GenomeNet

Database: PDB
Entry: 5KCO
LinkDB: 5KCO
Original site: 5KCO 
HEADER    TRANSFERASE                             06-JUN-16   5KCO              
TITLE     SETDB1 IN COMPLEX WITH AN EARLY STAGE, LOW AFFINITY FRAGMENT CANDIDATE
TITLE    2 MODELLED AT REDUCED OCCUPANCY                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETDB1;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 196-403;                                      
COMPND   5 SYNONYM: ERG-ASSOCIATED PROTEIN WITH SET DOMAIN,ESET,HISTONE H3-K9   
COMPND   6 METHYLTRANSFERASE 4,H3-K9-HMTASE 4,LYSINE N-METHYLTRANSFERASE 1E,SET 
COMPND   7 DOMAIN BIFURCATED 1;                                                 
COMPND   8 EC: 2.1.1.43;                                                        
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SETDB1, KIAA0067, KMT1E;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) CODON PLUS;                     
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28-MHL                                 
KEYWDS    FRAGMENT SCREENING, DIAMOND I04-1 XCHEM, PANDDA, STRUCTURAL GENOMICS, 
KEYWDS   2 STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.TEMPEL,R.J.HARDING,P.MADER,E.DOBROVETSKY,J.R.WALKER,P.J.BROWN,      
AUTHOR   2 M.SCHAPIRA,P.COLLINS,N.PEARCE,J.BRANDAO-NETO,A.DOUANGAMATH,F.VON     
AUTHOR   3 DELFT,C.BOUNTRA,C.H.ARROWSMITH,A.M.EDWARDS,V.SANTHAKUMAR,STRUCTURAL  
AUTHOR   4 GENOMICS CONSORTIUM (SGC)                                            
REVDAT   2   27-SEP-23 5KCO    1       REMARK                                   
REVDAT   1   27-JUL-16 5KCO    0                                                
JRNL        AUTH   W.TEMPEL,R.J.HARDING,P.MADER,E.DOBROVETSKY,J.R.WALKER,       
JRNL        AUTH 2 P.J.BROWN,M.SCHAPIRA,C.H.ARROWSMITH,A.M.EDWARDS,             
JRNL        AUTH 3 S.SANTHAKUMAR,STRUCTURAL GENOMICS CONSORTIUM (SGC)           
JRNL        TITL   SETDB1 IN COMPLEX WITH AN EARLY STAGE, LOW AFFINITY FRAGMENT 
JRNL        TITL 2 CANDIDATE MODELLED AT REDUCED OCCUPANCY                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.47 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0151                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.47                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 41091                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2204                            
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) : 1.47                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.51                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2907                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.18                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2980                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 156                          
REMARK   3   BIN FREE R VALUE                    : 0.3190                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1711                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 81                                      
REMARK   3   SOLVENT ATOMS            : 143                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.63                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.90000                                              
REMARK   3    B22 (A**2) : -0.86000                                             
REMARK   3    B33 (A**2) : -0.04000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.068         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.071         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.052         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.422         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1882 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1780 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2568 ; 1.761 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4094 ; 1.008 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   234 ; 6.744 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    83 ;28.206 ;22.530       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   326 ;10.409 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;16.620 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   278 ; 0.118 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2135 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   454 ; 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):   880 ; 2.347 ; 1.865       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   881 ; 2.346 ; 1.865       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1110 ; 3.305 ; 2.790       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : MASK                                                 
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: USERS OF THIS CRYSTAL STRUCTURE: VERIFY   
REMARK   3  OUR INTEPRETION OF THE ELECTRON DENSITY. AMPLITUDES AND UNMERGED    
REMARK   3  INTENSITIES ARE INCLUDED WITH THIS DEPOSITION. DIFFRACTION          
REMARK   3  IMAGES WILL BE DEPOSITED IN A PUBLIC REPOSITORY. GEOMETRY           
REMARK   3  RESTRAINTS FOR THE FRAGMENT CANDIDATE WERE PREPARED WITH GRADE.     
REMARK   3  SOME OCCUPANCIES WERE REFINED WITH PHENIX SOFTWARE. AMBIGUOUS       
REMARK   3  DIFFERENCE DENSITY SUGGESTS MORE THAN ONE MAIN CHAIN                
REMARK   3  CONFORMATION FOR RESIDUES 235..239.                                 
REMARK   4                                                                      
REMARK   4 5KCO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000222007.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.92819                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.26                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43355                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.470                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.47                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.44500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 3DLM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG-3350, 0.2M LITHIUM SULFATE,      
REMARK 280  0.1M BIS-TRIS. TRYPSIN HAD BEEN ADDED TO THE PROTEIN STOCK          
REMARK 280  SOLUTION., PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE       
REMARK 280  291K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       27.88600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.26100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.88050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       35.26100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.88600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.88050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   179                                                      
REMARK 465     HIS A   180                                                      
REMARK 465     HIS A   181                                                      
REMARK 465     HIS A   182                                                      
REMARK 465     HIS A   183                                                      
REMARK 465     HIS A   184                                                      
REMARK 465     HIS A   185                                                      
REMARK 465     SER A   186                                                      
REMARK 465     SER A   187                                                      
REMARK 465     GLY A   188                                                      
REMARK 465     ARG A   189                                                      
REMARK 465     LYS A   402                                                      
REMARK 465     THR A   403                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 215    CD   CE   NZ                                        
REMARK 470     LYS A 233    NZ                                                  
REMARK 470     ASN A 236    CG   OD1  ND2                                       
REMARK 470     LYS A 237    CG   CD   CE   NZ                                   
REMARK 470     LYS A 239    NZ                                                  
REMARK 470     LYS A 257    CG   CD   CE   NZ                                   
REMARK 470     LYS A 267    CD   CE   NZ                                        
REMARK 470     LYS A 269    CD   CE   NZ                                        
REMARK 470     LYS A 288    CE   NZ                                             
REMARK 470     LYS A 355    CE   NZ                                             
REMARK 470     ASP A 381    CG   OD1  OD2                                       
REMARK 470     MET A 401    C    O    CB   CG   SD   CE                         
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    GLU A 283   CD    GLU A 283   OE1     0.067                       
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    ARG A 315   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 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    SER A 201       -8.81     90.33                                   
REMARK 500    SER A 201      -10.98     92.66                                   
REMARK 500    ASN A 236       51.31   -116.12                                   
REMARK 500    LYS A 237     -171.44   -175.48                                   
REMARK 500    ASP A 250       51.83    -95.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6RO A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 551                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 552                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 553                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5KCH   RELATED DB: PDB                                   
DBREF  5KCO A  196   403  UNP    Q15047   SETB1_HUMAN    196    403             
SEQADV 5KCO MET A  179  UNP  Q15047              INITIATING METHIONINE          
SEQADV 5KCO HIS A  180  UNP  Q15047              EXPRESSION TAG                 
SEQADV 5KCO HIS A  181  UNP  Q15047              EXPRESSION TAG                 
SEQADV 5KCO HIS A  182  UNP  Q15047              EXPRESSION TAG                 
SEQADV 5KCO HIS A  183  UNP  Q15047              EXPRESSION TAG                 
SEQADV 5KCO HIS A  184  UNP  Q15047              EXPRESSION TAG                 
SEQADV 5KCO HIS A  185  UNP  Q15047              EXPRESSION TAG                 
SEQADV 5KCO SER A  186  UNP  Q15047              EXPRESSION TAG                 
SEQADV 5KCO SER A  187  UNP  Q15047              EXPRESSION TAG                 
SEQADV 5KCO GLY A  188  UNP  Q15047              EXPRESSION TAG                 
SEQADV 5KCO ARG A  189  UNP  Q15047              EXPRESSION TAG                 
SEQADV 5KCO GLU A  190  UNP  Q15047              EXPRESSION TAG                 
SEQADV 5KCO ASN A  191  UNP  Q15047              EXPRESSION TAG                 
SEQADV 5KCO LEU A  192  UNP  Q15047              EXPRESSION TAG                 
SEQADV 5KCO TYR A  193  UNP  Q15047              EXPRESSION TAG                 
SEQADV 5KCO PHE A  194  UNP  Q15047              EXPRESSION TAG                 
SEQADV 5KCO GLN A  195  UNP  Q15047              EXPRESSION TAG                 
SEQRES   1 A  225  MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN          
SEQRES   2 A  225  LEU TYR PHE GLN GLY ASP LEU ILE VAL SER MET ARG ILE          
SEQRES   3 A  225  LEU GLY LYS LYS ARG THR LYS THR TRP HIS LYS GLY THR          
SEQRES   4 A  225  LEU ILE ALA ILE GLN THR VAL GLY PRO GLY LYS LYS TYR          
SEQRES   5 A  225  LYS VAL LYS PHE ASP ASN LYS GLY LYS SER LEU LEU SER          
SEQRES   6 A  225  GLY ASN HIS ILE ALA TYR ASP TYR HIS PRO PRO ALA ASP          
SEQRES   7 A  225  LYS LEU TYR VAL GLY SER ARG VAL VAL ALA LYS TYR LYS          
SEQRES   8 A  225  ASP GLY ASN GLN VAL TRP LEU TYR ALA GLY ILE VAL ALA          
SEQRES   9 A  225  GLU THR PRO ASN VAL LYS ASN LYS LEU ARG PHE LEU ILE          
SEQRES  10 A  225  PHE PHE ASP ASP GLY TYR ALA SER TYR VAL THR GLN SER          
SEQRES  11 A  225  GLU LEU TYR PRO ILE CYS ARG PRO LEU LYS LYS THR TRP          
SEQRES  12 A  225  GLU ASP ILE GLU ASP ILE SER CYS ARG ASP PHE ILE GLU          
SEQRES  13 A  225  GLU TYR VAL THR ALA TYR PRO ASN ARG PRO MET VAL LEU          
SEQRES  14 A  225  LEU LYS SER GLY GLN LEU ILE LYS THR GLU TRP GLU GLY          
SEQRES  15 A  225  THR TRP TRP LYS SER ARG VAL GLU GLU VAL ASP GLY SER          
SEQRES  16 A  225  LEU VAL ARG ILE LEU PHE LEU ASP ASP LYS ARG CYS GLU          
SEQRES  17 A  225  TRP ILE TYR ARG GLY SER THR ARG LEU GLU PRO MET PHE          
SEQRES  18 A  225  SER MET LYS THR                                              
HET    SO4  A 501       5                                                       
HET    SO4  A 502       5                                                       
HET    6RO  A 503      12                                                       
HET    UNX  A 504       1                                                       
HET    UNX  A 505       1                                                       
HET    UNX  A 506       1                                                       
HET    UNX  A 507       1                                                       
HET    UNX  A 508       1                                                       
HET    UNX  A 509       1                                                       
HET    UNX  A 510       1                                                       
HET    UNX  A 511       1                                                       
HET    UNX  A 512       1                                                       
HET    UNX  A 513       1                                                       
HET    UNX  A 514       1                                                       
HET    UNX  A 515       1                                                       
HET    UNX  A 516       1                                                       
HET    UNX  A 517       1                                                       
HET    UNX  A 518       1                                                       
HET    UNX  A 519       1                                                       
HET    UNX  A 520       1                                                       
HET    UNX  A 521       1                                                       
HET    UNX  A 522       1                                                       
HET    UNX  A 523       1                                                       
HET    UNX  A 524       1                                                       
HET    UNX  A 525       1                                                       
HET    UNX  A 526       1                                                       
HET    UNX  A 527       1                                                       
HET    UNX  A 528       1                                                       
HET    UNX  A 529       1                                                       
HET    UNX  A 530       1                                                       
HET    UNX  A 531       1                                                       
HET    UNX  A 532       1                                                       
HET    UNX  A 533       1                                                       
HET    UNX  A 534       1                                                       
HET    UNX  A 535       1                                                       
HET    UNX  A 536       1                                                       
HET    UNX  A 537       1                                                       
HET    UNX  A 538       1                                                       
HET    UNX  A 539       1                                                       
HET    UNX  A 540       1                                                       
HET    UNX  A 541       1                                                       
HET    UNX  A 542       1                                                       
HET    UNX  A 543       1                                                       
HET    UNX  A 544       1                                                       
HET    UNX  A 545       1                                                       
HET    UNX  A 546       1                                                       
HET    UNX  A 547       1                                                       
HET    UNX  A 548       1                                                       
HET    UNX  A 549       1                                                       
HET    UNX  A 550       1                                                       
HET    DMS  A 551       4                                                       
HET    DMS  A 552       4                                                       
HET    DMS  A 553       4                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     6RO ~{N}-(4-CHLOROPHENYL)METHANESULFONAMIDE                          
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETNAM     DMS DIMETHYL SULFOXIDE                                               
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4  6RO    C7 H8 CL N O2 S                                              
FORMUL   5  UNX    47(X)                                                        
FORMUL  52  DMS    3(C2 H6 O S)                                                 
FORMUL  55  HOH   *143(H2 O)                                                    
HELIX    1 AA1 SER A  243  ASN A  245  5                                   3    
HELIX    2 AA2 PRO A  254  LEU A  258  5                                   5    
HELIX    3 AA3 THR A  306  SER A  308  5                                   3    
HELIX    4 AA4 LYS A  319  ILE A  324  5                                   6    
HELIX    5 AA5 ASP A  326  TYR A  340  1                                  15    
HELIX    6 AA6 LEU A  395  MET A  401  1                                   7    
SHEET    1 AA1 4 ASN A 191  LEU A 192  0                                        
SHEET    2 AA1 4 TRP A 213  VAL A 224 -1  O  ILE A 221   N  LEU A 192           
SHEET    3 AA1 4 GLY A 227  PHE A 234 -1  O  LYS A 229   N  GLN A 222           
SHEET    4 AA1 4 LYS A 239  LEU A 242 -1  O  SER A 240   N  VAL A 232           
SHEET    1 AA2 4 ASN A 191  LEU A 192  0                                        
SHEET    2 AA2 4 TRP A 213  VAL A 224 -1  O  ILE A 221   N  LEU A 192           
SHEET    3 AA2 4 ARG A 203  LYS A 207 -1  N  GLY A 206   O  HIS A 214           
SHEET    4 AA2 4 ILE A 247  TYR A 249 -1  O  ALA A 248   N  LEU A 205           
SHEET    1 AA3 2 PHE A 194  GLN A 195  0                                        
SHEET    2 AA3 2 LEU A 198  ILE A 199 -1  O  LEU A 198   N  GLN A 195           
SHEET    1 AA4 5 ALA A 302  VAL A 305  0                                        
SHEET    2 AA4 5 PHE A 293  PHE A 297 -1  N  ILE A 295   O  SER A 303           
SHEET    3 AA4 5 GLN A 273  GLU A 283 -1  N  ALA A 282   O  LEU A 294           
SHEET    4 AA4 5 ARG A 263  ASP A 270 -1  N  TYR A 268   O  TRP A 275           
SHEET    5 AA4 5 LEU A 310  PRO A 312 -1  O  TYR A 311   N  VAL A 265           
SHEET    1 AA5 4 LEU A 353  TRP A 358  0                                        
SHEET    2 AA5 4 THR A 361  ASP A 371 -1  O  THR A 361   N  TRP A 358           
SHEET    3 AA5 4 LEU A 374  PHE A 379 -1  O  ARG A 376   N  GLU A 368           
SHEET    4 AA5 4 ARG A 384  TYR A 389 -1  O  ILE A 388   N  VAL A 375           
CISPEP   1 TYR A  340    PRO A  341          0        13.20                     
SITE     1 AC1  5 HIS A 214  LYS A 215  HOH A 612  HOH A 634                    
SITE     2 AC1  5 HOH A 639                                                     
SITE     1 AC2  5 ARG A 209  TRP A 363  LYS A 364  ASP A 381                    
SITE     2 AC2  5 HOH A 614                                                     
SITE     1 AC3  8 PHE A 296  GLY A 300  ALA A 302  SER A 328                    
SITE     2 AC3  8 PHE A 332  TYR A 389  SER A 392  HOH A 655                    
SITE     1 AC4  4 LYS A 207  LYS A 208  LYS A 211  HOH A 652                    
SITE     1 AC5  7 TRP A 358  TRP A 363  PHE A 379  ASP A 382                    
SITE     2 AC5  7 ARG A 384  HOH A 609  HOH A 672                               
SITE     1 AC6  3 GLU A 190  ASN A 191  THR A 223                               
CRYST1   55.772   63.761   70.522  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017930  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015684  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014180        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system