                                   9    
HELIX   51  51 SER E  877  SER E  888  1                                  12    
HELIX   52  52 SER E  890  ALA E  899  1                                  10    
HELIX   53  53 PRO E  900  PHE E  905  5                                   6    
HELIX   54  54 PRO F  183  ARG F  187  5                                   5    
HELIX   55  55 VAL F  228  TRP F  235  1                                   8    
HELIX   56  56 PRO F  256  ALA F  270  1                                  15    
HELIX   57  57 ASN F  291  GLU F  303  1                                  13    
HELIX   58  58 SER F  339  SER F  352  1                                  14    
HELIX   59  59 THR F  361  ASN F  366  1                                   6    
HELIX   60  60 CYS F  367  TYR F  374  5                                   8    
HELIX   61  61 PRO G  183  ARG G  187  5                                   5    
HELIX   62  62 VAL G  228  TRP G  235  1                                   8    
HELIX   63  63 PRO G  256  ALA G  270  1                                  15    
HELIX   64  64 ASN G  291  GLU G  303  1                                  13    
HELIX   65  65 SER G  339  SER G  352  1                                  14    
HELIX   66  66 THR G  361  ASN G  366  1                                   6    
HELIX   67  67 CYS G  367  TYR G  374  5                                   8    
HELIX   68  68 ALA H  640  LEU H  649  1                                  10    
HELIX   69  69 CYS H  662  HIS H  673  1                                  12    
HELIX   70  70 ASP H  682  VAL H  686  5                                   5    
HELIX   71  71 THR H  687  TRP H  694  1                                   8    
HELIX   72  72 CYS H  706  SER H  710  5                                   5    
HELIX   73  73 ARG H  725  ARG H  738  1                                  14    
HELIX   74  74 GLY H  758  GLU H  770  1                                  13    
HELIX   75  75 LYS H  779  VAL H  781  5                                   3    
HELIX   76  76 GLU H  810  LEU H  815  5                                   6    
HELIX   77  77 TRP H  856  GLY H  865  1                                  10    
HELIX   78  78 SER H  877  SER H  888  1                                  12    
HELIX   79  79 SER H  890  PHE H  898  1                                   9    
HELIX   80  80 ALA H  899  TYR H  904  5                                   6    
SHEET    1   A 7 ILE A 677  VAL A 680  0                                        
SHEET    2   A 7 VAL A 653  SER A 659  1  N  ALA A 658   O  VAL A 680           
SHEET    3   A 7 ILE A 630  LEU A 635  1  N  VAL A 632   O  ARG A 655           
SHEET    4   A 7 LEU A 699  GLY A 702  1  O  LEU A 699   N  LEU A 633           
SHEET    5   A 7 PHE A 748  VAL A 754  1  O  LEU A 750   N  VAL A 700           
SHEET    6   A 7 ALA A 787  GLY A 792 -1  O  TYR A 789   N  ASN A 753           
SHEET    7   A 7 ILE A 776  ASP A 777 -1  N  ILE A 776   O  ARG A 788           
SHEET    1   B 3 ILE A 820  ALA A 821  0                                        
SHEET    2   B 3 VAL A 846  MET A 848 -1  O  PHE A 847   N  ILE A 820           
SHEET    3   B 3 LYS A 851  ASP A 853 -1  O  LYS A 851   N  MET A 848           
SHEET    1   C 6 LEU B 218  VAL B 221  0                                        
SHEET    2   C 6 VAL B 192  LEU B 195  1  N  VAL B 192   O  LYS B 219           
SHEET    3   C 6 LEU B 240  ALA B 244  1  O  TYR B 242   N  LEU B 195           
SHEET    4   C 6 PHE B 281  ASP B 286  1  O  MET B 283   N  VAL B 241           
SHEET    5   C 6 ARG B 322  SER B 325 -1  O  ARG B 322   N  ASP B 286           
SHEET    6   C 6 VAL B 307  THR B 308 -1  N  VAL B 307   O  VAL B 323           
SHEET    1   D 6 LEU C 218  VAL C 221  0                                        
SHEET    2   D 6 VAL C 192  LEU C 195  1  N  VAL C 192   O  LYS C 219           
SHEET    3   D 6 LEU C 240  ALA C 244  1  O  TYR C 242   N  LEU C 195           
SHEET    4   D 6 PHE C 281  ASP C 286  1  O  MET C 283   N  VAL C 241           
SHEET    5   D 6 ARG C 322  SER C 325 -1  O  ARG C 322   N  ASP C 286           
SHEET    6   D 6 VAL C 307  THR C 308 -1  N  VAL C 307   O  VAL C 323           
SHEET    1   E 7 ILE D 677  VAL D 680  0                                        
SHEET    2   E 7 VAL D 653  SER D 659  1  N  ALA D 658   O  VAL D 680           
SHEET    3   E 7 ILE D 630  LEU D 635  1  N  SER D 634   O  ILE D 657           
SHEET    4   E 7 LEU D 699  GLY D 702  1  O  ILE D 701   N  LEU D 635           
SHEET    5   E 7 PHE D 748  VAL D 754  1  O  LEU D 750   N  VAL D 700           
SHEET    6   E 7 ALA D 787  GLY D 792 -1  O  TYR D 789   N  ASN D 753           
SHEET    7   E 7 ILE D 776  ASP D 777 -1  N  ILE D 776   O  ARG D 788           
SHEET    1   F 3 ARG D 819  ALA D 821  0                                        
SHEET    2   F 3 VAL D 846  MET D 848 -1  O  PHE D 847   N  ILE D 820           
SHEET    3   F 3 LYS D 851  ASP D 853 -1  O  LYS D 851   N  MET D 848           
SHEET    1   G 7 ILE E 677  VAL E 680  0                                        
SHEET    2   G 7 VAL E 653  SER E 659  1  N  ALA E 658   O  VAL E 680           
SHEET    3   G 7 ILE E 630  LEU E 635  1  N  SER E 634   O  ILE E 657           
SHEET    4   G 7 LEU E 699  GLY E 702  1  O  ILE E 701   N  LEU E 633           
SHEET    5   G 7 PHE E 748  VAL E 754  1  O  LEU E 750   N  VAL E 700           
SHEET    6   G 7 ALA E 787  GLY E 792 -1  O  TYR E 789   N  ASN E 753           
SHEET    7   G 7 ILE E 776  ASP E 777 -1  N  ILE E 776   O  ARG E 788           
SHEET    1   H 3 ILE E 820  ALA E 821  0                                        
SHEET    2   H 3 VAL E 846  PHE E 847 -1  O  PHE E 847   N  ILE E 820           
SHEET    3   H 3 GLU E 852  ASP E 853 -1  O  ASP E 853   N  VAL E 846           
SHEET    1   I 6 LEU F 218  VAL F 221  0                                        
SHEET    2   I 6 VAL F 192  LEU F 195  1  N  VAL F 192   O  LYS F 219           
SHEET    3   I 6 LEU F 240  ALA F 244  1  O  TYR F 242   N  LEU F 193           
SHEET    4   I 6 PHE F 281  ASP F 286  1  O  MET F 283   N  VAL F 241           
SHEET    5   I 6 ARG F 322  SER F 325 -1  O  ARG F 322   N  ASP F 286           
SHEET    6   I 6 VAL F 307  THR F 308 -1  N  VAL F 307   O  VAL F 323           
SHEET    1   J 6 LEU G 218  VAL G 221  0                                        
SHEET    2   J 6 VAL G 192  LEU G 195  1  N  VAL G 192   O  LYS G 219           
SHEET    3   J 6 LEU G 240  ALA G 244  1  O  TYR G 242   N  LEU G 193           
SHEET    4   J 6 PHE G 281  ASP G 286  1  O  MET G 283   N  VAL G 241           
SHEET    5   J 6 ARG G 322  SER G 325 -1  O  ARG G 322   N  ASP G 286           
SHEET    6   J 6 VAL G 307  THR G 308 -1  N  VAL G 307   O  VAL G 323           
SHEET    1   K 7 ILE H 677  VAL H 680  0                                        
SHEET    2   K 7 VAL H 653  SER H 659  1  N  TYR H 656   O  MET H 678           
SHEET    3   K 7 ILE H 630  LEU H 635  1  N  VAL H 632   O  ARG H 655           
SHEET    4   K 7 LEU H 699  GLY H 702  1  O  ILE H 701   N  LEU H 635           
SHEET    5   K 7 PHE H 748  VAL H 754  1  O  LEU H 750   N  VAL H 700           
SHEET    6   K 7 ALA H 787  GLY H 792 -1  O  TYR H 789   N  ASN H 753           
SHEET    7   K 7 ILE H 776  ASP H 777 -1  N  ILE H 776   O  ARG H 788           
SHEET    1   L 3 ILE H 820  ALA H 821  0                                        
SHEET    2   L 3 VAL H 846  PHE H 847 -1  O  PHE H 847   N  ILE H 820           
SHEET    3   L 3 GLU H 852  ASP H 853 -1  O  ASP H 853   N  VAL H 846           
SITE     1 AC1 18 PHE A 636  ASP A 637  GLY A 638  ILE A 639                    
SITE     2 AC1 18 THR A 641  SER A 659  GLU A 660  VAL A 661                    
SITE     3 AC1 18 CYS A 662  ASP A 682  VAL A 683  ARG A 684                    
SITE     4 AC1 18 GLY A 703  PRO A 705  LEU A 726  ARG A 887                    
SITE     5 AC1 18 SER A 888  TRP A 889                                          
SITE     1 AC2 18 PHE D 636  ASP D 637  GLY D 638  ILE D 639                    
SITE     2 AC2 18 THR D 641  SER D 659  GLU D 660  VAL D 661                    
SITE     3 AC2 18 CYS D 662  ASP D 682  VAL D 683  ARG D 684                    
SITE     4 AC2 18 GLY D 703  PRO D 705  LEU D 726  ARG D 887                    
SITE     5 AC2 18 SER D 888  TRP D 889                                          
SITE     1 AC3 17 PHE E 636  GLY E 638  ILE E 639  THR E 641                    
SITE     2 AC3 17 SER E 659  GLU E 660  VAL E 661  CYS E 662                    
SITE     3 AC3 17 ASP E 682  VAL E 683  ARG E 684  GLY E 703                    
SITE     4 AC3 17 PRO E 705  LEU E 726  ARG E 887  SER E 888                    
SITE     5 AC3 17 TRP E 889                                                     
SITE     1 AC4 13 PHE H 636  GLY H 638  ILE H 639  THR H 641                    
SITE     2 AC4 13 GLU H 660  VAL H 661  CYS H 662  ASP H 682                    
SITE     3 AC4 13 VAL H 683  GLY H 703  ARG H 887  SER H 888                    
SITE     4 AC4 13 TRP H 889                                                     
CRYST1  401.881  401.881   49.689  90.00  90.00 120.00 H 3          36          
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      0.002488  0.001437  0.000000        0.00000                         
SCALE2      0.000000  0.002873  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020125        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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