GenomeNet

Database: PDB
Entry: 4E47
LinkDB: 4E47
Original site: 4E47 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       12-MAR-12   4E47              
TITLE     SET7/9 IN COMPLEX WITH INHIBITOR (R)-(3-(3-CYANOPHENYL)-1-OXO-1-      
TITLE    2 (PYRROLIDIN-1-YL)PROPAN-2-YL)-1,2,3,4-TETRAHYDROISOQUINOLINE-6-      
TITLE    3 SULFONAMIDE AND S-ADENOSYLMETHIONINE                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETD7;                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: SET DOMAIN (UNP RESIDUES 109-366);                         
COMPND   5 SYNONYM: SET7/9, HISTONE H3-K4 METHYLTRANSFERASE SETD7, H3-K4-HMTASE 
COMPND   6 SETD7, LYSINE N-METHYLTRANSFERASE 7, SET DOMAIN-CONTAINING PROTEIN 7;
COMPND   7 EC: 2.1.1.43;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SETD7, KIAA1717, KMT7, SET7, SET9;                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)ROSETTA2;                         
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHIS2                                     
KEYWDS    TERNARY COMPLEX, SET DOMAIN, METHYLTRANSFERASE, INHIBITOR, S-         
KEYWDS   2 ADENOSYLMETHIONINE, CHROMATIN REGULATOR, CHROMOSOMAL PROTEIN,        
KEYWDS   3 NUCLEUS, TRANSCRIPTION, TRANSCRIPTION REGULATION, TRANSFERASE,       
KEYWDS   4 STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE-TRANSFERASE         
KEYWDS   5 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.WALKER,H.OUYANG,A.DONG,P.FISH,A.COOK,D.BARSYTE,M.VEDADI,          
AUTHOR   2 J.TATLOCK,D.OWEN,M.BUNNAGE,C.BOUNTRA,J.WEIGELT,A.M.EDWARDS,          
AUTHOR   3 C.H.ARROWSMITH,P.J.BROWN,STRUCTURAL GENOMICS CONSORTIUM (SGC)        
REVDAT   2   15-NOV-17 4E47    1       REMARK                                   
REVDAT   1   28-MAR-12 4E47    0                                                
JRNL        AUTH   J.R.WALKER,H.OUYANG,A.DONG,P.FISH,A.COOK,D.BARSYTE,M.VEDADI, 
JRNL        AUTH 2 J.TATLOCK,D.OWEN,M.BUNNAGE,C.BOUNTRA,A.M.EDWARDS,            
JRNL        AUTH 3 C.H.ARROWSMITH,P.J.BROWN,                                    
JRNL        AUTH 4 STRUCTURAL GENOMICS CONSORTIUM (SGC)                         
JRNL        TITL   SETD7 IN COMPLEX WITH INHIBITOR AND SAM                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.8.0                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 72353                          
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)  : 0.162                          
REMARK   3   R VALUE            (WORKING SET)  : 0.160                          
REMARK   3   FREE R VALUE                      : 0.201                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.020                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3632                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.00                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.05                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4932                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1920                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 4678                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1898                   
REMARK   3   BIN FREE R VALUE                        : 0.2308                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.15                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 254                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7693                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 241                                     
REMARK   3   SOLVENT ATOMS            : 857                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.51                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.58410                                              
REMARK   3    B22 (A**2) : 0.92480                                              
REMARK   3    B33 (A**2) : -1.50890                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.195               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 8312   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 11362  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2728   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 200    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1224   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 8176   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1033   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 10087  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.02                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.62                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 15.62                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -26.3729   29.1695   18.7746           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0423 T22:   -0.0624                                    
REMARK   3     T33:   -0.0410 T12:   -0.0258                                    
REMARK   3     T13:    0.0192 T23:    0.0006                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8771 L22:    0.6907                                    
REMARK   3     L33:    0.9317 L12:    0.3855                                    
REMARK   3     L13:    0.2164 L23:    0.0499                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0207 S12:    0.0670 S13:   -0.0190                     
REMARK   3     S21:   -0.0405 S22:    0.0205 S23:   -0.0601                     
REMARK   3     S31:   -0.0208 S32:    0.0574 S33:    0.0003                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -54.7182   -2.4390   17.7293           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0517 T22:   -0.0656                                    
REMARK   3     T33:   -0.0510 T12:   -0.0222                                    
REMARK   3     T13:    0.0055 T23:    0.0182                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6944 L22:    0.8639                                    
REMARK   3     L33:    1.1524 L12:    0.3572                                    
REMARK   3     L13:   -0.0017 L23:    0.1102                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0155 S12:   -0.0458 S13:   -0.0739                     
REMARK   3     S21:   -0.0043 S22:    0.0065 S23:   -0.0435                     
REMARK   3     S31:    0.0698 S32:   -0.0228 S33:   -0.0220                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -30.3467   29.9449   54.0801           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0756 T22:   -0.0428                                    
REMARK   3     T33:   -0.0538 T12:   -0.0065                                    
REMARK   3     T13:    0.0141 T23:   -0.0023                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.7073 L22:    0.7774                                    
REMARK   3     L33:    1.4371 L12:   -0.1824                                    
REMARK   3     L13:    0.2441 L23:   -0.3200                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0500 S12:   -0.0541 S13:   -0.0355                     
REMARK   3     S21:   -0.0085 S22:    0.0780 S23:    0.0694                     
REMARK   3     S31:   -0.0016 S32:   -0.0979 S33:   -0.0280                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -5.7396   -3.1326   49.5789           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1276 T22:   -0.0327                                    
REMARK   3     T33:   -0.0351 T12:   -0.0046                                    
REMARK   3     T13:   -0.0017 T23:    0.0072                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8284 L22:    1.2908                                    
REMARK   3     L33:    1.6225 L12:   -0.4329                                    
REMARK   3     L13:    0.4160 L23:   -0.8667                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0047 S12:   -0.1714 S13:   -0.0396                     
REMARK   3     S21:   -0.0251 S22:    0.0679 S23:    0.1696                     
REMARK   3     S31:    0.0425 S32:   -0.1046 S33:   -0.0632                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4E47 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000071147.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-MAR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97932                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 72406                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 9.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.62700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3M53                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% PEG3350, 0.1 M TRIS, PH 8.0, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.43250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.43250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       58.67150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.89950            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       58.67150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.89950            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       68.43250            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       58.67150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.89950            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       68.43250            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       58.67150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.89950            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     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   339                                                      
REMARK 465     SER A   340                                                      
REMARK 465     PRO A   341                                                      
REMARK 465     PRO A   342                                                      
REMARK 465     GLY A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     SER A   345                                                      
REMARK 465     HIS A   369                                                      
REMARK 465     HIS A   370                                                      
REMARK 465     HIS A   371                                                      
REMARK 465     HIS A   372                                                      
REMARK 465     GLN B   109                                                      
REMARK 465     TYR B   110                                                      
REMARK 465     LYS B   111                                                      
REMARK 465     ASP B   112                                                      
REMARK 465     ASN B   113                                                      
REMARK 465     ILE B   114                                                      
REMARK 465     ARG B   115                                                      
REMARK 465     HIS B   339                                                      
REMARK 465     SER B   340                                                      
REMARK 465     PRO B   341                                                      
REMARK 465     PRO B   342                                                      
REMARK 465     GLY B   343                                                      
REMARK 465     LYS B   344                                                      
REMARK 465     SER B   345                                                      
REMARK 465     GLY B   346                                                      
REMARK 465     PRO B   347                                                      
REMARK 465     HIS B   370                                                      
REMARK 465     HIS B   371                                                      
REMARK 465     HIS B   372                                                      
REMARK 465     GLN C   109                                                      
REMARK 465     TYR C   110                                                      
REMARK 465     LYS C   111                                                      
REMARK 465     ASP C   112                                                      
REMARK 465     ASN C   113                                                      
REMARK 465     ILE C   114                                                      
REMARK 465     ARG C   115                                                      
REMARK 465     HIS C   116                                                      
REMARK 465     PRO C   341                                                      
REMARK 465     PRO C   342                                                      
REMARK 465     GLY C   343                                                      
REMARK 465     LYS C   344                                                      
REMARK 465     SER C   345                                                      
REMARK 465     GLY C   346                                                      
REMARK 465     PRO C   347                                                      
REMARK 465     GLU C   348                                                      
REMARK 465     HIS C   370                                                      
REMARK 465     HIS C   371                                                      
REMARK 465     HIS C   372                                                      
REMARK 465     GLN D   109                                                      
REMARK 465     TYR D   110                                                      
REMARK 465     LYS D   111                                                      
REMARK 465     ASP D   112                                                      
REMARK 465     ASN D   113                                                      
REMARK 465     ILE D   114                                                      
REMARK 465     ARG D   115                                                      
REMARK 465     PRO D   342                                                      
REMARK 465     GLY D   343                                                      
REMARK 465     LYS D   344                                                      
REMARK 465     SER D   345                                                      
REMARK 465     HIS D   370                                                      
REMARK 465     HIS D   371                                                      
REMARK 465     HIS D   372                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A 116    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 271    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 272    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 338    CG   OD1  OD2                                       
REMARK 470     GLU A 348    CG   CD   OE1  OE2                                  
REMARK 470     HIS B 116    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU B 135    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 272    CD   OE1  OE2                                       
REMARK 470     GLU B 348    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 358    CD   CE   NZ                                        
REMARK 470     GLU C 135    CD   OE1  OE2                                       
REMARK 470     ARG C 152    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU C 272    CD   OE1  OE2                                       
REMARK 470     LYS C 286    CG   CD   CE   NZ                                   
REMARK 470     GLN C 365    CD   OE1  NE2                                       
REMARK 470     HIS D 116    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU D 135    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 152    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP D 259    OD1  OD2                                            
REMARK 470     GLU D 351    OE1  OE2                                            
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      -50.36   -136.52                                   
REMARK 500    ASP A 194       48.08   -149.23                                   
REMARK 500    THR A 197     -167.68   -118.47                                   
REMARK 500    CYS A 288       16.69   -143.43                                   
REMARK 500    PRO A 347      109.69    -58.34                                   
REMARK 500    ARG B 152      -49.14   -134.71                                   
REMARK 500    SER B 225       18.23     59.09                                   
REMARK 500    CYS B 288       16.70   -148.94                                   
REMARK 500    ILE B 316     -159.20   -136.70                                   
REMARK 500    ARG C 152      -46.08   -140.54                                   
REMARK 500    ASP C 194       53.79   -143.34                                   
REMARK 500    THR C 197     -165.50   -122.33                                   
REMARK 500    ARG D 152      -53.45   -136.44                                   
REMARK 500    THR D 197     -164.66   -119.45                                   
REMARK 500    CYS D 288       14.73   -141.46                                   
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 SAM A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0N6 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM B 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0N6 B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM C 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0N6 C 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM D 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0N6 D 801                 
DBREF  4E47 A  109   366  UNP    Q8WTS6   SETD7_HUMAN    109    366             
DBREF  4E47 B  109   366  UNP    Q8WTS6   SETD7_HUMAN    109    366             
DBREF  4E47 C  109   366  UNP    Q8WTS6   SETD7_HUMAN    109    366             
DBREF  4E47 D  109   366  UNP    Q8WTS6   SETD7_HUMAN    109    366             
SEQADV 4E47 HIS A  367  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS A  368  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS A  369  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS A  370  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS A  371  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS A  372  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS B  367  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS B  368  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS B  369  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS B  370  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS B  371  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS B  372  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS C  367  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS C  368  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS C  369  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS C  370  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS C  371  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS C  372  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS D  367  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS D  368  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS D  369  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS D  370  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS D  371  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 4E47 HIS D  372  UNP  Q8WTS6              EXPRESSION TAG                 
SEQRES   1 A  264  GLN TYR LYS ASP ASN ILE ARG HIS GLY VAL CYS TRP ILE          
SEQRES   2 A  264  TYR TYR PRO ASP GLY GLY SER LEU VAL GLY GLU VAL ASN          
SEQRES   3 A  264  GLU ASP GLY GLU MET THR GLY GLU LYS ILE ALA TYR VAL          
SEQRES   4 A  264  TYR PRO ASP GLU ARG THR ALA LEU TYR GLY LYS PHE ILE          
SEQRES   5 A  264  ASP GLY GLU MET ILE GLU GLY LYS LEU ALA THR LEU MET          
SEQRES   6 A  264  SER THR GLU GLU GLY ARG PRO HIS PHE GLU LEU MET PRO          
SEQRES   7 A  264  GLY ASN SER VAL TYR HIS PHE ASP LYS SER THR SER SER          
SEQRES   8 A  264  CYS ILE SER THR ASN ALA LEU LEU PRO ASP PRO TYR GLU          
SEQRES   9 A  264  SER GLU ARG VAL TYR VAL ALA GLU SER LEU ILE SER SER          
SEQRES  10 A  264  ALA GLY GLU GLY LEU PHE SER LYS VAL ALA VAL GLY PRO          
SEQRES  11 A  264  ASN THR VAL MET SER PHE TYR ASN GLY VAL ARG ILE THR          
SEQRES  12 A  264  HIS GLN GLU VAL ASP SER ARG ASP TRP ALA LEU ASN GLY          
SEQRES  13 A  264  ASN THR LEU SER LEU ASP GLU GLU THR VAL ILE ASP VAL          
SEQRES  14 A  264  PRO GLU PRO TYR ASN HIS VAL SER LYS TYR CYS ALA SER          
SEQRES  15 A  264  LEU GLY HIS LYS ALA ASN HIS SER PHE THR PRO ASN CYS          
SEQRES  16 A  264  ILE TYR ASP MET PHE VAL HIS PRO ARG PHE GLY PRO ILE          
SEQRES  17 A  264  LYS CYS ILE ARG THR LEU ARG ALA VAL GLU ALA ASP GLU          
SEQRES  18 A  264  GLU LEU THR VAL ALA TYR GLY TYR ASP HIS SER PRO PRO          
SEQRES  19 A  264  GLY LYS SER GLY PRO GLU ALA PRO GLU TRP TYR GLN VAL          
SEQRES  20 A  264  GLU LEU LYS ALA PHE GLN ALA THR GLN GLN LYS HIS HIS          
SEQRES  21 A  264  HIS HIS HIS HIS                                              
SEQRES   1 B  264  GLN TYR LYS ASP ASN ILE ARG HIS GLY VAL CYS TRP ILE          
SEQRES   2 B  264  TYR TYR PRO ASP GLY GLY SER LEU VAL GLY GLU VAL ASN          
SEQRES   3 B  264  GLU ASP GLY GLU MET THR GLY GLU LYS ILE ALA TYR VAL          
SEQRES   4 B  264  TYR PRO ASP GLU ARG THR ALA LEU TYR GLY LYS PHE ILE          
SEQRES   5 B  264  ASP GLY GLU MET ILE GLU GLY LYS LEU ALA THR LEU MET          
SEQRES   6 B  264  SER THR GLU GLU GLY ARG PRO HIS PHE GLU LEU MET PRO          
SEQRES   7 B  264  GLY ASN SER VAL TYR HIS PHE ASP LYS SER THR SER SER          
SEQRES   8 B  264  CYS ILE SER THR ASN ALA LEU LEU PRO ASP PRO TYR GLU          
SEQRES   9 B  264  SER GLU ARG VAL TYR VAL ALA GLU SER LEU ILE SER SER          
SEQRES  10 B  264  ALA GLY GLU GLY LEU PHE SER LYS VAL ALA VAL GLY PRO          
SEQRES  11 B  264  ASN THR VAL MET SER PHE TYR ASN GLY VAL ARG ILE THR          
SEQRES  12 B  264  HIS GLN GLU VAL ASP SER ARG ASP TRP ALA LEU ASN GLY          
SEQRES  13 B  264  ASN THR LEU SER LEU ASP GLU GLU THR VAL ILE ASP VAL          
SEQRES  14 B  264  PRO GLU PRO TYR ASN HIS VAL SER LYS TYR CYS ALA SER          
SEQRES  15 B  264  LEU GLY HIS LYS ALA ASN HIS SER PHE THR PRO ASN CYS          
SEQRES  16 B  264  ILE TYR ASP MET PHE VAL HIS PRO ARG PHE GLY PRO ILE          
SEQRES  17 B  264  LYS CYS ILE ARG THR LEU ARG ALA VAL GLU ALA ASP GLU          
SEQRES  18 B  264  GLU LEU THR VAL ALA TYR GLY TYR ASP HIS SER PRO PRO          
SEQRES  19 B  264  GLY LYS SER GLY PRO GLU ALA PRO GLU TRP TYR GLN VAL          
SEQRES  20 B  264  GLU LEU LYS ALA PHE GLN ALA THR GLN GLN LYS HIS HIS          
SEQRES  21 B  264  HIS HIS HIS HIS                                              
SEQRES   1 C  264  GLN TYR LYS ASP ASN ILE ARG HIS GLY VAL CYS TRP ILE          
SEQRES   2 C  264  TYR TYR PRO ASP GLY GLY SER LEU VAL GLY GLU VAL ASN          
SEQRES   3 C  264  GLU ASP GLY GLU MET THR GLY GLU LYS ILE ALA TYR VAL          
SEQRES   4 C  264  TYR PRO ASP GLU ARG THR ALA LEU TYR GLY LYS PHE ILE          
SEQRES   5 C  264  ASP GLY GLU MET ILE GLU GLY LYS LEU ALA THR LEU MET          
SEQRES   6 C  264  SER THR GLU GLU GLY ARG PRO HIS PHE GLU LEU MET PRO          
SEQRES   7 C  264  GLY ASN SER VAL TYR HIS PHE ASP LYS SER THR SER SER          
SEQRES   8 C  264  CYS ILE SER THR ASN ALA LEU LEU PRO ASP PRO TYR GLU          
SEQRES   9 C  264  SER GLU ARG VAL TYR VAL ALA GLU SER LEU ILE SER SER          
SEQRES  10 C  264  ALA GLY GLU GLY LEU PHE SER LYS VAL ALA VAL GLY PRO          
SEQRES  11 C  264  ASN THR VAL MET SER PHE TYR ASN GLY VAL ARG ILE THR          
SEQRES  12 C  264  HIS GLN GLU VAL ASP SER ARG ASP TRP ALA LEU ASN GLY          
SEQRES  13 C  264  ASN THR LEU SER LEU ASP GLU GLU THR VAL ILE ASP VAL          
SEQRES  14 C  264  PRO GLU PRO TYR ASN HIS VAL SER LYS TYR CYS ALA SER          
SEQRES  15 C  264  LEU GLY HIS LYS ALA ASN HIS SER PHE THR PRO ASN CYS          
SEQRES  16 C  264  ILE TYR ASP MET PHE VAL HIS PRO ARG PHE GLY PRO ILE          
SEQRES  17 C  264  LYS CYS ILE ARG THR LEU ARG ALA VAL GLU ALA ASP GLU          
SEQRES  18 C  264  GLU LEU THR VAL ALA TYR GLY TYR ASP HIS SER PRO PRO          
SEQRES  19 C  264  GLY LYS SER GLY PRO GLU ALA PRO GLU TRP TYR GLN VAL          
SEQRES  20 C  264  GLU LEU LYS ALA PHE GLN ALA THR GLN GLN LYS HIS HIS          
SEQRES  21 C  264  HIS HIS HIS HIS                                              
SEQRES   1 D  264  GLN TYR LYS ASP ASN ILE ARG HIS GLY VAL CYS TRP ILE          
SEQRES   2 D  264  TYR TYR PRO ASP GLY GLY SER LEU VAL GLY GLU VAL ASN          
SEQRES   3 D  264  GLU ASP GLY GLU MET THR GLY GLU LYS ILE ALA TYR VAL          
SEQRES   4 D  264  TYR PRO ASP GLU ARG THR ALA LEU TYR GLY LYS PHE ILE          
SEQRES   5 D  264  ASP GLY GLU MET ILE GLU GLY LYS LEU ALA THR LEU MET          
SEQRES   6 D  264  SER THR GLU GLU GLY ARG PRO HIS PHE GLU LEU MET PRO          
SEQRES   7 D  264  GLY ASN SER VAL TYR HIS PHE ASP LYS SER THR SER SER          
SEQRES   8 D  264  CYS ILE SER THR ASN ALA LEU LEU PRO ASP PRO TYR GLU          
SEQRES   9 D  264  SER GLU ARG VAL TYR VAL ALA GLU SER LEU ILE SER SER          
SEQRES  10 D  264  ALA GLY GLU GLY LEU PHE SER LYS VAL ALA VAL GLY PRO          
SEQRES  11 D  264  ASN THR VAL MET SER PHE TYR ASN GLY VAL ARG ILE THR          
SEQRES  12 D  264  HIS GLN GLU VAL ASP SER ARG ASP TRP ALA LEU ASN GLY          
SEQRES  13 D  264  ASN THR LEU SER LEU ASP GLU GLU THR VAL ILE ASP VAL          
SEQRES  14 D  264  PRO GLU PRO TYR ASN HIS VAL SER LYS TYR CYS ALA SER          
SEQRES  15 D  264  LEU GLY HIS LYS ALA ASN HIS SER PHE THR PRO ASN CYS          
SEQRES  16 D  264  ILE TYR ASP MET PHE VAL HIS PRO ARG PHE GLY PRO ILE          
SEQRES  17 D  264  LYS CYS ILE ARG THR LEU ARG ALA VAL GLU ALA ASP GLU          
SEQRES  18 D  264  GLU LEU THR VAL ALA TYR GLY TYR ASP HIS SER PRO PRO          
SEQRES  19 D  264  GLY LYS SER GLY PRO GLU ALA PRO GLU TRP TYR GLN VAL          
SEQRES  20 D  264  GLU LEU LYS ALA PHE GLN ALA THR GLN GLN LYS HIS HIS          
SEQRES  21 D  264  HIS HIS HIS HIS                                              
HET    SAM  A 401      27                                                       
HET    0N6  A 402      31                                                       
HET    BME  A 403       4                                                       
HET    SO4  A 404       5                                                       
HET    SAM  B 800      27                                                       
HET    0N6  B 801      31                                                       
HET    SAM  C 800      27                                                       
HET    0N6  C 801      31                                                       
HET    SAM  D 800      27                                                       
HET    0N6  D 801      31                                                       
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     0N6 (R)-(3-(3-CYANOPHENYL)-1-OXO-1-(PYRROLIDIN-1-YL)PROPAN-          
HETNAM   2 0N6  2-YL)-1,2,3,4-TETRAHYDROISOQUINOLINE-6-SULFONAMIDE              
HETNAM     BME BETA-MERCAPTOETHANOL                                             
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  SAM    4(C15 H22 N6 O5 S)                                           
FORMUL   6  0N6    4(C23 H26 N4 O3 S)                                           
FORMUL   7  BME    C2 H6 O S                                                    
FORMUL   8  SO4    O4 S 2-                                                      
FORMUL  15  HOH   *857(H2 O)                                                    
HELIX    1   1 ASP A  209  GLU A  214  1                                   6    
HELIX    2   2 HIS A  252  ARG A  258  1                                   7    
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  GLN A  364  1                                  15    
HELIX    6   6 ASP B  209  ARG B  215  1                                   7    
HELIX    7   7 THR B  251  ARG B  258  1                                   8    
HELIX    8   8 ASP B  259  ASN B  263  5                                   5    
HELIX    9   9 LEU B  291  ALA B  295  5                                   5    
HELIX   10  10 PRO B  350  GLN B  364  1                                  15    
HELIX   11  11 ASP C  209  ARG C  215  1                                   7    
HELIX   12  12 THR C  251  SER C  257  1                                   7    
HELIX   13  13 ASP C  259  ASN C  263  5                                   5    
HELIX   14  14 LEU C  291  ALA C  295  5                                   5    
HELIX   15  15 PRO C  350  GLN C  364  1                                  15    
HELIX   16  16 ASP D  209  ARG D  215  1                                   7    
HELIX   17  17 THR D  251  SER D  257  1                                   7    
HELIX   18  18 ASP D  259  ASN D  263  5                                   5    
HELIX   19  19 LEU D  291  ALA D  295  5                                   5    
HELIX   20  20 PRO D  350  GLN D  364  1                                  15    
SHEET    1   A 6 CYS A 119  TYR A 122  0                                        
SHEET    2   A 6 SER A 128  GLY A 131 -1  O  LEU A 129   N  ILE A 121           
SHEET    3   A 6 GLY A 141  VAL A 147 -1  O  VAL A 147   N  SER A 128           
SHEET    4   A 6 THR A 153  ILE A 160 -1  O  GLY A 157   N  ILE A 144           
SHEET    5   A 6 GLU A 163  GLU A 176 -1  O  LYS A 168   N  TYR A 156           
SHEET    6   A 6 ARG A 179  LEU A 184 -1  O  HIS A 181   N  SER A 174           
SHEET    1   B 6 CYS A 119  TYR A 122  0                                        
SHEET    2   B 6 SER A 128  GLY A 131 -1  O  LEU A 129   N  ILE A 121           
SHEET    3   B 6 GLY A 141  VAL A 147 -1  O  VAL A 147   N  SER A 128           
SHEET    4   B 6 THR A 153  ILE A 160 -1  O  GLY A 157   N  ILE A 144           
SHEET    5   B 6 GLU A 163  GLU A 176 -1  O  LYS A 168   N  TYR A 156           
SHEET    6   B 6 VAL A 190  TYR A 191 -1  O  TYR A 191   N  GLY A 167           
SHEET    1   C 4 VAL A 216  GLU A 220  0                                        
SHEET    2   C 4 GLU A 228  SER A 232 -1  O  PHE A 231   N  TYR A 217           
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  LYS A 317   N  TYR A 245           
SHEET    3   D 3 CYS A 303  HIS A 310 -1  N  ILE A 304   O  ARG A 320           
SHEET    1   E 3 VAL A 248  THR A 251  0                                        
SHEET    2   E 3 THR A 273  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 6 VAL B 118  TYR B 122  0                                        
SHEET    2   F 6 SER B 128  GLU B 132 -1  O  LEU B 129   N  ILE B 121           
SHEET    3   F 6 GLY B 141  VAL B 147 -1  O  VAL B 147   N  SER B 128           
SHEET    4   F 6 THR B 153  ILE B 160 -1  O  GLY B 157   N  ILE B 144           
SHEET    5   F 6 GLU B 163  GLU B 176 -1  O  ALA B 170   N  ALA B 154           
SHEET    6   F 6 ARG B 179  LEU B 184 -1  O  HIS B 181   N  SER B 174           
SHEET    1   G 6 VAL B 118  TYR B 122  0                                        
SHEET    2   G 6 SER B 128  GLU B 132 -1  O  LEU B 129   N  ILE B 121           
SHEET    3   G 6 GLY B 141  VAL B 147 -1  O  VAL B 147   N  SER B 128           
SHEET    4   G 6 THR B 153  ILE B 160 -1  O  GLY B 157   N  ILE B 144           
SHEET    5   G 6 GLU B 163  GLU B 176 -1  O  ALA B 170   N  ALA B 154           
SHEET    6   G 6 VAL B 190  TYR B 191 -1  O  TYR B 191   N  GLY B 167           
SHEET    1   H 4 VAL B 216  GLU B 220  0                                        
SHEET    2   H 4 GLU B 228  SER B 232 -1  O  GLY B 229   N  ALA B 219           
SHEET    3   H 4 GLU B 330  VAL B 333 -1  O  LEU B 331   N  LEU B 230           
SHEET    4   H 4 ASN B 296  HIS B 297  1  N  ASN B 296   O  VAL B 333           
SHEET    1   I 3 VAL B 241  TYR B 245  0                                        
SHEET    2   I 3 GLY B 314  THR B 321 -1  O  ILE B 319   N  MET B 242           
SHEET    3   I 3 CYS B 303  HIS B 310 -1  N  PHE B 308   O  ILE B 316           
SHEET    1   J 3 VAL B 248  ILE B 250  0                                        
SHEET    2   J 3 VAL B 274  ASP B 276 -1  O  VAL B 274   N  ILE B 250           
SHEET    3   J 3 LEU B 267  SER B 268 -1  N  LEU B 267   O  ILE B 275           
SHEET    1   K 6 VAL C 118  TYR C 122  0                                        
SHEET    2   K 6 SER C 128  GLU C 132 -1  O  LEU C 129   N  ILE C 121           
SHEET    3   K 6 GLY C 141  VAL C 147 -1  O  ALA C 145   N  VAL C 130           
SHEET    4   K 6 THR C 153  ILE C 160 -1  O  GLY C 157   N  ILE C 144           
SHEET    5   K 6 GLU C 163  GLU C 176 -1  O  LYS C 168   N  TYR C 156           
SHEET    6   K 6 ARG C 179  LEU C 184 -1  O  GLU C 183   N  THR C 171           
SHEET    1   L 6 VAL C 118  TYR C 122  0                                        
SHEET    2   L 6 SER C 128  GLU C 132 -1  O  LEU C 129   N  ILE C 121           
SHEET    3   L 6 GLY C 141  VAL C 147 -1  O  ALA C 145   N  VAL C 130           
SHEET    4   L 6 THR C 153  ILE C 160 -1  O  GLY C 157   N  ILE C 144           
SHEET    5   L 6 GLU C 163  GLU C 176 -1  O  LYS C 168   N  TYR C 156           
SHEET    6   L 6 VAL C 190  TYR C 191 -1  O  TYR C 191   N  GLY C 167           
SHEET    1   M 4 VAL C 216  GLU C 220  0                                        
SHEET    2   M 4 GLU C 228  SER C 232 -1  O  PHE C 231   N  TYR C 217           
SHEET    3   M 4 GLU C 330  VAL C 333 -1  O  LEU C 331   N  LEU C 230           
SHEET    4   M 4 ASN C 296  HIS C 297  1  N  ASN C 296   O  VAL C 333           
SHEET    1   N 3 VAL C 241  TYR C 245  0                                        
SHEET    2   N 3 GLY C 314  THR C 321 -1  O  ILE C 319   N  MET C 242           
SHEET    3   N 3 CYS C 303  HIS C 310 -1  N  PHE C 308   O  ILE C 316           
SHEET    1   O 3 VAL C 248  ILE C 250  0                                        
SHEET    2   O 3 VAL C 274  ASP C 276 -1  O  VAL C 274   N  ILE C 250           
SHEET    3   O 3 LEU C 267  SER C 268 -1  N  LEU C 267   O  ILE C 275           
SHEET    1   P 6 VAL D 118  TYR D 122  0                                        
SHEET    2   P 6 SER D 128  GLU D 132 -1  O  LEU D 129   N  ILE D 121           
SHEET    3   P 6 GLY D 141  VAL D 147 -1  O  VAL D 147   N  SER D 128           
SHEET    4   P 6 THR D 153  ILE D 160 -1  O  GLY D 157   N  ILE D 144           
SHEET    5   P 6 GLU D 163  GLU D 176 -1  O  LYS D 168   N  TYR D 156           
SHEET    6   P 6 ARG D 179  LEU D 184 -1  O  HIS D 181   N  SER D 174           
SHEET    1   Q 6 VAL D 118  TYR D 122  0                                        
SHEET    2   Q 6 SER D 128  GLU D 132 -1  O  LEU D 129   N  ILE D 121           
SHEET    3   Q 6 GLY D 141  VAL D 147 -1  O  VAL D 147   N  SER D 128           
SHEET    4   Q 6 THR D 153  ILE D 160 -1  O  GLY D 157   N  ILE D 144           
SHEET    5   Q 6 GLU D 163  GLU D 176 -1  O  LYS D 168   N  TYR D 156           
SHEET    6   Q 6 VAL D 190  TYR D 191 -1  O  TYR D 191   N  GLY D 167           
SHEET    1   R 4 VAL D 216  GLU D 220  0                                        
SHEET    2   R 4 GLU D 228  SER D 232 -1  O  GLY D 229   N  ALA D 219           
SHEET    3   R 4 GLU D 330  VAL D 333 -1  O  LEU D 331   N  LEU D 230           
SHEET    4   R 4 ASN D 296  HIS D 297  1  N  ASN D 296   O  VAL D 333           
SHEET    1   S 3 VAL D 241  TYR D 245  0                                        
SHEET    2   S 3 GLY D 314  THR D 321 -1  O  ILE D 319   N  MET D 242           
SHEET    3   S 3 CYS D 303  HIS D 310 -1  N  PHE D 308   O  ILE D 316           
SHEET    1   T 3 VAL D 248  ILE D 250  0                                        
SHEET    2   T 3 VAL D 274  ASP D 276 -1  O  VAL D 274   N  ILE D 250           
SHEET    3   T 3 LEU D 267  SER D 268 -1  N  LEU D 267   O  ILE D 275           
LINK         SG  CYS A 200                 S2  BME A 403     1555   1555  1.81  
CISPEP   1 GLU A  279    PRO A  280          0         2.64                     
CISPEP   2 GLU B  279    PRO B  280          0         1.49                     
CISPEP   3 GLU C  279    PRO C  280          0         6.93                     
CISPEP   4 GLU D  279    PRO D  280          0         2.69                     
SITE     1 AC1 18 ALA A 226  GLU A 228  GLY A 264  ASN A 265                    
SITE     2 AC1 18 HIS A 293  LYS A 294  ALA A 295  ASN A 296                    
SITE     3 AC1 18 HIS A 297  TYR A 335  TRP A 352  HOH A 522                    
SITE     4 AC1 18 HOH A 530  HOH A 597  HOH A 598  HOH A 603                    
SITE     5 AC1 18 HOH A 625  HOH A 632                                          
SITE     1 AC2 13 TYR A 245  HIS A 252  ASP A 256  ASN A 263                    
SITE     2 AC2 13 GLY A 264  THR A 266  LEU A 267  SER A 268                    
SITE     3 AC2 13 TYR A 305  TYR A 335  GLY A 336  TYR A 337                    
SITE     4 AC2 13 HOH A 513                                                     
SITE     1 AC3  5 CYS A 200  SER A 202  HOH A 506  GLU D 351                    
SITE     2 AC3  5 GLN D 354                                                     
SITE     1 AC4  5 TYR A 122  HOH A 512  HOH A 741  TRP B 120                    
SITE     2 AC4  5 TYR B 122                                                     
SITE     1 AC5 19 ALA B 226  GLU B 228  GLY B 264  ASN B 265                    
SITE     2 AC5 19 HIS B 293  LYS B 294  ALA B 295  ASN B 296                    
SITE     3 AC5 19 HIS B 297  TYR B 335  TRP B 352  HOH B 930                    
SITE     4 AC5 19 HOH B 969  HOH B 972  HOH B 985  HOH B 988                    
SITE     5 AC5 19 HOH B1014  HOH B1038  HOH B1058                               
SITE     1 AC6 13 TYR B 245  HIS B 252  ASP B 256  ASN B 263                    
SITE     2 AC6 13 GLY B 264  THR B 266  LEU B 267  SER B 268                    
SITE     3 AC6 13 TYR B 305  TYR B 335  GLY B 336  TYR B 337                    
SITE     4 AC6 13 HOH B 966                                                     
SITE     1 AC7 19 ALA C 226  GLU C 228  GLY C 264  ASN C 265                    
SITE     2 AC7 19 HIS C 293  LYS C 294  ALA C 295  ASN C 296                    
SITE     3 AC7 19 HIS C 297  TYR C 335  TRP C 352  HOH C 937                    
SITE     4 AC7 19 HOH C 949  HOH C 962  HOH C 977  HOH C1015                    
SITE     5 AC7 19 HOH C1056  HOH C1057  HOH C1071                               
SITE     1 AC8 15 TYR C 245  HIS C 252  ASP C 256  TRP C 260                    
SITE     2 AC8 15 ASN C 263  GLY C 264  THR C 266  LEU C 267                    
SITE     3 AC8 15 SER C 268  TYR C 305  TYR C 335  GLY C 336                    
SITE     4 AC8 15 TYR C 337  HIS C 339  HOH C 989                               
SITE     1 AC9 17 ALA D 226  GLU D 228  GLY D 264  ASN D 265                    
SITE     2 AC9 17 HIS D 293  LYS D 294  ALA D 295  ASN D 296                    
SITE     3 AC9 17 HIS D 297  TYR D 335  TRP D 352  HOH D 910                    
SITE     4 AC9 17 HOH D 964  HOH D1011  HOH D1055  HOH D1059                    
SITE     5 AC9 17 HOH D1071                                                     
SITE     1 BC1 14 TYR D 245  HIS D 252  ASP D 256  TRP D 260                    
SITE     2 BC1 14 ASN D 263  GLY D 264  THR D 266  LEU D 267                    
SITE     3 BC1 14 SER D 268  TYR D 305  TYR D 335  GLY D 336                    
SITE     4 BC1 14 TYR D 337  HOH D 927                                          
CRYST1  117.343  133.799  136.865  90.00  90.00  90.00 C 2 2 21     32          
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      0.008522  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007474  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007306        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system