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Database: PDB
Entry: 1U2Z
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HEADER    TRANSFERASE                             20-JUL-04   1U2Z              
TITLE     CRYSTAL STRUCTURE OF HISTONE K79 METHYLTRANSFERASE DOT1P              
TITLE    2 FROM YEAST                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-79           
COMPND   3 SPECIFIC;                                                            
COMPND   4 CHAIN: A, B, C;                                                      
COMPND   5 FRAGMENT: C-TERMINAL DOMAIN;                                         
COMPND   6 SYNONYM: HISTONE H3-K79 METHYLTRANSFERASE, H3-K79-HMTASE,            
COMPND   7 DISRUPTER OF TELOMERE SILENCING PROTEIN 1;                           
COMPND   8 EC: 2.1.1.43;                                                        
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: DOT1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PXC415                                    
KEYWDS    HISTONE METHYLTRANSFERASE, NUCLEOSOME                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.SAWADA,Z.YANG,J.R.HORTON,R.E.COLLINS,X.ZHANG,X.CHENG                
REVDAT   3   24-FEB-09 1U2Z    1       VERSN                                    
REVDAT   2   24-JAN-06 1U2Z    1       JRNL                                     
REVDAT   1   07-SEP-04 1U2Z    0                                                
JRNL        AUTH   K.SAWADA,Z.YANG,J.R.HORTON,R.E.COLLINS,X.ZHANG,              
JRNL        AUTH 2 X.CHENG                                                      
JRNL        TITL   STRUCTURE OF THE CONSERVED CORE OF THE YEAST                 
JRNL        TITL 2 DOT1P, A NUCLEOSOMAL HISTONE H3 LYSINE 79                    
JRNL        TITL 3 METHYLTRANSFERASE                                            
JRNL        REF    J.BIOL.CHEM.                  V. 279 43296 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15292170                                                     
JRNL        DOI    10.1074/JBC.M405902200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1019720.490                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 78422                          
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) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3958                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 12051                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2720                       
REMARK   3   BIN FREE R VALUE                    : 0.3130                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 641                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9298                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 78                                      
REMARK   3   SOLVENT ATOMS            : 533                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.80000                                             
REMARK   3    B22 (A**2) : 4.90000                                              
REMARK   3    B33 (A**2) : -4.10000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.77000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.24                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.34                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.33                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.00                           
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 43.29                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : SAM.PARAM                                      
REMARK   3  PARAMETER FILE  4  : DNA-RNA_REP.PARAM                              
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   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1U2Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUL-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB023179.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-NOV-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X26C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79720                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, GLYCEROL, HEPES, PH 7.0,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       73.13750            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   150                                                      
REMARK 465     GLY A   151                                                      
REMARK 465     HIS A   152                                                      
REMARK 465     HIS A   153                                                      
REMARK 465     HIS A   154                                                      
REMARK 465     HIS A   155                                                      
REMARK 465     HIS A   156                                                      
REMARK 465     HIS A   157                                                      
REMARK 465     LYS A   158                                                      
REMARK 465     LYS A   159                                                      
REMARK 465     PRO A   160                                                      
REMARK 465     LEU A   161                                                      
REMARK 465     LYS A   162                                                      
REMARK 465     LYS A   163                                                      
REMARK 465     GLY A   164                                                      
REMARK 465     ARG A   165                                                      
REMARK 465     ALA A   166                                                      
REMARK 465     ASN A   167                                                      
REMARK 465     LYS A   168                                                      
REMARK 465     LYS A   169                                                      
REMARK 465     ASN A   170                                                      
REMARK 465     ASP A   171                                                      
REMARK 465     ARG A   172                                                      
REMARK 465     ASP A   173                                                      
REMARK 465     SER A   174                                                      
REMARK 465     PRO A   175                                                      
REMARK 465     THR A   217                                                      
REMARK 465     ASN A   218                                                      
REMARK 465     SER A   219                                                      
REMARK 465     PRO A   220                                                      
REMARK 465     GLN A   221                                                      
REMARK 465     PRO A   222                                                      
REMARK 465     THR A   223                                                      
REMARK 465     SER A   224                                                      
REMARK 465     LEU A   225                                                      
REMARK 465     THR A   226                                                      
REMARK 465     SER A   227                                                      
REMARK 465     ASP A   228                                                      
REMARK 465     ASN A   229                                                      
REMARK 465     ASP A   230                                                      
REMARK 465     THR A   231                                                      
REMARK 465     SER A   232                                                      
REMARK 465     SER A   233                                                      
REMARK 465     VAL A   234                                                      
REMARK 465     ALA A   568                                                      
REMARK 465     ARG A   569                                                      
REMARK 465     GLY A   570                                                      
REMARK 465     ARG A   571                                                      
REMARK 465     ARG A   572                                                      
REMARK 465     ASN A   573                                                      
REMARK 465     GLY A   575                                                      
REMARK 465     THR A   576                                                      
REMARK 465     PRO A   577                                                      
REMARK 465     ARG A   582                                                      
REMARK 465     MET B   150                                                      
REMARK 465     GLY B   151                                                      
REMARK 465     HIS B   152                                                      
REMARK 465     HIS B   153                                                      
REMARK 465     HIS B   154                                                      
REMARK 465     HIS B   155                                                      
REMARK 465     HIS B   156                                                      
REMARK 465     HIS B   157                                                      
REMARK 465     LYS B   158                                                      
REMARK 465     LYS B   159                                                      
REMARK 465     PRO B   160                                                      
REMARK 465     LEU B   161                                                      
REMARK 465     LYS B   162                                                      
REMARK 465     LYS B   163                                                      
REMARK 465     GLY B   164                                                      
REMARK 465     ARG B   165                                                      
REMARK 465     ALA B   166                                                      
REMARK 465     ASN B   167                                                      
REMARK 465     LYS B   168                                                      
REMARK 465     LYS B   169                                                      
REMARK 465     ASN B   170                                                      
REMARK 465     ASP B   171                                                      
REMARK 465     ARG B   172                                                      
REMARK 465     ASP B   173                                                      
REMARK 465     SER B   174                                                      
REMARK 465     PRO B   175                                                      
REMARK 465     SER B   176                                                      
REMARK 465     ASN B   218                                                      
REMARK 465     SER B   219                                                      
REMARK 465     PRO B   220                                                      
REMARK 465     GLN B   221                                                      
REMARK 465     PRO B   222                                                      
REMARK 465     THR B   223                                                      
REMARK 465     SER B   224                                                      
REMARK 465     LEU B   225                                                      
REMARK 465     THR B   226                                                      
REMARK 465     SER B   227                                                      
REMARK 465     ASP B   228                                                      
REMARK 465     ASN B   229                                                      
REMARK 465     ASP B   230                                                      
REMARK 465     THR B   231                                                      
REMARK 465     SER B   232                                                      
REMARK 465     SER B   233                                                      
REMARK 465     VAL B   234                                                      
REMARK 465     ALA B   567                                                      
REMARK 465     ALA B   568                                                      
REMARK 465     ARG B   569                                                      
REMARK 465     GLY B   570                                                      
REMARK 465     ARG B   571                                                      
REMARK 465     ARG B   572                                                      
REMARK 465     ASN B   573                                                      
REMARK 465     GLY B   575                                                      
REMARK 465     THR B   576                                                      
REMARK 465     ARG B   582                                                      
REMARK 465     MET C   150                                                      
REMARK 465     GLY C   151                                                      
REMARK 465     HIS C   152                                                      
REMARK 465     HIS C   153                                                      
REMARK 465     HIS C   154                                                      
REMARK 465     HIS C   155                                                      
REMARK 465     HIS C   156                                                      
REMARK 465     HIS C   157                                                      
REMARK 465     LYS C   158                                                      
REMARK 465     LYS C   159                                                      
REMARK 465     PRO C   160                                                      
REMARK 465     LEU C   161                                                      
REMARK 465     LYS C   162                                                      
REMARK 465     LYS C   163                                                      
REMARK 465     GLY C   164                                                      
REMARK 465     ARG C   165                                                      
REMARK 465     ALA C   166                                                      
REMARK 465     ASN C   167                                                      
REMARK 465     LYS C   168                                                      
REMARK 465     LYS C   169                                                      
REMARK 465     ASN C   170                                                      
REMARK 465     ASP C   171                                                      
REMARK 465     ARG C   172                                                      
REMARK 465     ASP C   173                                                      
REMARK 465     SER C   174                                                      
REMARK 465     PRO C   175                                                      
REMARK 465     ASN C   218                                                      
REMARK 465     SER C   219                                                      
REMARK 465     PRO C   220                                                      
REMARK 465     GLN C   221                                                      
REMARK 465     PRO C   222                                                      
REMARK 465     THR C   223                                                      
REMARK 465     SER C   224                                                      
REMARK 465     LEU C   225                                                      
REMARK 465     THR C   226                                                      
REMARK 465     SER C   227                                                      
REMARK 465     ASP C   228                                                      
REMARK 465     ASN C   229                                                      
REMARK 465     ASP C   230                                                      
REMARK 465     THR C   231                                                      
REMARK 465     SER C   232                                                      
REMARK 465     SER C   233                                                      
REMARK 465     VAL C   234                                                      
REMARK 465     GLY C   570                                                      
REMARK 465     ARG C   571                                                      
REMARK 465     ARG C   572                                                      
REMARK 465     ASN C   573                                                      
REMARK 465     GLY C   575                                                      
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   OG   SER C   282     OE2  GLU C   286              1.97            
REMARK 500   NE   ARG C   533     OE2  GLU C   549              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PRO B 283   CA    PRO B 283   C      -0.120                       
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    PRO A 283   C   -  N   -  CA  ANGL. DEV. =  21.5 DEGREES          
REMARK 500    PRO A 283   C   -  N   -  CD  ANGL. DEV. = -29.7 DEGREES          
REMARK 500    PRO B 283   C   -  N   -  CD  ANGL. DEV. = -19.3 DEGREES          
REMARK 500    PHE C 255   CB  -  CG  -  CD2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    PHE C 255   CB  -  CG  -  CD1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    PRO C 283   C   -  N   -  CA  ANGL. DEV. =  16.0 DEGREES          
REMARK 500    PRO C 283   C   -  N   -  CD  ANGL. DEV. = -30.1 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    PRO A 192       80.37    -65.80                                   
REMARK 500    THR A 208       60.35   -119.68                                   
REMARK 500    LYS A 256      -73.83    -83.58                                   
REMARK 500    ARG A 257       89.08    -39.06                                   
REMARK 500    SER A 258     -114.46     51.20                                   
REMARK 500    THR A 259     -134.20    109.07                                   
REMARK 500    ALA A 260     -138.41     67.98                                   
REMARK 500    ILE A 261      -86.97    -17.91                                   
REMARK 500    TYR A 364      123.36    -36.33                                   
REMARK 500    ASN A 518     -133.50   -134.24                                   
REMARK 500    PRO B 192       85.09    -68.48                                   
REMARK 500    LYS B 256      -73.03    -64.97                                   
REMARK 500    ARG B 257      163.20    -45.95                                   
REMARK 500    SER B 258      -81.11    -37.15                                   
REMARK 500    THR B 259      115.44     73.69                                   
REMARK 500    ALA B 260       -8.19    172.65                                   
REMARK 500    TYR B 262      129.01   -173.23                                   
REMARK 500    SER B 512      152.04    -48.25                                   
REMARK 500    PRO C 192       79.48    -66.77                                   
REMARK 500    ARG C 216      -78.96   -100.48                                   
REMARK 500    SER C 353      -33.73   -135.92                                   
REMARK 500    TYR C 364      127.64    -38.81                                   
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 801                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 802                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH C 803                 
DBREF  1U2Z A  158   582  UNP    Q04089   DOT1_YEAST     158    582             
DBREF  1U2Z B  158   582  UNP    Q04089   DOT1_YEAST     158    582             
DBREF  1U2Z C  158   582  UNP    Q04089   DOT1_YEAST     158    582             
SEQADV 1U2Z MET A  150  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z GLY A  151  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS A  152  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS A  153  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS A  154  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS A  155  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS A  156  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS A  157  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z MET B  150  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z GLY B  151  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS B  152  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS B  153  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS B  154  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS B  155  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS B  156  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS B  157  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z MET C  150  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z GLY C  151  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS C  152  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS C  153  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS C  154  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS C  155  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS C  156  UNP  Q04089              EXPRESSION TAG                 
SEQADV 1U2Z HIS C  157  UNP  Q04089              EXPRESSION TAG                 
SEQRES   1 A  433  MET GLY HIS HIS HIS HIS HIS HIS LYS LYS PRO LEU LYS          
SEQRES   2 A  433  LYS GLY ARG ALA ASN LYS LYS ASN ASP ARG ASP SER PRO          
SEQRES   3 A  433  SER SER THR PHE VAL ASP TRP ASN GLY PRO CYS LEU ARG          
SEQRES   4 A  433  LEU GLN TYR PRO LEU PHE ASP ILE GLU TYR LEU ARG SER          
SEQRES   5 A  433  HIS GLU ILE TYR SER GLY THR PRO ILE GLN SER ILE SER          
SEQRES   6 A  433  LEU ARG THR ASN SER PRO GLN PRO THR SER LEU THR SER          
SEQRES   7 A  433  ASP ASN ASP THR SER SER VAL THR THR ALA LYS LEU GLN          
SEQRES   8 A  433  SER ILE LEU PHE SER ASN TYR MET GLU GLU TYR LYS VAL          
SEQRES   9 A  433  ASP PHE LYS ARG SER THR ALA ILE TYR ASN PRO MET SER          
SEQRES  10 A  433  GLU ILE GLY LYS LEU ILE GLU TYR SER CYS LEU VAL PHE          
SEQRES  11 A  433  LEU PRO SER PRO TYR ALA GLU GLN LEU LYS GLU THR ILE          
SEQRES  12 A  433  LEU PRO ASP LEU ASN ALA SER PHE ASP ASN SER ASP THR          
SEQRES  13 A  433  LYS GLY PHE VAL ASN ALA ILE ASN LEU TYR ASN LYS MET          
SEQRES  14 A  433  ILE ARG GLU ILE PRO ARG GLN ARG ILE ILE ASP HIS LEU          
SEQRES  15 A  433  GLU THR ILE ASP LYS ILE PRO ARG SER PHE ILE HIS ASP          
SEQRES  16 A  433  PHE LEU HIS ILE VAL TYR THR ARG SER ILE HIS PRO GLN          
SEQRES  17 A  433  ALA ASN LYS LEU LYS HIS TYR LYS ALA PHE SER ASN TYR          
SEQRES  18 A  433  VAL TYR GLY GLU LEU LEU PRO ASN PHE LEU SER ASP VAL          
SEQRES  19 A  433  TYR GLN GLN CYS GLN LEU LYS LYS GLY ASP THR PHE MET          
SEQRES  20 A  433  ASP LEU GLY SER GLY VAL GLY ASN CYS VAL VAL GLN ALA          
SEQRES  21 A  433  ALA LEU GLU CYS GLY CYS ALA LEU SER PHE GLY CYS GLU          
SEQRES  22 A  433  ILE MET ASP ASP ALA SER ASP LEU THR ILE LEU GLN TYR          
SEQRES  23 A  433  GLU GLU LEU LYS LYS ARG CYS LYS LEU TYR GLY MET ARG          
SEQRES  24 A  433  LEU ASN ASN VAL GLU PHE SER LEU LYS LYS SER PHE VAL          
SEQRES  25 A  433  ASP ASN ASN ARG VAL ALA GLU LEU ILE PRO GLN CYS ASP          
SEQRES  26 A  433  VAL ILE LEU VAL ASN ASN PHE LEU PHE ASP GLU ASP LEU          
SEQRES  27 A  433  ASN LYS LYS VAL GLU LYS ILE LEU GLN THR ALA LYS VAL          
SEQRES  28 A  433  GLY CYS LYS ILE ILE SER LEU LYS SER LEU ARG SER LEU          
SEQRES  29 A  433  THR TYR GLN ILE ASN PHE TYR ASN VAL GLU ASN ILE PHE          
SEQRES  30 A  433  ASN ARG LEU LYS VAL GLN ARG TYR ASP LEU LYS GLU ASP          
SEQRES  31 A  433  SER VAL SER TRP THR HIS SER GLY GLY GLU TYR TYR ILE          
SEQRES  32 A  433  SER THR VAL MET GLU ASP VAL ASP GLU SER LEU PHE SER          
SEQRES  33 A  433  PRO ALA ALA ARG GLY ARG ARG ASN ARG GLY THR PRO VAL          
SEQRES  34 A  433  LYS TYR THR ARG                                              
SEQRES   1 B  433  MET GLY HIS HIS HIS HIS HIS HIS LYS LYS PRO LEU LYS          
SEQRES   2 B  433  LYS GLY ARG ALA ASN LYS LYS ASN ASP ARG ASP SER PRO          
SEQRES   3 B  433  SER SER THR PHE VAL ASP TRP ASN GLY PRO CYS LEU ARG          
SEQRES   4 B  433  LEU GLN TYR PRO LEU PHE ASP ILE GLU TYR LEU ARG SER          
SEQRES   5 B  433  HIS GLU ILE TYR SER GLY THR PRO ILE GLN SER ILE SER          
SEQRES   6 B  433  LEU ARG THR ASN SER PRO GLN PRO THR SER LEU THR SER          
SEQRES   7 B  433  ASP ASN ASP THR SER SER VAL THR THR ALA LYS LEU GLN          
SEQRES   8 B  433  SER ILE LEU PHE SER ASN TYR MET GLU GLU TYR LYS VAL          
SEQRES   9 B  433  ASP PHE LYS ARG SER THR ALA ILE TYR ASN PRO MET SER          
SEQRES  10 B  433  GLU ILE GLY LYS LEU ILE GLU TYR SER CYS LEU VAL PHE          
SEQRES  11 B  433  LEU PRO SER PRO TYR ALA GLU GLN LEU LYS GLU THR ILE          
SEQRES  12 B  433  LEU PRO ASP LEU ASN ALA SER PHE ASP ASN SER ASP THR          
SEQRES  13 B  433  LYS GLY PHE VAL ASN ALA ILE ASN LEU TYR ASN LYS MET          
SEQRES  14 B  433  ILE ARG GLU ILE PRO ARG GLN ARG ILE ILE ASP HIS LEU          
SEQRES  15 B  433  GLU THR ILE ASP LYS ILE PRO ARG SER PHE ILE HIS ASP          
SEQRES  16 B  433  PHE LEU HIS ILE VAL TYR THR ARG SER ILE HIS PRO GLN          
SEQRES  17 B  433  ALA ASN LYS LEU LYS HIS TYR LYS ALA PHE SER ASN TYR          
SEQRES  18 B  433  VAL TYR GLY GLU LEU LEU PRO ASN PHE LEU SER ASP VAL          
SEQRES  19 B  433  TYR GLN GLN CYS GLN LEU LYS LYS GLY ASP THR PHE MET          
SEQRES  20 B  433  ASP LEU GLY SER GLY VAL GLY ASN CYS VAL VAL GLN ALA          
SEQRES  21 B  433  ALA LEU GLU CYS GLY CYS ALA LEU SER PHE GLY CYS GLU          
SEQRES  22 B  433  ILE MET ASP ASP ALA SER ASP LEU THR ILE LEU GLN TYR          
SEQRES  23 B  433  GLU GLU LEU LYS LYS ARG CYS LYS LEU TYR GLY MET ARG          
SEQRES  24 B  433  LEU ASN ASN VAL GLU PHE SER LEU LYS LYS SER PHE VAL          
SEQRES  25 B  433  ASP ASN ASN ARG VAL ALA GLU LEU ILE PRO GLN CYS ASP          
SEQRES  26 B  433  VAL ILE LEU VAL ASN ASN PHE LEU PHE ASP GLU ASP LEU          
SEQRES  27 B  433  ASN LYS LYS VAL GLU LYS ILE LEU GLN THR ALA LYS VAL          
SEQRES  28 B  433  GLY CYS LYS ILE ILE SER LEU LYS SER LEU ARG SER LEU          
SEQRES  29 B  433  THR TYR GLN ILE ASN PHE TYR ASN VAL GLU ASN ILE PHE          
SEQRES  30 B  433  ASN ARG LEU LYS VAL GLN ARG TYR ASP LEU LYS GLU ASP          
SEQRES  31 B  433  SER VAL SER TRP THR HIS SER GLY GLY GLU TYR TYR ILE          
SEQRES  32 B  433  SER THR VAL MET GLU ASP VAL ASP GLU SER LEU PHE SER          
SEQRES  33 B  433  PRO ALA ALA ARG GLY ARG ARG ASN ARG GLY THR PRO VAL          
SEQRES  34 B  433  LYS TYR THR ARG                                              
SEQRES   1 C  433  MET GLY HIS HIS HIS HIS HIS HIS LYS LYS PRO LEU LYS          
SEQRES   2 C  433  LYS GLY ARG ALA ASN LYS LYS ASN ASP ARG ASP SER PRO          
SEQRES   3 C  433  SER SER THR PHE VAL ASP TRP ASN GLY PRO CYS LEU ARG          
SEQRES   4 C  433  LEU GLN TYR PRO LEU PHE ASP ILE GLU TYR LEU ARG SER          
SEQRES   5 C  433  HIS GLU ILE TYR SER GLY THR PRO ILE GLN SER ILE SER          
SEQRES   6 C  433  LEU ARG THR ASN SER PRO GLN PRO THR SER LEU THR SER          
SEQRES   7 C  433  ASP ASN ASP THR SER SER VAL THR THR ALA LYS LEU GLN          
SEQRES   8 C  433  SER ILE LEU PHE SER ASN TYR MET GLU GLU TYR LYS VAL          
SEQRES   9 C  433  ASP PHE LYS ARG SER THR ALA ILE TYR ASN PRO MET SER          
SEQRES  10 C  433  GLU ILE GLY LYS LEU ILE GLU TYR SER CYS LEU VAL PHE          
SEQRES  11 C  433  LEU PRO SER PRO TYR ALA GLU GLN LEU LYS GLU THR ILE          
SEQRES  12 C  433  LEU PRO ASP LEU ASN ALA SER PHE ASP ASN SER ASP THR          
SEQRES  13 C  433  LYS GLY PHE VAL ASN ALA ILE ASN LEU TYR ASN LYS MET          
SEQRES  14 C  433  ILE ARG GLU ILE PRO ARG GLN ARG ILE ILE ASP HIS LEU          
SEQRES  15 C  433  GLU THR ILE ASP LYS ILE PRO ARG SER PHE ILE HIS ASP          
SEQRES  16 C  433  PHE LEU HIS ILE VAL TYR THR ARG SER ILE HIS PRO GLN          
SEQRES  17 C  433  ALA ASN LYS LEU LYS HIS TYR LYS ALA PHE SER ASN TYR          
SEQRES  18 C  433  VAL TYR GLY GLU LEU LEU PRO ASN PHE LEU SER ASP VAL          
SEQRES  19 C  433  TYR GLN GLN CYS GLN LEU LYS LYS GLY ASP THR PHE MET          
SEQRES  20 C  433  ASP LEU GLY SER GLY VAL GLY ASN CYS VAL VAL GLN ALA          
SEQRES  21 C  433  ALA LEU GLU CYS GLY CYS ALA LEU SER PHE GLY CYS GLU          
SEQRES  22 C  433  ILE MET ASP ASP ALA SER ASP LEU THR ILE LEU GLN TYR          
SEQRES  23 C  433  GLU GLU LEU LYS LYS ARG CYS LYS LEU TYR GLY MET ARG          
SEQRES  24 C  433  LEU ASN ASN VAL GLU PHE SER LEU LYS LYS SER PHE VAL          
SEQRES  25 C  433  ASP ASN ASN ARG VAL ALA GLU LEU ILE PRO GLN CYS ASP          
SEQRES  26 C  433  VAL ILE LEU VAL ASN ASN PHE LEU PHE ASP GLU ASP LEU          
SEQRES  27 C  433  ASN LYS LYS VAL GLU LYS ILE LEU GLN THR ALA LYS VAL          
SEQRES  28 C  433  GLY CYS LYS ILE ILE SER LEU LYS SER LEU ARG SER LEU          
SEQRES  29 C  433  THR TYR GLN ILE ASN PHE TYR ASN VAL GLU ASN ILE PHE          
SEQRES  30 C  433  ASN ARG LEU LYS VAL GLN ARG TYR ASP LEU LYS GLU ASP          
SEQRES  31 C  433  SER VAL SER TRP THR HIS SER GLY GLY GLU TYR TYR ILE          
SEQRES  32 C  433  SER THR VAL MET GLU ASP VAL ASP GLU SER LEU PHE SER          
SEQRES  33 C  433  PRO ALA ALA ARG GLY ARG ARG ASN ARG GLY THR PRO VAL          
SEQRES  34 C  433  LYS TYR THR ARG                                              
HET    SAH  A 801      26                                                       
HET    SAH  B 802      26                                                       
HET    SAH  C 803      26                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   4  SAH    3(C14 H20 N6 O5 S)                                           
FORMUL   7  HOH   *533(H2 O)                                                    
HELIX    1   1 ASP A  195  HIS A  202  1                                   8    
HELIX    2   2 GLN A  211  LEU A  215  5                                   5    
HELIX    3   3 ASN A  263  VAL A  278  1                                  16    
HELIX    4   4 PRO A  283  ILE A  292  1                                  10    
HELIX    5   5 ILE A  292  ASN A  302  1                                  11    
HELIX    6   6 ASP A  304  ARG A  320  1                                  17    
HELIX    7   7 PRO A  323  GLU A  332  1                                  10    
HELIX    8   8 ARG A  339  ILE A  354  1                                  16    
HELIX    9   9 HIS A  355  LYS A  362  5                                   8    
HELIX   10  10 PHE A  367  VAL A  371  5                                   5    
HELIX   11  11 LEU A  376  CYS A  387  1                                  12    
HELIX   12  12 GLY A  403  GLY A  414  1                                  12    
HELIX   13  13 MET A  424  TYR A  445  1                                  22    
HELIX   14  14 ASN A  463  ILE A  470  1                                   8    
HELIX   15  15 PRO A  471  CYS A  473  5                                   3    
HELIX   16  16 ASP A  484  GLN A  496  1                                  13    
HELIX   17  17 ASN A  524  ASN A  527  5                                   4    
HELIX   18  18 ASP A  560  PHE A  564  5                                   5    
HELIX   19  19 ASP B  195  HIS B  202  1                                   8    
HELIX   20  20 GLN B  211  LEU B  215  5                                   5    
HELIX   21  21 ASN B  263  VAL B  278  1                                  16    
HELIX   22  22 PRO B  283  ASN B  302  1                                  20    
HELIX   23  23 ASP B  304  GLU B  321  1                                  18    
HELIX   24  24 PRO B  323  GLU B  332  1                                  10    
HELIX   25  25 ARG B  339  ILE B  354  1                                  16    
HELIX   26  26 HIS B  355  HIS B  363  5                                   9    
HELIX   27  27 PHE B  367  VAL B  371  5                                   5    
HELIX   28  28 LEU B  376  CYS B  387  1                                  12    
HELIX   29  29 GLY B  403  GLY B  414  1                                  12    
HELIX   30  30 MET B  424  TYR B  445  1                                  22    
HELIX   31  31 ASN B  463  ILE B  470  1                                   8    
HELIX   32  32 PRO B  471  CYS B  473  5                                   3    
HELIX   33  33 ASP B  484  GLN B  496  1                                  13    
HELIX   34  34 ASN B  518  VAL B  522  5                                   5    
HELIX   35  35 ASN B  524  ASN B  527  5                                   4    
HELIX   36  36 ASP B  560  PHE B  564  5                                   5    
HELIX   37  37 ASP C  195  HIS C  202  1                                   8    
HELIX   38  38 GLN C  211  LEU C  215  5                                   5    
HELIX   39  39 ASN C  263  VAL C  278  1                                  16    
HELIX   40  40 PRO C  283  ASN C  302  1                                  20    
HELIX   41  41 ASP C  304  ARG C  320  1                                  17    
HELIX   42  42 PRO C  323  GLU C  332  1                                  10    
HELIX   43  43 ARG C  339  ILE C  354  1                                  16    
HELIX   44  44 HIS C  355  LYS C  362  5                                   8    
HELIX   45  45 PHE C  367  VAL C  371  5                                   5    
HELIX   46  46 LEU C  376  CYS C  387  1                                  12    
HELIX   47  47 GLY C  403  GLY C  414  1                                  12    
HELIX   48  48 MET C  424  TYR C  445  1                                  22    
HELIX   49  49 ASN C  463  ILE C  470  1                                   8    
HELIX   50  50 PRO C  471  CYS C  473  5                                   3    
HELIX   51  51 ASP C  484  GLN C  496  1                                  13    
HELIX   52  52 ASN C  524  ASN C  527  5                                   4    
HELIX   53  53 ASP C  560  SER C  565  5                                   6    
SHEET    1   A 2 CYS A 186  ARG A 188  0                                        
SHEET    2   A 2 LYS A 336  PRO A 338 -1  O  ILE A 337   N  LEU A 187           
SHEET    1   B 2 THR A 236  GLN A 240  0                                        
SHEET    2   B 2 MET A 248  LYS A 252 -1  O  TYR A 251   N  ALA A 237           
SHEET    1   C 7 VAL A 452  LEU A 456  0                                        
SHEET    2   C 7 LEU A 417  GLU A 422  1  N  SER A 418   O  GLU A 453           
SHEET    3   C 7 THR A 394  LEU A 398  1  N  PHE A 395   O  PHE A 419           
SHEET    4   C 7 VAL A 475  VAL A 478  1  O  LEU A 477   N  MET A 396           
SHEET    5   C 7 LYS A 503  SER A 506  1  O  ILE A 505   N  ILE A 476           
SHEET    6   C 7 GLU A 549  VAL A 555 -1  O  TYR A 551   N  SER A 506           
SHEET    7   C 7 LEU A 529  ASP A 535 -1  N  LYS A 530   O  THR A 554           
SHEET    1   D 2 CYS B 186  ARG B 188  0                                        
SHEET    2   D 2 LYS B 336  PRO B 338 -1  O  ILE B 337   N  LEU B 187           
SHEET    1   E 2 THR B 236  GLN B 240  0                                        
SHEET    2   E 2 MET B 248  LYS B 252 -1  O  TYR B 251   N  ALA B 237           
SHEET    1   F 7 VAL B 452  LEU B 456  0                                        
SHEET    2   F 7 LEU B 417  GLU B 422  1  N  SER B 418   O  GLU B 453           
SHEET    3   F 7 THR B 394  LEU B 398  1  N  PHE B 395   O  PHE B 419           
SHEET    4   F 7 VAL B 475  VAL B 478  1  O  LEU B 477   N  MET B 396           
SHEET    5   F 7 LYS B 503  SER B 506  1  O  ILE B 505   N  ILE B 476           
SHEET    6   F 7 GLU B 549  VAL B 555 -1  O  TYR B 551   N  SER B 506           
SHEET    7   F 7 LEU B 529  ASP B 535 -1  N  LYS B 530   O  THR B 554           
SHEET    1   G 2 CYS C 186  ARG C 188  0                                        
SHEET    2   G 2 LYS C 336  PRO C 338 -1  O  ILE C 337   N  LEU C 187           
SHEET    1   H 2 THR C 236  GLN C 240  0                                        
SHEET    2   H 2 MET C 248  LYS C 252 -1  O  TYR C 251   N  ALA C 237           
SHEET    1   I 7 VAL C 452  LEU C 456  0                                        
SHEET    2   I 7 LEU C 417  GLU C 422  1  N  SER C 418   O  GLU C 453           
SHEET    3   I 7 THR C 394  LEU C 398  1  N  PHE C 395   O  PHE C 419           
SHEET    4   I 7 VAL C 475  VAL C 478  1  O  LEU C 477   N  MET C 396           
SHEET    5   I 7 LYS C 503  SER C 506  1  O  ILE C 505   N  ILE C 476           
SHEET    6   I 7 GLU C 549  VAL C 555 -1  O  TYR C 551   N  SER C 506           
SHEET    7   I 7 LEU C 529  ASP C 535 -1  N  LYS C 530   O  THR C 554           
CISPEP   1 SER A  282    PRO A  283          0        13.49                     
CISPEP   2 SER B  282    PRO B  283          0        -9.55                     
CISPEP   3 SER C  282    PRO C  283          0         8.18                     
SITE     1 AC1 19 ASN A 369  TYR A 370  GLY A 373  LEU A 375                    
SITE     2 AC1 19 ASP A 397  GLY A 399  CYS A 405  GLU A 422                    
SITE     3 AC1 19 ILE A 423  MET A 424  SER A 459  PHE A 460                    
SITE     4 AC1 19 ASN A 479  HOH A 802  HOH A 814  HOH A 867                    
SITE     5 AC1 19 HOH A 874  HOH A 916  GLU C 197                               
SITE     1 AC2 18 ASN B 369  TYR B 370  GLY B 373  LEU B 375                    
SITE     2 AC2 18 ASP B 397  GLY B 399  CYS B 405  GLU B 422                    
SITE     3 AC2 18 ILE B 423  MET B 424  SER B 459  PHE B 460                    
SITE     4 AC2 18 ASN B 479  HOH B 805  HOH B 806  HOH B 810                    
SITE     5 AC2 18 HOH B 811  HOH B 812                                          
SITE     1 AC3 19 ASN C 369  TYR C 370  GLY C 373  LEU C 375                    
SITE     2 AC3 19 ASP C 397  GLY C 399  CYS C 405  GLU C 422                    
SITE     3 AC3 19 ILE C 423  MET C 424  SER C 459  PHE C 460                    
SITE     4 AC3 19 ASN C 479  LEU C 487  HOH C 805  HOH C 825                    
SITE     5 AC3 19 HOH C 830  HOH C 858  HOH C 878                               
CRYST1   73.070  146.275   75.412  90.00  97.68  90.00 P 1 21 1      6          
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      0.013686  0.000000  0.001845        0.00000                         
SCALE2      0.000000  0.006836  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013381        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system