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Database: PDB
Entry: 5WW0
LinkDB: 5WW0
Original site: 5WW0 
HEADER    TRANSCRIPTION                           30-DEC-16   5WW0              
TITLE     CRYSTAL STRUCTURE OF SET7, A NOVEL HISTONE METHYLTRANSFERASE IN       
TITLE    2 SCHIZOSSACHAROMYCES POMBE                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SET DOMAIN-CONTAINING PROTEIN 7;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 1-145;                                        
COMPND   5 EC: 2.1.1.43;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE;                      
SOURCE   3 ORGANISM_COMMON: FISSION YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 284812;                                              
SOURCE   5 STRAIN: 972 / ATCC 24843;                                            
SOURCE   6 GENE: SET7, SPCC297.04C;                                             
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PTYB12                                    
KEYWDS    HISTONE, METHYTRANSFERASE, SCHIZOSACCHAROMYCES POMBE SET7,            
KEYWDS   2 EPIGENETIC, TRANSCRIPTION                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.E.H.F.MEVIUS,Y.SHEN,M.MORISHITA,B.CARROZZINI,R.CALIANDRO,E.DI       
AUTHOR   2 LUCCIO                                                               
REVDAT   2   17-JAN-18 5WW0    1       AUTHOR JRNL                              
REVDAT   1   06-DEC-17 5WW0    0                                                
JRNL        AUTH   D.E.H.F.MEVIUS,Y.SHEN,M.MORISHITA,B.CARROZZINI,R.CALIANDRO,  
JRNL        AUTH 2 E.DI LUCCIO                                                  
JRNL        TITL   TO BE PUBLISHED                                              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 18019                          
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) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 960                             
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1059                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 57                           
REMARK   3   BIN FREE R VALUE                    : 0.2680                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2013                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 199                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.14000                                             
REMARK   3    B22 (A**2) : -0.14000                                             
REMARK   3    B33 (A**2) : 0.45000                                              
REMARK   3    B12 (A**2) : -0.07000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.191         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.185         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.126         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.811         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2073 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1907 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2807 ; 1.799 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4392 ; 1.011 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   241 ; 7.037 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   109 ;35.057 ;23.670       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   359 ;14.498 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;12.454 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   291 ; 0.109 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2330 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   502 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):   970 ; 2.749 ; 2.618       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   969 ; 2.738 ; 2.616       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1209 ; 4.139 ; 3.906       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1210 ; 4.137 ; 3.908       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1103 ; 3.833 ; 3.187       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1095 ; 3.719 ; 3.175       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1586 ; 6.039 ; 4.561       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  2442 ; 8.547 ;22.312       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  2369 ; 8.422 ;21.781       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 RIDING   
REMARK   3   POSITIONS. SF FILE CONTAINS FRIEDEL PAIRS UNDER I/F_MINUS AND I/   
REMARK   3   F_PLUS COLUMNS.                                                    
REMARK   4                                                                      
REMARK   4 5WW0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300002485.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-MAY-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 7A (6B, 6C1)                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97933                            
REMARK 200  MONOCHROMATOR                  : DCM SI (111) CRYSTAL               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000 2.3.9                     
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000 2.3.9                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19879                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 10.60                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.80                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.82400                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: SIR2014 16.10                                         
REMARK 200 STARTING MODEL: 3KMA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS COLUMNS.    
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% ETHYLENE GLYCOL (CRYOPROTECTANT      
REMARK 280  FOR 101)250MM AMMONIUM SULFATE, 14% PEG 3.350, 1(PROTEIN):          
REMARK 280  1(BUFFER):0.4 RATIO OF 0.3M GLYCYL-GLYCYL-GLYCINE (~48MM FINAL      
REMARK 280  CONC), PROTEIN CONCENTRATION(4MG/ML), PROTEIN BUFFER(10MM TRIS      
REMARK 280  PH 7.5) TEMPERATURE(13), WELL VOLUME(500UL), 5UL OF HCL (12.1M)     
REMARK 280  WAS ADDED TO THE RESERVOIR DROP PRIOR TO DROP SETUP, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 286K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      172.71533            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       86.35767            
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      129.53650            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       43.17883            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      215.89417            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      172.71533            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       86.35767            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       43.17883            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      129.53650            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      215.89417            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ALA A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     MET A    -2                                                      
REMARK 465     THR A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A   125                                                      
REMARK 465     SER A   126                                                      
REMARK 465     SER A   127                                                      
REMARK 465     ALA A   128                                                      
REMARK 465     SER A   129                                                      
REMARK 465     ARG A   130                                                      
REMARK 465     ILE A   131                                                      
REMARK 465     SER A   132                                                      
REMARK 465     PRO A   133                                                      
REMARK 465     ASN A   134                                                      
REMARK 465     GLU A   135                                                      
REMARK 465     GLU A   136                                                      
REMARK 465     ASN A   137                                                      
REMARK 465     GLU A   138                                                      
REMARK 465     ASP A   139                                                      
REMARK 465     PHE A   140                                                      
REMARK 465     PRO A   141                                                      
REMARK 465     LEU A   142                                                      
REMARK 465     GLN A   143                                                      
REMARK 465     ASN A   144                                                      
REMARK 465     ILE A   145                                                      
REMARK 465     SER A   146                                                      
REMARK 465     LEU A   147                                                      
REMARK 465     LEU A   148                                                      
REMARK 465     GLU A   149                                                      
REMARK 465     THR A   150                                                      
REMARK 465     MET A   151                                                      
REMARK 465     TYR A   152                                                      
REMARK 465     PRO A   153                                                      
REMARK 465     TYR A   154                                                      
REMARK 465     ASP A   155                                                      
REMARK 465     VAL A   156                                                      
REMARK 465     PRO A   157                                                      
REMARK 465     ASP A   158                                                      
REMARK 465     TYR A   159                                                      
REMARK 465     ALA A   160                                                      
REMARK 465     ALA A   161                                                      
REMARK 465     PRO A   162                                                      
REMARK 465     GLY A   163                                                      
REMARK 465     TYR B   115                                                      
REMARK 465     GLY B   116                                                      
REMARK 465     ASP B   117                                                      
REMARK 465     HIS B   118                                                      
REMARK 465     LEU B   119                                                      
REMARK 465     TRP B   120                                                      
REMARK 465     PHE B   121                                                      
REMARK 465     GLU B   122                                                      
REMARK 465     ASP B   123                                                      
REMARK 465     GLU B   124                                                      
REMARK 465     ALA B   125                                                      
REMARK 465     SER B   126                                                      
REMARK 465     SER B   127                                                      
REMARK 465     ALA B   128                                                      
REMARK 465     SER B   129                                                      
REMARK 465     ARG B   130                                                      
REMARK 465     ILE B   131                                                      
REMARK 465     SER B   132                                                      
REMARK 465     PRO B   133                                                      
REMARK 465     ASN B   134                                                      
REMARK 465     GLU B   135                                                      
REMARK 465     GLU B   136                                                      
REMARK 465     ASN B   137                                                      
REMARK 465     GLU B   138                                                      
REMARK 465     ASP B   139                                                      
REMARK 465     PHE B   140                                                      
REMARK 465     PRO B   141                                                      
REMARK 465     LEU B   142                                                      
REMARK 465     GLN B   143                                                      
REMARK 465     ASN B   144                                                      
REMARK 465     ILE B   145                                                      
REMARK 465     SER B   146                                                      
REMARK 465     LEU B   147                                                      
REMARK 465     LEU B   148                                                      
REMARK 465     GLU B   149                                                      
REMARK 465     THR B   150                                                      
REMARK 465     MET B   151                                                      
REMARK 465     TYR B   152                                                      
REMARK 465     PRO B   153                                                      
REMARK 465     TYR B   154                                                      
REMARK 465     ASP B   155                                                      
REMARK 465     VAL B   156                                                      
REMARK 465     PRO B   157                                                      
REMARK 465     ASP B   158                                                      
REMARK 465     TYR B   159                                                      
REMARK 465     ALA B   160                                                      
REMARK 465     ALA B   161                                                      
REMARK 465     PRO B   162                                                      
REMARK 465     GLY B   163                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   359     O    HOH B   374              2.10            
REMARK 500   O    HOH A   355     O    HOH A   382              2.10            
REMARK 500   O    HOH B   344     O    HOH B   381              2.14            
REMARK 500   O    HOH A   340     O    HOH A   363              2.16            
REMARK 500   O    HOH A   315     O    HOH A   333              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ILE A  12   C     ARG A  13   N       0.197                       
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    VAL A  62   O   -  C   -  N   ANGL. DEV. = -14.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  50      -49.42   -136.53                                   
REMARK 500    HIS B  50      -53.52   -135.63                                   
REMARK 500    LEU B  72     -158.49    -83.88                                   
REMARK 500    HIS B  83       77.56   -111.05                                   
REMARK 500    ASN B  95       57.33     71.15                                   
REMARK 500    ASN B 108       -3.33     75.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 403        DISTANCE =  6.62 ANGSTROMS                       
REMARK 525    HOH B 396        DISTANCE =  6.32 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 201                 
DBREF  5WW0 A    1   145  UNP    Q9Y7Q6   SET7_SCHPO       1    145             
DBREF  5WW0 B    1   145  UNP    Q9Y7Q6   SET7_SCHPO       1    145             
SEQADV 5WW0 ALA A   -5  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 GLY A   -4  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 HIS A   -3  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 MET A   -2  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 THR A   -1  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 SER A    0  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 SER A  146  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 LEU A  147  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 LEU A  148  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 GLU A  149  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 THR A  150  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 MET A  151  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 TYR A  152  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 PRO A  153  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 TYR A  154  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 ASP A  155  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 VAL A  156  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 PRO A  157  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 ASP A  158  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 TYR A  159  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 ALA A  160  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 ALA A  161  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 PRO A  162  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 GLY A  163  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 ALA B   -5  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 GLY B   -4  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 HIS B   -3  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 MET B   -2  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 THR B   -1  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 SER B    0  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 SER B  146  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 LEU B  147  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 LEU B  148  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 GLU B  149  UNP  Q9Y7Q6              CLONING SITE RESIDUE           
SEQADV 5WW0 THR B  150  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 MET B  151  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 TYR B  152  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 PRO B  153  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 TYR B  154  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 ASP B  155  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 VAL B  156  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 PRO B  157  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 ASP B  158  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 TYR B  159  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 ALA B  160  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 ALA B  161  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 PRO B  162  UNP  Q9Y7Q6              DETECTION TAG                  
SEQADV 5WW0 GLY B  163  UNP  Q9Y7Q6              DETECTION TAG                  
SEQRES   1 A  169  ALA GLY HIS MET THR SER MET ARG ILE PRO VAL ILE ARG          
SEQRES   2 A  169  SER PRO LEU GLU ILE ARG ASP THR GLU ARG LYS GLY ARG          
SEQRES   3 A  169  GLY VAL PHE ALA LEU GLU PRO ILE PRO ALA GLN THR CYS          
SEQRES   4 A  169  ILE GLU ILE SER PRO VAL LEU MET PHE SER LYS GLU GLU          
SEQRES   5 A  169  TYR GLU GLN HIS GLY GLN TYR THR VAL LEU ASN GLU TYR          
SEQRES   6 A  169  THR TYR VAL TRP SER GLU GLY LYS GLN GLY LEU ALA LEU          
SEQRES   7 A  169  GLY LEU GLY SER MET PHE ASN HIS ASP ARG HIS PRO ASN          
SEQRES   8 A  169  VAL TYR TRP LYS LYS ASP ASN ARG ASN ASN TYR ILE SER          
SEQRES   9 A  169  TYR TYR THR LEU ARG GLU ILE LYS THR ASN GLU GLU LEU          
SEQRES  10 A  169  CYS ILE SER TYR GLY ASP HIS LEU TRP PHE GLU ASP GLU          
SEQRES  11 A  169  ALA SER SER ALA SER ARG ILE SER PRO ASN GLU GLU ASN          
SEQRES  12 A  169  GLU ASP PHE PRO LEU GLN ASN ILE SER LEU LEU GLU THR          
SEQRES  13 A  169  MET TYR PRO TYR ASP VAL PRO ASP TYR ALA ALA PRO GLY          
SEQRES   1 B  169  ALA GLY HIS MET THR SER MET ARG ILE PRO VAL ILE ARG          
SEQRES   2 B  169  SER PRO LEU GLU ILE ARG ASP THR GLU ARG LYS GLY ARG          
SEQRES   3 B  169  GLY VAL PHE ALA LEU GLU PRO ILE PRO ALA GLN THR CYS          
SEQRES   4 B  169  ILE GLU ILE SER PRO VAL LEU MET PHE SER LYS GLU GLU          
SEQRES   5 B  169  TYR GLU GLN HIS GLY GLN TYR THR VAL LEU ASN GLU TYR          
SEQRES   6 B  169  THR TYR VAL TRP SER GLU GLY LYS GLN GLY LEU ALA LEU          
SEQRES   7 B  169  GLY LEU GLY SER MET PHE ASN HIS ASP ARG HIS PRO ASN          
SEQRES   8 B  169  VAL TYR TRP LYS LYS ASP ASN ARG ASN ASN TYR ILE SER          
SEQRES   9 B  169  TYR TYR THR LEU ARG GLU ILE LYS THR ASN GLU GLU LEU          
SEQRES  10 B  169  CYS ILE SER TYR GLY ASP HIS LEU TRP PHE GLU ASP GLU          
SEQRES  11 B  169  ALA SER SER ALA SER ARG ILE SER PRO ASN GLU GLU ASN          
SEQRES  12 B  169  GLU ASP PHE PRO LEU GLN ASN ILE SER LEU LEU GLU THR          
SEQRES  13 B  169  MET TYR PRO TYR ASP VAL PRO ASP TYR ALA ALA PRO GLY          
HET    SO4  A 201       5                                                       
HET    SO4  B 201       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  HOH   *199(H2 O)                                                    
HELIX    1 AA1 SER A   43  HIS A   50  1                                   8    
HELIX    2 AA2 GLY A   51  TYR A   59  5                                   9    
HELIX    3 AA3 SER A   64  GLY A   66  5                                   3    
HELIX    4 AA4 LEU A   74  PHE A   78  5                                   5    
HELIX    5 AA5 SER B   43  HIS B   50  1                                   8    
HELIX    6 AA6 GLY B   51  TYR B   59  5                                   9    
HELIX    7 AA7 SER B   64  GLY B   66  5                                   3    
SHEET    1 AA1 5 ILE A   3  PRO A   4  0                                        
SHEET    2 AA1 5 LEU B  10  THR B  15 -1  O  ILE B  12   N  ILE A   3           
SHEET    3 AA1 5 GLY B  19  ALA B  24 -1  O  PHE B  23   N  GLU B  11           
SHEET    4 AA1 5 GLU B 110  ILE B 113 -1  O  LEU B 111   N  VAL B  22           
SHEET    5 AA1 5 ASN B  79  HIS B  80  1  N  ASN B  79   O  ILE B 113           
SHEET    1 AA2 5 ASN A  79  HIS A  80  0                                        
SHEET    2 AA2 5 GLU A 110  ILE A 113  1  O  ILE A 113   N  ASN A  79           
SHEET    3 AA2 5 GLY A  19  ALA A  24 -1  N  VAL A  22   O  LEU A 111           
SHEET    4 AA2 5 LEU A  10  THR A  15 -1  N  GLU A  11   O  PHE A  23           
SHEET    5 AA2 5 SER B   0  PRO B   4 -1  O  ILE B   3   N  ILE A  12           
SHEET    1 AA3 5 TYR A  61  VAL A  62  0                                        
SHEET    2 AA3 5 GLN A  68  ALA A  71 -1  O  GLY A  69   N  TYR A  61           
SHEET    3 AA3 5 CYS A  33  PHE A  42 -1  N  PHE A  42   O  GLN A  68           
SHEET    4 AA3 5 TYR A  96  THR A 101 -1  O  ILE A  97   N  SER A  37           
SHEET    5 AA3 5 VAL A  86  ASP A  91 -1  N  ASP A  91   O  TYR A  96           
SHEET    1 AA4 5 TYR B  61  VAL B  62  0                                        
SHEET    2 AA4 5 GLN B  68  ALA B  71 -1  O  GLY B  69   N  TYR B  61           
SHEET    3 AA4 5 CYS B  33  PHE B  42 -1  N  PHE B  42   O  GLN B  68           
SHEET    4 AA4 5 TYR B  96  THR B 101 -1  O  ILE B  97   N  SER B  37           
SHEET    5 AA4 5 VAL B  86  ASP B  91 -1  N  ASP B  91   O  TYR B  96           
SITE     1 AC1  6 GLN A  52  TYR A  87  TRP A 120  HOH A 306                    
SITE     2 AC1  6 HOH A 309  HOH A 334                                          
SITE     1 AC2  7 ALA B  -5  LYS B  18  GLY B  19  ARG B  20                    
SITE     2 AC2  7 TYR B  59  HOH B 301  HOH B 345                               
CRYST1   66.119   66.119  259.073  90.00  90.00 120.00 P 65 2 2     24          
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      0.015124  0.008732  0.000000        0.00000                         
SCALE2      0.000000  0.017464  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003860        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system