GenomeNet

Database: PDB
Entry: 6G54
LinkDB: 6G54
Original site: 6G54 
HEADER    TRANSFERASE                             29-MAR-18   6G54              
TITLE     CRYSTAL STRUCTURE OF ERK2 COVALENTLY BOUND TO SM1-71                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MAPK 1,ERT1,EXTRACELLULAR SIGNAL-REGULATED KINASE 2,ERK-2,  
COMPND   5 MAP KINASE ISOFORM P42,P42-MAPK,MITOGEN-ACTIVATED PROTEIN KINASE 2,  
COMPND   6 MAPK 2;                                                              
COMPND   7 EC: 2.7.11.24;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MAPK1, ERK2, PRKM1, PRKM2;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: R3;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    KINASE, COVALENT INHIBITOR, MAPK, STRUCTURAL GENOMICS, STRUCTURAL     
KEYWDS   2 GENOMICS CONSORTIUM, SGC, TRANSFERASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.CHAIKUAD,R.SUMAN,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,N.S.GRAY,     
AUTHOR   2 S.KNAPP,STRUCTURAL GENOMICS CONSORTIUM (SGC)                         
REVDAT   3   03-JUL-19 6G54    1       JRNL                                     
REVDAT   2   01-MAY-19 6G54    1       JRNL                                     
REVDAT   1   27-FEB-19 6G54    0                                                
JRNL        AUTH   S.RAO,D.GURBANI,G.DU,R.A.EVERLEY,C.M.BROWNE,A.CHAIKUAD,      
JRNL        AUTH 2 L.TAN,M.SCHRODER,S.GONDI,S.B.FICARRO,T.SIM,N.D.KIM,          
JRNL        AUTH 3 M.J.BERBERICH,S.KNAPP,J.A.MARTO,K.D.WESTOVER,P.K.SORGER,     
JRNL        AUTH 4 N.S.GRAY                                                     
JRNL        TITL   LEVERAGING COMPOUND PROMISCUITY TO IDENTIFY TARGETABLE       
JRNL        TITL 2 CYSTEINES WITHIN THE KINOME.                                 
JRNL        REF    CELL CHEM BIOL                V.  26   818 2019              
JRNL        REFN                   ESSN 2451-9456                               
JRNL        PMID   30982749                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2019.02.021                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0218                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.65                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 29380                          
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) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1400                            
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) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2153                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3240                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 88                           
REMARK   3   BIN FREE R VALUE                    : 0.3630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2834                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 96                                      
REMARK   3   SOLVENT ATOMS            : 195                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.79                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.04000                                             
REMARK   3    B22 (A**2) : -0.04000                                             
REMARK   3    B33 (A**2) : 0.13000                                              
REMARK   3    B12 (A**2) : -0.02000                                             
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): 0.165         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.151         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.112         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.901         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3011 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2825 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4058 ; 1.348 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6561 ; 0.734 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   352 ; 6.311 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   143 ;39.277 ;24.126       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   525 ;14.461 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;21.555 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   438 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3352 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   598 ; 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):  1393 ; 1.677 ; 3.348       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1392 ; 1.676 ; 3.348       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1742 ; 2.631 ; 5.014       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1743 ; 2.631 ; 5.015       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1618 ; 2.159 ; 3.767       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1618 ; 2.149 ; 3.767       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2314 ; 3.461 ; 5.499       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3531 ; 7.098 ;41.529       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3532 ; 7.100 ;41.548       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    10        A    52                          
REMARK   3    ORIGIN FOR THE GROUP (A):  80.2110  10.1121   8.0592              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0090 T22:   0.2538                                     
REMARK   3      T33:   0.3502 T12:  -0.0025                                     
REMARK   3      T13:   0.0004 T23:   0.2280                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4337 L22:   3.5517                                     
REMARK   3      L33:   4.3794 L12:   0.0225                                     
REMARK   3      L13:   0.3530 L23:  -1.4152                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0390 S12:  -0.4392 S13:  -0.0769                       
REMARK   3      S21:  -0.0432 S22:  -0.2507 S23:  -0.7905                       
REMARK   3      S31:   0.1761 S32:   0.1375 S33:   0.2117                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    53        A   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):  62.1751   9.5769   0.9965              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1927 T22:   0.1811                                     
REMARK   3      T33:   0.1006 T12:   0.0689                                     
REMARK   3      T13:   0.0447 T23:   0.0788                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2006 L22:   1.1906                                     
REMARK   3      L33:   0.6872 L12:   0.7936                                     
REMARK   3      L13:  -0.4269 L23:  -0.4782                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1147 S12:  -0.0932 S13:  -0.2292                       
REMARK   3      S21:  -0.1698 S22:  -0.3309 S23:  -0.3105                       
REMARK   3      S31:   0.0966 S32:   0.1738 S33:   0.2162                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   189        A   330                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.4834  14.1034   2.9626              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1616 T22:   0.1533                                     
REMARK   3      T33:   0.0399 T12:   0.0046                                     
REMARK   3      T13:  -0.0046 T23:   0.0293                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0225 L22:   1.4178                                     
REMARK   3      L33:   3.2023 L12:   1.4220                                     
REMARK   3      L13:  -1.7588 L23:  -1.7538                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1176 S12:   0.1594 S13:   0.2364                       
REMARK   3      S21:  -0.0555 S22:   0.1423 S23:   0.2333                       
REMARK   3      S31:   0.1868 S32:  -0.3088 S33:  -0.2599                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   331        A   356                          
REMARK   3    ORIGIN FOR THE GROUP (A):  68.7151  -6.1908  -4.9931              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4254 T22:   0.3690                                     
REMARK   3      T33:   0.5485 T12:   0.1848                                     
REMARK   3      T13:   0.0539 T23:  -0.0859                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1562 L22:   6.4659                                     
REMARK   3      L33:   7.8492 L12:   3.8661                                     
REMARK   3      L13:  -0.9241 L23:  -0.9285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0248 S12:   0.6009 S13:  -0.9044                       
REMARK   3      S21:  -0.6354 S22:   0.0366 S23:  -0.0683                       
REMARK   3      S31:   0.9358 S32:  -0.4088 S33:  -0.0119                       
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                                                           
REMARK   4                                                                      
REMARK   4 6G54 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009426.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-FEB-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30813                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.650                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.900                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.91100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4QTA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.9M LI2SO4 AND 0.1M CITRATE 5.9, PH     
REMARK 280  5.9, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.15K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
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   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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       66.20333            
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       33.10167            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       33.10167            
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       66.20333            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL                         
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CL    CL A 417  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 596  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 615  LIES ON A SPECIAL POSITION.                          
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     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     GLY A   357                                                      
REMARK 465     TYR A   358                                                      
REMARK 465     ARG A   359                                                      
REMARK 465     SER A   360                                                      
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   O2   EDO A   415     O    HOH A   501              2.18            
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    THR A 110     -169.35   -166.12                                   
REMARK 500    ASP A 149       45.02   -140.67                                   
REMARK 500    ASP A 167       69.62     65.87                                   
REMARK 500    ASP A 175       69.12   -157.04                                   
REMARK 500    LEU A 294       53.72    -98.17                                   
REMARK 500    ASP A 318       94.77   -164.35                                   
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 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6H3 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 416                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 417                  
DBREF  6G54 A    1   360  UNP    P28482   MK01_HUMAN       1    360             
SEQADV 6G54 SER A    0  UNP  P28482              EXPRESSION TAG                 
SEQRES   1 A  361  SER MET ALA ALA ALA ALA ALA ALA GLY ALA GLY PRO GLU          
SEQRES   2 A  361  MET VAL ARG GLY GLN VAL PHE ASP VAL GLY PRO ARG TYR          
SEQRES   3 A  361  THR ASN LEU SER TYR ILE GLY GLU GLY ALA TYR GLY MET          
SEQRES   4 A  361  VAL CYS SER ALA TYR ASP ASN VAL ASN LYS VAL ARG VAL          
SEQRES   5 A  361  ALA ILE LYS LYS ILE SER PRO PHE GLU HIS GLN THR TYR          
SEQRES   6 A  361  CYS GLN ARG THR LEU ARG GLU ILE LYS ILE LEU LEU ARG          
SEQRES   7 A  361  PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN ASP ILE ILE          
SEQRES   8 A  361  ARG ALA PRO THR ILE GLU GLN MET LYS ASP VAL TYR ILE          
SEQRES   9 A  361  VAL GLN ASP LEU MET GLU THR ASP LEU TYR LYS LEU LEU          
SEQRES  10 A  361  LYS THR GLN HIS LEU SER ASN ASP HIS ILE CYS TYR PHE          
SEQRES  11 A  361  LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE HIS SER          
SEQRES  12 A  361  ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO SER ASN LEU          
SEQRES  13 A  361  LEU LEU ASN THR THR CYS ASP LEU LYS ILE CYS ASP PHE          
SEQRES  14 A  361  GLY LEU ALA ARG VAL ALA ASP PRO ASP HIS ASP HIS THR          
SEQRES  15 A  361  GLY PHE LEU THR GLU TYR VAL ALA THR ARG TRP TYR ARG          
SEQRES  16 A  361  ALA PRO GLU ILE MET LEU ASN SER LYS GLY TYR THR LYS          
SEQRES  17 A  361  SER ILE ASP ILE TRP SER VAL GLY CYS ILE LEU ALA GLU          
SEQRES  18 A  361  MET LEU SER ASN ARG PRO ILE PHE PRO GLY LYS HIS TYR          
SEQRES  19 A  361  LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE LEU GLY SER          
SEQRES  20 A  361  PRO SER GLN GLU ASP LEU ASN CYS ILE ILE ASN LEU LYS          
SEQRES  21 A  361  ALA ARG ASN TYR LEU LEU SER LEU PRO HIS LYS ASN LYS          
SEQRES  22 A  361  VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA ASP SER LYS          
SEQRES  23 A  361  ALA LEU ASP LEU LEU ASP LYS MET LEU THR PHE ASN PRO          
SEQRES  24 A  361  HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU ALA HIS PRO          
SEQRES  25 A  361  TYR LEU GLU GLN TYR TYR ASP PRO SER ASP GLU PRO ILE          
SEQRES  26 A  361  ALA GLU ALA PRO PHE LYS PHE ASP MET GLU LEU ASP ASP          
SEQRES  27 A  361  LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE PHE GLU GLU          
SEQRES  28 A  361  THR ALA ARG PHE GLN PRO GLY TYR ARG SER                      
HET    SO4  A 401       5                                                       
HET    SO4  A 402       5                                                       
HET    6H3  A 403      33                                                       
HET    EDO  A 404       4                                                       
HET    EDO  A 405       4                                                       
HET    EDO  A 406       4                                                       
HET    EDO  A 407       4                                                       
HET    EDO  A 408       4                                                       
HET    EDO  A 409       4                                                       
HET    EDO  A 410       4                                                       
HET    EDO  A 411       4                                                       
HET    EDO  A 412       4                                                       
HET    EDO  A 413       4                                                       
HET    EDO  A 414       4                                                       
HET    EDO  A 415       4                                                       
HET    EDO  A 416       4                                                       
HET     CL  A 417       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     6H3 N-{2-[(5-CHLORO-2-{[4-(4-METHYLPIPERAZIN-1-YL)                   
HETNAM   2 6H3  PHENYL]AMINO}PYRIMIDIN-4-YL)AMINO]PHENYL}PROPANAMIDE            
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      CL CHLORIDE ION                                                     
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4  6H3    C24 H28 CL N7 O                                              
FORMUL   5  EDO    13(C2 H6 O2)                                                 
FORMUL  18   CL    CL 1-                                                        
FORMUL  19  HOH   *195(H2 O)                                                    
HELIX    1 AA1 HIS A   61  PHE A   78  1                                  18    
HELIX    2 AA2 LEU A  112  GLN A  119  1                                   8    
HELIX    3 AA3 SER A  122  ALA A  143  1                                  22    
HELIX    4 AA4 LYS A  151  SER A  153  5                                   3    
HELIX    5 AA5 ASP A  175  ASP A  179  5                                   5    
HELIX    6 AA6 THR A  190  ARG A  194  5                                   5    
HELIX    7 AA7 ALA A  195  MET A  199  5                                   5    
HELIX    8 AA8 LYS A  207  ASN A  224  1                                  18    
HELIX    9 AA9 HIS A  232  GLY A  245  1                                  14    
HELIX   10 AB1 SER A  248  ASN A  253  1                                   6    
HELIX   11 AB2 ASN A  257  LEU A  267  1                                  11    
HELIX   12 AB3 PRO A  274  PHE A  279  1                                   6    
HELIX   13 AB4 ASP A  283  LEU A  294  1                                  12    
HELIX   14 AB5 GLU A  303  ALA A  309  1                                   7    
HELIX   15 AB6 HIS A  310  GLU A  314  5                                   5    
HELIX   16 AB7 ASP A  318  GLU A  322  5                                   5    
HELIX   17 AB8 GLU A  334  LEU A  338  5                                   5    
HELIX   18 AB9 PRO A  339  THR A  351  1                                  13    
HELIX   19 AC1 ALA A  352  GLN A  355  5                                   4    
SHEET    1 AA1 2 MET A  13  VAL A  14  0                                        
SHEET    2 AA1 2 GLN A  17  VAL A  18 -1  O  GLN A  17   N  VAL A  14           
SHEET    1 AA2 5 TYR A  25  GLU A  33  0                                        
SHEET    2 AA2 5 MET A  38  ASP A  44 -1  O  TYR A  43   N  THR A  26           
SHEET    3 AA2 5 VAL A  49  ILE A  56 -1  O  ILE A  53   N  CYS A  40           
SHEET    4 AA2 5 VAL A 101  ASP A 106 -1  O  VAL A 101   N  ILE A  56           
SHEET    5 AA2 5 ASP A  88  ILE A  90 -1  N  ASP A  88   O  VAL A 104           
SHEET    1 AA3 3 THR A 110  ASP A 111  0                                        
SHEET    2 AA3 3 LEU A 155  LEU A 157 -1  O  LEU A 157   N  THR A 110           
SHEET    3 AA3 3 LEU A 163  ILE A 165 -1  O  LYS A 164   N  LEU A 156           
SHEET    1 AA4 2 VAL A 145  LEU A 146  0                                        
SHEET    2 AA4 2 ARG A 172  VAL A 173 -1  O  ARG A 172   N  LEU A 146           
LINK         SG  CYS A 166                 C31 6H3 A 403     1555   1555  1.81  
CISPEP   1 GLY A   22    PRO A   23          0         1.27                     
SITE     1 AC1  7 ARG A 191  ARG A 194  HIS A 232  TYR A 233                    
SITE     2 AC1  7 HOH A 523  HOH A 596  HOH A 615                               
SITE     1 AC2  4 ARG A  15  SER A  29  TYR A  30  HOH A 568                    
SITE     1 AC3 15 ILE A  31  GLU A  33  VAL A  39  ALA A  52                    
SITE     2 AC3 15 GLN A 105  ASP A 106  MET A 108  GLU A 109                    
SITE     3 AC3 15 LYS A 114  CYS A 166  ASP A 167  EDO A 404                    
SITE     4 AC3 15 HOH A 522  HOH A 571  HOH A 599                               
SITE     1 AC4  2 LYS A 114  6H3 A 403                                          
SITE     1 AC5  3 LYS A 292  ILE A 302  HIS A 310                               
SITE     1 AC6  4 ARG A  67  ARG A  70  ARG A 172  HOH A 580                    
SITE     1 AC7  4 HIS A  61  GLN A  62  LYS A 340  HOH A 610                    
SITE     1 AC8  6 ARG A  91  ALA A  92  GLN A  97  MET A  98                    
SITE     2 AC8  6 LYS A  99  ASP A 100                                          
SITE     1 AC9  5 LYS A 151  SER A 153  EDO A 410  EDO A 416                    
SITE     2 AC9  5 HOH A 646                                                     
SITE     1 AD1  4 LYS A 151  THR A 190  EDO A 409  HOH A 622                    
SITE     1 AD2  5 TYR A 139  ASN A 271  ALA A 325  GLU A 326                    
SITE     2 AD2  5 HOH A 537                                                     
SITE     1 AD3  2 ASN A 158  HOH A 637                                          
SITE     1 AD4  3 SER A 122  ASN A 123  HOH A 518                               
SITE     1 AD5  4 LYS A 285  ASP A 288  HIS A 310  PRO A 311                    
SITE     1 AD6  5 SER A 142  ARG A 277  HOH A 501  HOH A 504                    
SITE     2 AD6  5 HOH A 506                                                     
SITE     1 AD7  4 LYS A 151  EDO A 409  HOH A 529  HOH A 629                    
SITE     1 AD8  2 LEU A 234  HOH A 620                                          
CRYST1   91.751   91.751   99.305  90.00  90.00 120.00 P 32 2 1      6          
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      0.010899  0.006293  0.000000        0.00000                         
SCALE2      0.000000  0.012585  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010070        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system