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Database: PDB
Entry: 2BQZ
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Original site: 2BQZ 
HEADER    TRANSFERASE                             28-APR-05   2BQZ              
TITLE     CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF THE HUMAN HISTONE           
TITLE    2 METHYLTRANSFERASE PR-SET7 (ALSO KNOWN AS SET8)                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SET8 PROTEIN;                                              
COMPND   3 CHAIN: A, E;                                                         
COMPND   4 FRAGMENT: SET-DOMAIN, RESIDUES 192-352;                              
COMPND   5 SYNONYM: HISTONE-LYSINE METHYLTRANSFERASE PR-SET7;                   
COMPND   6 EC: 2.1.1.43;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: HISTONE H4;                                                
COMPND  10 CHAIN: B, F;                                                         
COMPND  11 FRAGMENT: RESIDUES 17-25                                             
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;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 SYNTHETIC: YES;                                                      
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606                                                 
KEYWDS    HISTONE H4 METHYLTRANSFERSAE, LYSINE METHYLTRANSFERASE, SET           
KEYWDS   2 DOMAIN, TRANSFERASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.XIAO,C.JING,G.KELLY,P.A.WALKER,F.W.MUSKETT,T.A.FRENKIEL,            
AUTHOR   2 S.R.MARTIN,K.SARMA,D.REINBERG,S.J.GAMBLIN,J.R.WILSON                 
REVDAT   3   24-FEB-09 2BQZ    1       VERSN                                    
REVDAT   2   23-JUN-05 2BQZ    1       SOURCE JRNL                              
REVDAT   1   08-JUN-05 2BQZ    0                                                
JRNL        AUTH   B.XIAO,C.JING,G.KELLY,P.A.WALKER,F.W.MUSKETT,                
JRNL        AUTH 2 T.A.FRENKIEL,S.R.MARTIN,K.SARMA,D.REINBERG,                  
JRNL        AUTH 3 S.J.GAMBLIN,J.R.WILSON                                       
JRNL        TITL   SPECIFICITY AND MECHANISM OF THE HISTONE                     
JRNL        TITL 2 METHYLTRANSFERASE PR-SET7                                    
JRNL        REF    GENES DEV.                    V.  19  1444 2005              
JRNL        REFN                   ISSN 0890-9369                               
JRNL        PMID   15933069                                                     
JRNL        DOI    10.1101/GAD.1315905                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.5  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
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) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 50828                          
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) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2663                            
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) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3734                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2550                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 202                          
REMARK   3   BIN FREE R VALUE                    : 0.3090                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2754                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 613                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.79000                                              
REMARK   3    B22 (A**2) : -1.87000                                             
REMARK   3    B33 (A**2) : -0.24000                                             
REMARK   3    B12 (A**2) : 0.58000                                              
REMARK   3    B13 (A**2) : -0.10000                                             
REMARK   3    B23 (A**2) : 0.41000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.121         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.084         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.074         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.934         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.952                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2870 ; 0.011 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2568 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3840 ; 1.579 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5988 ; 0.722 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   334 ; 4.432 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   537 ;16.125 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   408 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3136 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   592 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   639 ; 0.322 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2633 ; 0.229 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):     1 ; 0.139 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   479 ; 0.211 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
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):    58 ; 0.267 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):   114 ; 0.352 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    46 ; 0.258 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
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):  1694 ; 0.893 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2696 ; 1.580 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1176 ; 2.112 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1144 ; 3.299 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   192        A   352                          
REMARK   3    RESIDUE RANGE :   B    17        B    26                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.8050   0.7050   1.9790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3989 T22:   0.5214                                     
REMARK   3      T33:   0.4322 T12:  -0.0297                                     
REMARK   3      T13:  -0.0190 T23:  -0.0244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5402 L22:   1.7726                                     
REMARK   3      L33:   1.5966 L12:   0.2290                                     
REMARK   3      L13:  -0.1745 L23:  -0.0687                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0472 S12:  -0.0387 S13:  -0.1173                       
REMARK   3      S21:  -0.0102 S22:   0.0294 S23:   0.0137                       
REMARK   3      S31:   0.0422 S32:  -0.0663 S33:   0.0177                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   192        E   352                          
REMARK   3    RESIDUE RANGE :   F    17        F    26                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.1550  26.9770  20.1650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4327 T22:   0.5326                                     
REMARK   3      T33:   0.4111 T12:  -0.0875                                     
REMARK   3      T13:   0.0116 T23:  -0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5824 L22:   1.6109                                     
REMARK   3      L33:   2.3888 L12:   0.2192                                     
REMARK   3      L13:   0.8310 L23:   0.7914                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0145 S12:  -0.0078 S13:   0.0454                       
REMARK   3      S21:   0.0666 S22:   0.0286 S23:  -0.1147                       
REMARK   3      S31:  -0.1309 S32:   0.1389 S33:  -0.0431                       
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 :   W     1        W   613                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.9830  12.2940  10.3700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1487 T22:   0.2792                                     
REMARK   3      T33:   0.1570 T12:  -0.0264                                     
REMARK   3      T13:  -0.0046 T23:  -0.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5180 L22:   0.8035                                     
REMARK   3      L33:   0.8133 L12:   0.3728                                     
REMARK   3      L13:   0.2167 L23:   0.3249                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0287 S12:  -0.0274 S13:  -0.0673                       
REMARK   3      S21:  -0.0098 S22:  -0.0156 S23:   0.0136                       
REMARK   3      S31:  -0.0115 S32:  -0.0037 S33:  -0.0132                       
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 2BQZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-APR-05.                  
REMARK 100 THE PDBE ID CODE IS EBI-23835.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63273                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.1                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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 300 DETAILS:THE DIMER IN THIS ENTRY IS FORMED BY THE                     
REMARK 300  COMPLEXOF CHAIN A WITH A PEPTIDE CHAIN B AND                        
REMARK 300 CHAIN E WITHPEPTIDE CHAIN F. CHAINS A AND E                          
REMARK 300 ARE MONOMERIC IN THEPHYSIOLOGICAL STATE.                             
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
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 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
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 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   SG   CYS A   305  -  O    HOH A  2238              2.14            
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                                                                      
REMARK 500   OE2  GLU A   197     NH2  ARG E   238     1455      2.12           
REMARK 500   NH2  ARG E   238     OE2  GLU A   197     1655      2.12           
REMARK 500   O    HOH A  2167     O    HOH A  2196     1456      2.14           
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    ASP A 265   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A 313   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG A 324   NE  -  CZ  -  NH2 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG E 192   CB  -  CA  -  C   ANGL. DEV. = -14.7 DEGREES          
REMARK 500    LYS E 193   N   -  CA  -  C   ANGL. DEV. = -25.1 DEGREES          
REMARK 500    ASP E 313   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASN F  25   N   -  CA  -  C   ANGL. DEV. =  16.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 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    SER A 194      172.63    -56.63                                   
REMARK 500    GLU A 215       65.38   -119.67                                   
REMARK 500    VAL A 242      -60.72   -107.09                                   
REMARK 500    ASP B  24      113.58     -4.43                                   
REMARK 500    ASN B  25       52.88   -145.37                                   
REMARK 500    LYS E 193     -155.81     60.97                                   
REMARK 500    VAL E 242      -60.43   -106.29                                   
REMARK 500    ASP F  24      -99.77    172.52                                   
REMARK 500    ASN F  25      164.89     64.31                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LYS E 193        47.3      L          L   OUTSIDE RANGE           
REMARK 500    ASN F  25        22.8      L          L   OUTSIDE RANGE           
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 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     SAH A 1354                                                       
REMARK 610     SAH E 1354                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A1354                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH E1354                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE OF CHAINS A AND E CORRESPONDS MOST CLOSELY TO           
REMARK 999 THE NCBI ENTRY NP_065115. THERE IS A SINGLE SEQUENCE DIFFERENCE      
REMARK 999 BETWEEN NP_065115 AND UNIPROT ENTRY Q86W83, AT POSITION 316,         
REMARK 999 WHICH IS GIVEN AS PRO IN THE NCBI ENTRY BUT ARG IN UNIPROT.          
DBREF  2BQZ A  192   352  UNP    Q86W83   Q86W83_HUMAN   192    352             
DBREF  2BQZ E  192   352  UNP    Q86W83   Q86W83_HUMAN   192    352             
DBREF  2BQZ B   17    25  UNP    P62805   H4_HUMAN        17     25             
DBREF  2BQZ B   26    26  PDB    2BQZ     2BQZ            26     26             
DBREF  2BQZ F   17    25  UNP    P62805   H4_HUMAN        17     25             
DBREF  2BQZ F   26    26  PDB    2BQZ     2BQZ            26     26             
SEQADV 2BQZ PRO A  316  UNP  Q86W83    ARG   316 CONFLICT SEE REMARK 999        
SEQADV 2BQZ PRO E  316  UNP  Q86W83    ARG   316 CONFLICT SEE REMARK 999        
SEQRES   1 A  161  ARG LYS SER LYS ALA GLU LEU GLN SER GLU GLU ARG LYS          
SEQRES   2 A  161  ARG ILE ASP GLU LEU ILE GLU SER GLY LYS GLU GLU GLY          
SEQRES   3 A  161  MET LYS ILE ASP LEU ILE ASP GLY LYS GLY ARG GLY VAL          
SEQRES   4 A  161  ILE ALA THR LYS GLN PHE SER ARG GLY ASP PHE VAL VAL          
SEQRES   5 A  161  GLU TYR HIS GLY ASP LEU ILE GLU ILE THR ASP ALA LYS          
SEQRES   6 A  161  LYS ARG GLU ALA LEU TYR ALA GLN ASP PRO SER THR GLY          
SEQRES   7 A  161  CYS TYR MET TYR TYR PHE GLN TYR LEU SER LYS THR TYR          
SEQRES   8 A  161  CYS VAL ASP ALA THR ARG GLU THR ASN ARG LEU GLY ARG          
SEQRES   9 A  161  LEU ILE ASN HIS SER LYS CYS GLY ASN CYS GLN THR LYS          
SEQRES  10 A  161  LEU HIS ASP ILE ASP GLY VAL PRO HIS LEU ILE LEU ILE          
SEQRES  11 A  161  ALA SER ARG ASP ILE ALA ALA GLY GLU GLU LEU LEU TYR          
SEQRES  12 A  161  ASP TYR GLY ASP ARG SER LYS ALA SER ILE GLU ALA HIS          
SEQRES  13 A  161  PRO TRP LEU LYS HIS                                          
SEQRES   1 B   10  ARG HIS ARG MLZ VAL LEU ARG ASP ASN TYR                      
SEQRES   1 E  161  ARG LYS SER LYS ALA GLU LEU GLN SER GLU GLU ARG LYS          
SEQRES   2 E  161  ARG ILE ASP GLU LEU ILE GLU SER GLY LYS GLU GLU GLY          
SEQRES   3 E  161  MET LYS ILE ASP LEU ILE ASP GLY LYS GLY ARG GLY VAL          
SEQRES   4 E  161  ILE ALA THR LYS GLN PHE SER ARG GLY ASP PHE VAL VAL          
SEQRES   5 E  161  GLU TYR HIS GLY ASP LEU ILE GLU ILE THR ASP ALA LYS          
SEQRES   6 E  161  LYS ARG GLU ALA LEU TYR ALA GLN ASP PRO SER THR GLY          
SEQRES   7 E  161  CYS TYR MET TYR TYR PHE GLN TYR LEU SER LYS THR TYR          
SEQRES   8 E  161  CYS VAL ASP ALA THR ARG GLU THR ASN ARG LEU GLY ARG          
SEQRES   9 E  161  LEU ILE ASN HIS SER LYS CYS GLY ASN CYS GLN THR LYS          
SEQRES  10 E  161  LEU HIS ASP ILE ASP GLY VAL PRO HIS LEU ILE LEU ILE          
SEQRES  11 E  161  ALA SER ARG ASP ILE ALA ALA GLY GLU GLU LEU LEU TYR          
SEQRES  12 E  161  ASP TYR GLY ASP ARG SER LYS ALA SER ILE GLU ALA HIS          
SEQRES  13 E  161  PRO TRP LEU LYS HIS                                          
SEQRES   1 F   10  ARG HIS ARG MLZ VAL LEU ARG ASP ASN TYR                      
MODRES 2BQZ MLZ B   20  LYS  N-METHYL-LYSINE                                    
MODRES 2BQZ MLZ F   20  LYS  N-METHYL-LYSINE                                    
HET    MLZ  B  20      10                                                       
HET    MLZ  F  20      10                                                       
HET    SAH  A1354      25                                                       
HET    SAH  E1354      25                                                       
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   *613(H2 O1)                                                   
HELIX    1   1 SER A  194  GLY A  213  1                                  20    
HELIX    2   2 ILE A  252  GLN A  264  1                                  13    
HELIX    3   3 LEU A  293  ILE A  297  5                                   5    
HELIX    4   4 SER A  340  HIS A  347  1                                   8    
HELIX    5   5 PRO A  348  HIS A  352  5                                   5    
HELIX    6   6 SER E  194  GLY E  213  1                                  20    
HELIX    7   7 ILE E  252  GLN E  264  1                                  13    
HELIX    8   8 LEU E  293  ILE E  297  5                                   5    
HELIX    9   9 SER E  340  HIS E  347  1                                   8    
HELIX   10  10 PRO E  348  HIS E  352  5                                   5    
SHEET    1  AA 2 MET A 218  ILE A 223  0                                        
SHEET    2  AA 2 GLY A 227  ALA A 232 -1  O  GLY A 227   N  ILE A 223           
SHEET    1  AB 3 PHE A 241  TYR A 245  0                                        
SHEET    2  AB 3 VAL A 315  ALA A 322 -1  O  LEU A 318   N  TYR A 245           
SHEET    3  AB 3 CYS A 305  ILE A 312 -1  O  GLN A 306   N  ILE A 321           
SHEET    1  AC 3 ASP A 248  GLU A 251  0                                        
SHEET    2  AC 3 LYS A 280  ASP A 285 -1  O  CYS A 283   N  ILE A 250           
SHEET    3  AC 3 MET A 272  TYR A 277 -1  O  TYR A 273   N  VAL A 284           
SHEET    1  AD 2 ASN A 298  HIS A 299  0                                        
SHEET    2  AD 2 LEU A 333  TYR A 334  1  N  TYR A 334   O  ASN A 298           
SHEET    1  EA 2 MET E 218  ILE E 223  0                                        
SHEET    2  EA 2 GLY E 227  ALA E 232 -1  O  GLY E 227   N  ILE E 223           
SHEET    1  EB 3 PHE E 241  GLU E 244  0                                        
SHEET    2  EB 3 VAL E 315  ALA E 322 -1  O  LEU E 320   N  VAL E 242           
SHEET    3  EB 3 CYS E 305  ILE E 312 -1  O  GLN E 306   N  ILE E 321           
SHEET    1  EC 3 ASP E 248  GLU E 251  0                                        
SHEET    2  EC 3 LYS E 280  ASP E 285 -1  O  CYS E 283   N  ILE E 250           
SHEET    3  EC 3 MET E 272  TYR E 277 -1  O  TYR E 273   N  VAL E 284           
SHEET    1  ED 2 ASN E 298  HIS E 299  0                                        
SHEET    2  ED 2 LEU E 333  TYR E 334  1  N  TYR E 334   O  ASN E 298           
LINK         C   ARG B  19                 N   MLZ B  20     1555   1555  1.34  
LINK         C   MLZ B  20                 N   VAL B  21     1555   1555  1.44  
LINK         C   ARG F  19                 N   MLZ F  20     1555   1555  1.31  
LINK         C   MLZ F  20                 N   VAL F  21     1555   1555  1.39  
SITE     1 AC1 16 GLY A 225  LYS A 226  ARG A 228  TYR A 271                    
SITE     2 AC1 16 ARG A 295  LEU A 296  ASN A 298  HIS A 299                    
SITE     3 AC1 16 TYR A 336  TRP A 349  HOH A2315  HOH A2317                    
SITE     4 AC1 16 HOH A2318  HIS B  18  MLZ B  20  HOH E2136                    
SITE     1 AC2 20 HOH A2159  ARG B  23  HOH B2012  GLY E 225                    
SITE     2 AC2 20 LYS E 226  ARG E 228  TYR E 271  ARG E 295                    
SITE     3 AC2 20 LEU E 296  ASN E 298  HIS E 299  TYR E 336                    
SITE     4 AC2 20 TRP E 349  HOH E2123  HOH E2245  HOH E2246                    
SITE     5 AC2 20 HOH E2247  HOH E2248  HIS F  18  MLZ F  20                    
CRYST1   42.179   46.322   51.998  64.74  86.66  90.61 P 1           2          
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      0.023708  0.000252 -0.001651        0.00000                         
SCALE2      0.000000  0.021589 -0.010227        0.00000                         
SCALE3      0.000000  0.000000  0.021316        0.00000                         
MTRIX1   1 -0.983220 -0.122620  0.135050       11.66670    1                    
MTRIX2   1 -0.047420 -0.543070 -0.838350       32.69479    1                    
MTRIX3   1  0.176140 -0.830690  0.528140       11.51827    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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