GenomeNet

Database: PDB
Entry: 1XQH
LinkDB: 1XQH
Original site: 1XQH 
HEADER    TRANSFERASE                             12-OCT-04   1XQH              
TITLE     CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF THE                         
TITLE    2 METHYLTRANSFERASE SET9 (ALSO KNOWN AS SET7/9) WITH A P53             
TITLE    3 PEPTIDE AND SAH                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-4            
COMPND   3 SPECIFIC;                                                            
COMPND   4 CHAIN: A, E;                                                         
COMPND   5 FRAGMENT: N-DOMAIN, SET-DOMAIN;                                      
COMPND   6 SYNONYM: LYSINE N-METHYLTRANSFERASE, HISTONE H3-K4                   
COMPND   7 METHYLTRANSFERASE, H3-K4-HMTASE, SET DOMAIN- CONTAINING              
COMPND   8 SET7, SET9, SET7/9;                                                  
COMPND   9 EC: 2.1.1.43;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: 9-MER PEPTIDE FROM TUMOR PROTEIN P53;                      
COMPND  13 CHAIN: B, F;                                                         
COMPND  14 FRAGMENT: MONO-METHYLATED P53 PEPTIDE;                               
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.             
KEYWDS    SET9-P53 COMPLEX, SET-DOMAIN, LYSINE METHYLATION,                     
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.CHUIKOV,J.K.KURASH,J.R.WILSON,B.XIAO,N.JUSTIN,G.S.IVANOV,           
AUTHOR   2 K.MCKINNEY,P.TEMPST,C.PRIVES,S.J.GAMBLIN,N.A.BARLEV,                 
AUTHOR   3 D.REINBERG                                                           
REVDAT   2   24-FEB-09 1XQH    1       VERSN                                    
REVDAT   1   23-NOV-04 1XQH    0                                                
JRNL        AUTH   S.CHUIKOV,J.K.KURASH,J.R.WILSON,B.XIAO,N.JUSTIN,             
JRNL        AUTH 2 G.S.IVANOV,K.MCKINNEY,P.TEMPST,C.PRIVES,                     
JRNL        AUTH 3 S.J.GAMBLIN,N.A.BARLEV,D.REINBERG                            
JRNL        TITL   REGULATION OF P53 ACTIVITY THROUGH LYSINE                    
JRNL        TITL 2 METHYLATION                                                  
JRNL        REF    NATURE                        V. 432   353 2004              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   15525938                                                     
JRNL        DOI    10.1038/NATURE03117                                          
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5                                             
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 49595                          
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 + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2667                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.80                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2513                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 66.50                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 128                          
REMARK   3   BIN FREE R VALUE                    : 0.3180                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4002                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 717                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 7.38                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.62000                                             
REMARK   3    B22 (A**2) : 0.28000                                              
REMARK   3    B33 (A**2) : 1.34000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.65000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.282         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.126         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.111         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.783         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4158 ; 0.010 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  3552 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5640 ; 1.753 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8336 ; 1.732 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   504 ; 4.536 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   709 ;17.846 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   602 ; 0.166 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4600 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   818 ; 0.007 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   925 ; 0.268 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3638 ; 0.241 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.292 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   682 ; 0.182 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     6 ; 0.078 ; 0.500       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     8 ; 0.243 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    57 ; 0.233 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    48 ; 0.215 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):     3 ; 0.024 ; 0.500       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2550 ; 0.551 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4108 ; 1.058 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1608 ; 1.429 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1532 ; 2.314 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  4158 ; 0.887 ; 2.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   717 ; 0.952 ; 2.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  4054 ; 0.577 ; 2.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   117        A   192                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0140  18.5430  18.2130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4923 T22:   0.2651                                     
REMARK   3      T33:   0.2623 T12:   0.0123                                     
REMARK   3      T13:  -0.0289 T23:  -0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9338 L22:   4.0525                                     
REMARK   3      L33:   1.9738 L12:   0.7220                                     
REMARK   3      L13:  -0.2481 L23:   0.0362                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0655 S12:  -0.0383 S13:   0.3120                       
REMARK   3      S21:   0.1934 S22:   0.0115 S23:   0.4713                       
REMARK   3      S31:  -0.1678 S32:  -0.1123 S33:   0.0540                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   193        A   366                          
REMARK   3    RESIDUE RANGE :   B   369        B   374                          
REMARK   3    RESIDUE RANGE :   A  1501        A  1501                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.5000  -7.1130  15.7820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5087 T22:   0.2598                                     
REMARK   3      T33:   0.1895 T12:  -0.0045                                     
REMARK   3      T13:  -0.0208 T23:   0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4508 L22:   2.2838                                     
REMARK   3      L33:   1.2660 L12:  -0.2193                                     
REMARK   3      L13:  -0.1624 L23:   0.0859                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0341 S12:  -0.0527 S13:  -0.3547                       
REMARK   3      S21:   0.2150 S22:  -0.0030 S23:  -0.0103                       
REMARK   3      S31:   0.2539 S32:   0.0255 S33:   0.0372                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   117        E   192                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.1540  29.5240  18.2270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4844 T22:   0.2708                                     
REMARK   3      T33:   0.2598 T12:   0.0094                                     
REMARK   3      T13:  -0.0399 T23:   0.0137                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7236 L22:   4.5383                                     
REMARK   3      L33:   1.7579 L12:   0.6019                                     
REMARK   3      L13:   0.1191 L23:  -0.1078                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0429 S12:  -0.0536 S13:  -0.2897                       
REMARK   3      S21:   0.2033 S22:  -0.0153 S23:  -0.4484                       
REMARK   3      S31:   0.1524 S32:   0.1191 S33:   0.0582                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   193        E   366                          
REMARK   3    RESIDUE RANGE :   F   369        F   374                          
REMARK   3    RESIDUE RANGE :   A  1501        A  1501                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.6620  55.3190  15.7170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5105 T22:   0.2587                                     
REMARK   3      T33:   0.1931 T12:  -0.0035                                     
REMARK   3      T13:  -0.0534 T23:  -0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4083 L22:   2.5017                                     
REMARK   3      L33:   1.3441 L12:  -0.2379                                     
REMARK   3      L13:   0.1172 L23:  -0.1194                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0410 S12:  -0.0522 S13:   0.3721                       
REMARK   3      S21:   0.2258 S22:   0.0043 S23:   0.0056                       
REMARK   3      S31:  -0.2711 S32:  -0.0229 S33:   0.0367                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1502        A  1852                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.4010  24.1700  15.0340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3222 T22:   0.1954                                     
REMARK   3      T33:   0.0067 T12:  -0.0018                                     
REMARK   3      T13:  -0.0463 T23:  -0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3149 L22:   1.5654                                     
REMARK   3      L33:   0.3296 L12:   0.1148                                     
REMARK   3      L13:  -0.0054 L23:  -0.0278                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0031 S12:   0.0221 S13:  -0.0045                       
REMARK   3      S21:   0.1393 S22:  -0.0356 S23:  -0.0090                       
REMARK   3      S31:  -0.0061 S32:   0.0002 S33:   0.0325                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 1XQH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-OCT-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030647.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAY-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978                              
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52283                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY                : 15.000                             
REMARK 200  R MERGE                    (I) : 0.03800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1O9S                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, TRIS-HCL, PH 7.8, VAPOR         
REMARK 280  DIFFUSION, TEMPERATURE 291K                                         
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       51.56150            
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                                                    
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: THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT CONSISTS OF   TWO       
REMARK 300 BIOLOGICAL MOLECULES,                                                
REMARK 300  THE DIMER IS FORMED BY THE COMPLEX                                  
REMARK 300 OF CHAIN A WITH A PEPTIDE CHAIN B AND CHAIN E WITH                   
REMARK 300 A PEPTIDE CHAIN F. CHAINS A AND E ARE MONOMERIC IN THE               
REMARK 300 PHYSIOLOGICAL STATE.                                                 
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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     GLY A   103                                                      
REMARK 465     PRO A   104                                                      
REMARK 465     LEU A   105                                                      
REMARK 465     GLY A   106                                                      
REMARK 465     SER A   107                                                      
REMARK 465     GLY A   108                                                      
REMARK 465     GLN A   109                                                      
REMARK 465     TYR A   110                                                      
REMARK 465     LYS A   111                                                      
REMARK 465     ASP A   112                                                      
REMARK 465     ASN A   113                                                      
REMARK 465     ILE A   114                                                      
REMARK 465     ARG A   115                                                      
REMARK 465     HIS A   116                                                      
REMARK 465     GLN B   375                                                      
REMARK 465     SER B   376                                                      
REMARK 465     THR B   377                                                      
REMARK 465     TYR B   378                                                      
REMARK 465     GLY E   103                                                      
REMARK 465     PRO E   104                                                      
REMARK 465     LEU E   105                                                      
REMARK 465     GLY E   106                                                      
REMARK 465     SER E   107                                                      
REMARK 465     GLY E   108                                                      
REMARK 465     GLN E   109                                                      
REMARK 465     TYR E   110                                                      
REMARK 465     LYS E   111                                                      
REMARK 465     ASP E   112                                                      
REMARK 465     ASN E   113                                                      
REMARK 465     ILE E   114                                                      
REMARK 465     ARG E   115                                                      
REMARK 465     HIS E   116                                                      
REMARK 465     GLN F   375                                                      
REMARK 465     SER F   376                                                      
REMARK 465     THR F   377                                                      
REMARK 465     TYR F   378                                                      
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    HOH A  1683     O    HOH A  1803              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS E   366     O    HOH A  1845     2555     2.12            
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    CYS A 119   CA  -  CB  -  SG  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ARG A 215   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 215   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    GLY A 346   N   -  CA  -  C   ANGL. DEV. = -23.4 DEGREES          
REMARK 500    CYS E 119   CA  -  CB  -  SG  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ARG E 215   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG E 215   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    THR E 363   N   -  CA  -  C   ANGL. DEV. = -22.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 152      -48.01   -135.71                                   
REMARK 500    THR A 197     -167.51   -120.87                                   
REMARK 500    ILE A 316     -159.45   -139.80                                   
REMARK 500    LYS A 344      106.13     86.30                                   
REMARK 500    THR A 363      -17.25     73.40                                   
REMARK 500    GLN A 365       48.10    -89.28                                   
REMARK 500    LYS B 370       47.06    -57.86                                   
REMARK 500    ARG E 152      -50.47   -133.97                                   
REMARK 500    THR E 197     -165.36   -119.51                                   
REMARK 500    SER E 340       77.52   -151.15                                   
REMARK 500    SER E 345      100.02     65.18                                   
REMARK 500    PRO E 347      109.91    -53.86                                   
REMARK 500    GLN E 361       75.47    -66.98                                   
REMARK 500    ALA E 362       81.58     94.45                                   
REMARK 500    THR E 363      -13.89   -168.57                                   
REMARK 500    GLN E 365       52.59    -98.25                                   
REMARK 500    LYS F 370       48.90    -96.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH E2657        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH E2725        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH E2726        DISTANCE =  7.32 ANGSTROMS                       
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 1501                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH E 2501                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1H3I   RELATED DB: PDB                                   
REMARK 900 APO PROTEIN                                                          
REMARK 900 RELATED ID: 1O9S   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH HISTONE H3 PEPTIDE                   
DBREF  1XQH A  108   366  UNP    Q8WTS6   SET7_HUMAN     108    366             
DBREF  1XQH E  108   366  UNP    Q8WTS6   SET7_HUMAN     108    366             
DBREF  1XQH B  369   377  UNP    P04637   P53_HUMAN      369    377             
DBREF  1XQH F  369   377  UNP    P04637   P53_HUMAN      369    377             
SEQADV 1XQH GLY A  103  UNP  Q8WTS6              CLONING ARTIFACT               
SEQADV 1XQH PRO A  104  UNP  Q8WTS6              CLONING ARTIFACT               
SEQADV 1XQH LEU A  105  UNP  Q8WTS6              CLONING ARTIFACT               
SEQADV 1XQH GLY A  106  UNP  Q8WTS6              CLONING ARTIFACT               
SEQADV 1XQH SER A  107  UNP  Q8WTS6              CLONING ARTIFACT               
SEQADV 1XQH GLY E  103  UNP  Q8WTS6              CLONING ARTIFACT               
SEQADV 1XQH PRO E  104  UNP  Q8WTS6              CLONING ARTIFACT               
SEQADV 1XQH LEU E  105  UNP  Q8WTS6              CLONING ARTIFACT               
SEQADV 1XQH GLY E  106  UNP  Q8WTS6              CLONING ARTIFACT               
SEQADV 1XQH SER E  107  UNP  Q8WTS6              CLONING ARTIFACT               
SEQADV 1XQH MLZ B  372  UNP  P04637    LYS   372 MODIFIED RESIDUE               
SEQADV 1XQH TYR B  378  UNP  P04637              CLONING ARTIFACT               
SEQADV 1XQH MLZ F  372  UNP  P04637    LYS   372 MODIFIED RESIDUE               
SEQADV 1XQH TYR F  378  UNP  P04637              CLONING ARTIFACT               
SEQRES   1 A  264  GLY PRO LEU GLY SER GLY GLN TYR LYS ASP ASN ILE ARG          
SEQRES   2 A  264  HIS GLY VAL CYS TRP ILE TYR TYR PRO ASP GLY GLY SER          
SEQRES   3 A  264  LEU VAL GLY GLU VAL ASN GLU ASP GLY GLU MET THR GLY          
SEQRES   4 A  264  GLU LYS ILE ALA TYR VAL TYR PRO ASP GLU ARG THR ALA          
SEQRES   5 A  264  LEU TYR GLY LYS PHE ILE ASP GLY GLU MET ILE GLU GLY          
SEQRES   6 A  264  LYS LEU ALA THR LEU MET SER THR GLU GLU GLY ARG PRO          
SEQRES   7 A  264  HIS PHE GLU LEU MET PRO GLY ASN SER VAL TYR HIS PHE          
SEQRES   8 A  264  ASP LYS SER THR SER SER CYS ILE SER THR ASN ALA LEU          
SEQRES   9 A  264  LEU PRO ASP PRO TYR GLU SER GLU ARG VAL TYR VAL ALA          
SEQRES  10 A  264  GLU SER LEU ILE SER SER ALA GLY GLU GLY LEU PHE SER          
SEQRES  11 A  264  LYS VAL ALA VAL GLY PRO ASN THR VAL MET SER PHE TYR          
SEQRES  12 A  264  ASN GLY VAL ARG ILE THR HIS GLN GLU VAL ASP SER ARG          
SEQRES  13 A  264  ASP TRP ALA LEU ASN GLY ASN THR LEU SER LEU ASP GLU          
SEQRES  14 A  264  GLU THR VAL ILE ASP VAL PRO GLU PRO TYR ASN HIS VAL          
SEQRES  15 A  264  SER LYS TYR CYS ALA SER LEU GLY HIS LYS ALA ASN HIS          
SEQRES  16 A  264  SER PHE THR PRO ASN CYS ILE TYR ASP MET PHE VAL HIS          
SEQRES  17 A  264  PRO ARG PHE GLY PRO ILE LYS CYS ILE ARG THR LEU ARG          
SEQRES  18 A  264  ALA VAL GLU ALA ASP GLU GLU LEU THR VAL ALA TYR GLY          
SEQRES  19 A  264  TYR ASP HIS SER PRO PRO GLY LYS SER GLY PRO GLU ALA          
SEQRES  20 A  264  PRO GLU TRP TYR GLN VAL GLU LEU LYS ALA PHE GLN ALA          
SEQRES  21 A  264  THR GLN GLN LYS                                              
SEQRES   1 B   10  LEU LYS SER MLZ LYS GLY GLN SER THR TYR                      
SEQRES   1 E  264  GLY PRO LEU GLY SER GLY GLN TYR LYS ASP ASN ILE ARG          
SEQRES   2 E  264  HIS GLY VAL CYS TRP ILE TYR TYR PRO ASP GLY GLY SER          
SEQRES   3 E  264  LEU VAL GLY GLU VAL ASN GLU ASP GLY GLU MET THR GLY          
SEQRES   4 E  264  GLU LYS ILE ALA TYR VAL TYR PRO ASP GLU ARG THR ALA          
SEQRES   5 E  264  LEU TYR GLY LYS PHE ILE ASP GLY GLU MET ILE GLU GLY          
SEQRES   6 E  264  LYS LEU ALA THR LEU MET SER THR GLU GLU GLY ARG PRO          
SEQRES   7 E  264  HIS PHE GLU LEU MET PRO GLY ASN SER VAL TYR HIS PHE          
SEQRES   8 E  264  ASP LYS SER THR SER SER CYS ILE SER THR ASN ALA LEU          
SEQRES   9 E  264  LEU PRO ASP PRO TYR GLU SER GLU ARG VAL TYR VAL ALA          
SEQRES  10 E  264  GLU SER LEU ILE SER SER ALA GLY GLU GLY LEU PHE SER          
SEQRES  11 E  264  LYS VAL ALA VAL GLY PRO ASN THR VAL MET SER PHE TYR          
SEQRES  12 E  264  ASN GLY VAL ARG ILE THR HIS GLN GLU VAL ASP SER ARG          
SEQRES  13 E  264  ASP TRP ALA LEU ASN GLY ASN THR LEU SER LEU ASP GLU          
SEQRES  14 E  264  GLU THR VAL ILE ASP VAL PRO GLU PRO TYR ASN HIS VAL          
SEQRES  15 E  264  SER LYS TYR CYS ALA SER LEU GLY HIS LYS ALA ASN HIS          
SEQRES  16 E  264  SER PHE THR PRO ASN CYS ILE TYR ASP MET PHE VAL HIS          
SEQRES  17 E  264  PRO ARG PHE GLY PRO ILE LYS CYS ILE ARG THR LEU ARG          
SEQRES  18 E  264  ALA VAL GLU ALA ASP GLU GLU LEU THR VAL ALA TYR GLY          
SEQRES  19 E  264  TYR ASP HIS SER PRO PRO GLY LYS SER GLY PRO GLU ALA          
SEQRES  20 E  264  PRO GLU TRP TYR GLN VAL GLU LEU LYS ALA PHE GLN ALA          
SEQRES  21 E  264  THR GLN GLN LYS                                              
SEQRES   1 F   10  LEU LYS SER MLZ LYS GLY GLN SER THR TYR                      
MODRES 1XQH MLZ B  372  LYS  N-METHYL-LYSINE                                    
MODRES 1XQH MLZ F  372  LYS  N-METHYL-LYSINE                                    
HET    MLZ  B 372      10                                                       
HET    MLZ  F 372      10                                                       
HET    SAH  A1501      26                                                       
HET    SAH  E2501      26                                                       
HETNAM     MLZ N-METHYL-LYSINE                                                  
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   2  MLZ    2(C7 H16 N2 O2)                                              
FORMUL   5  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL   7  HOH   *717(H2 O)                                                    
HELIX    1   1 ASP A  209  GLU A  214  1                                   6    
HELIX    2   2 THR A  251  ARG A  258  1                                   8    
HELIX    3   3 ASP A  259  ASN A  263  5                                   5    
HELIX    4   4 LEU A  291  ALA A  295  5                                   5    
HELIX    5   5 PRO A  350  ALA A  362  1                                  13    
HELIX    6   6 ASP E  209  GLU E  214  1                                   6    
HELIX    7   7 THR E  251  SER E  257  1                                   7    
HELIX    8   8 ASP E  259  ASN E  263  5                                   5    
HELIX    9   9 LEU E  291  ALA E  295  5                                   5    
HELIX   10  10 PRO E  350  GLN E  361  1                                  12    
SHEET    1   A12 ARG A 179  LEU A 184  0                                        
SHEET    2   A12 GLU A 163  GLU A 176 -1  N  SER A 174   O  HIS A 181           
SHEET    3   A12 THR A 153  ILE A 160 -1  N  TYR A 156   O  LYS A 168           
SHEET    4   A12 GLY A 141  VAL A 147 -1  N  ILE A 144   O  GLY A 157           
SHEET    5   A12 SER A 128  GLU A 132 -1  N  SER A 128   O  VAL A 147           
SHEET    6   A12 VAL A 118  TYR A 122 -1  N  ILE A 121   O  LEU A 129           
SHEET    7   A12 VAL E 118  TYR E 122 -1  O  VAL E 118   N  TYR A 122           
SHEET    8   A12 SER E 128  GLU E 132 -1  O  LEU E 129   N  ILE E 121           
SHEET    9   A12 GLY E 141  VAL E 147 -1  O  VAL E 147   N  SER E 128           
SHEET   10   A12 THR E 153  ILE E 160 -1  O  GLY E 157   N  ILE E 144           
SHEET   11   A12 GLU E 163  GLU E 176 -1  O  LYS E 168   N  TYR E 156           
SHEET   12   A12 ARG E 179  LEU E 184 -1  O  GLU E 183   N  THR E 171           
SHEET    1   B12 VAL A 190  TYR A 191  0                                        
SHEET    2   B12 GLU A 163  GLU A 176 -1  N  GLY A 167   O  TYR A 191           
SHEET    3   B12 THR A 153  ILE A 160 -1  N  TYR A 156   O  LYS A 168           
SHEET    4   B12 GLY A 141  VAL A 147 -1  N  ILE A 144   O  GLY A 157           
SHEET    5   B12 SER A 128  GLU A 132 -1  N  SER A 128   O  VAL A 147           
SHEET    6   B12 VAL A 118  TYR A 122 -1  N  ILE A 121   O  LEU A 129           
SHEET    7   B12 VAL E 118  TYR E 122 -1  O  VAL E 118   N  TYR A 122           
SHEET    8   B12 SER E 128  GLU E 132 -1  O  LEU E 129   N  ILE E 121           
SHEET    9   B12 GLY E 141  VAL E 147 -1  O  VAL E 147   N  SER E 128           
SHEET   10   B12 THR E 153  ILE E 160 -1  O  GLY E 157   N  ILE E 144           
SHEET   11   B12 GLU E 163  GLU E 176 -1  O  LYS E 168   N  TYR E 156           
SHEET   12   B12 VAL E 190  TYR E 191 -1  O  TYR E 191   N  GLY E 167           
SHEET    1   C 4 VAL A 216  GLU A 220  0                                        
SHEET    2   C 4 GLU A 228  SER A 232 -1  O  GLY A 229   N  ALA A 219           
SHEET    3   C 4 GLU A 330  VAL A 333 -1  O  LEU A 331   N  LEU A 230           
SHEET    4   C 4 ASN A 296  HIS A 297  1  N  ASN A 296   O  VAL A 333           
SHEET    1   D 3 VAL A 241  TYR A 245  0                                        
SHEET    2   D 3 GLY A 314  THR A 321 -1  O  ILE A 319   N  MET A 242           
SHEET    3   D 3 CYS A 303  HIS A 310 -1  N  PHE A 308   O  ILE A 316           
SHEET    1   E 3 VAL A 248  ILE A 250  0                                        
SHEET    2   E 3 VAL A 274  ASP A 276 -1  O  VAL A 274   N  ILE A 250           
SHEET    3   E 3 LEU A 267  SER A 268 -1  N  LEU A 267   O  ILE A 275           
SHEET    1   F 4 VAL E 216  GLU E 220  0                                        
SHEET    2   F 4 GLU E 228  SER E 232 -1  O  GLY E 229   N  ALA E 219           
SHEET    3   F 4 GLU E 330  VAL E 333 -1  O  LEU E 331   N  LEU E 230           
SHEET    4   F 4 ASN E 296  HIS E 297  1  N  ASN E 296   O  VAL E 333           
SHEET    1   G 3 VAL E 241  TYR E 245  0                                        
SHEET    2   G 3 GLY E 314  THR E 321 -1  O  ILE E 319   N  MET E 242           
SHEET    3   G 3 CYS E 303  HIS E 310 -1  N  PHE E 308   O  ILE E 316           
SHEET    1   H 3 VAL E 248  ILE E 250  0                                        
SHEET    2   H 3 VAL E 274  ASP E 276 -1  O  VAL E 274   N  ILE E 250           
SHEET    3   H 3 LEU E 267  SER E 268 -1  N  LEU E 267   O  ILE E 275           
LINK         C   SER B 371                 N   MLZ B 372     1555   1555  1.52  
LINK         C   MLZ B 372                 N   LYS B 373     1555   1555  1.57  
LINK         C   SER F 371                 N   MLZ F 372     1555   1555  1.48  
LINK         C   MLZ F 372                 N   LYS F 373     1555   1555  1.64  
CISPEP   1 GLU A  279    PRO A  280          0         1.36                     
CISPEP   2 GLU E  279    PRO E  280          0         1.48                     
SITE     1 AC1 19 ALA A 226  GLU A 228  ASN A 265  HIS A 293                    
SITE     2 AC1 19 LYS A 294  ASN A 296  HIS A 297  TYR A 335                    
SITE     3 AC1 19 TRP A 352  GLU A 356  HOH A1522  HOH A1526                    
SITE     4 AC1 19 HOH A1530  HOH A1535  HOH A1536  HOH A1621                    
SITE     5 AC1 19 HOH A1702  HOH A1709  MLZ B 372                               
SITE     1 AC2 21 ALA E 226  GLY E 227  GLU E 228  ASN E 265                    
SITE     2 AC2 21 HIS E 293  LYS E 294  ASN E 296  HIS E 297                    
SITE     3 AC2 21 TYR E 335  TRP E 352  GLU E 356  HOH E2523                    
SITE     4 AC2 21 HOH E2528  HOH E2532  HOH E2535  HOH E2540                    
SITE     5 AC2 21 HOH E2667  HOH E2687  HOH E2708  HOH E2757                    
SITE     6 AC2 21 MLZ F 372                                                     
CRYST1   40.374  103.123   67.165  90.00  90.04  90.00 P 1 21 1      4          
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      0.024768  0.000000  0.000017        0.00000                         
SCALE2      0.000000  0.009697  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014889        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system