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Database: PDB
Entry: 5V3H
LinkDB: 5V3H
Original site: 5V3H 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       07-MAR-17   5V3H              
TITLE     CRYSTAL STRUCTURE OF SMYD2 WITH SAM AND EPZ033294                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-LYSINE METHYLTRANSFERASE SMYD2;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HSKM-B,HISTONE METHYLTRANSFERASE SMYD2,LYSINE N-            
COMPND   5 METHYLTRANSFERASE 3C,SET AND MYND DOMAIN-CONTAINING PROTEIN 2;       
COMPND   6 EC: 2.1.1.-,2.1.1.43;                                                
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SMYD2, KMT3C;                                                  
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBACHTB-LIC                           
KEYWDS    PROTEIN-INHIBITOR COMPLEX, PROTEIN LYSINE METHYLTRANSFERASE,          
KEYWDS   2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.A.BORIACK-SJODIN                                                    
REVDAT   2   13-JUN-18 5V3H    1       TITLE                                    
REVDAT   1   25-APR-18 5V3H    0                                                
JRNL        AUTH   M.THOMENIUS,J.TOTMAN,A.R.GRASSIAN,D.HARVEY,L.H.MITCHELL,     
JRNL        AUTH 2 T.V.RIERA,C.KLAUS,M.FOLEY,E.A.ADMIRAND,H.JAHIC,C.MAJER,      
JRNL        AUTH 3 T.J.WIGLE,S.L.JACQUES,J.GUREASKO,K.COSMOPOULOS,D.BRACH,      
JRNL        AUTH 4 K.WEST,S.SMITH,N.RIOUX,N.J.WATERS,C.TANG,A.RAIMONDI,         
JRNL        AUTH 5 M.MUNCHOF,J.E.MILLS,S.RIBICH,M.PORTER SCOTT,K.W.KUNTZ,       
JRNL        AUTH 6 W.P.JANZEN,M.MOYER,J.J.SMITH,R.CHESWORTH,R.A.COPELAND,       
JRNL        AUTH 7 P.A.BORIACK-SJODIN                                           
JRNL        TITL   SMYD ENZYME DISRUPTION BY GENE ABLATION AND SMALL MOLECULE   
JRNL        TITL 2 INHIBITORS CONFER DISCORDANT PHENOTYPES IN CANCER CELLS      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0155                                      
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) : 2.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 16191                          
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) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 892                             
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) : 2.68                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.75                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 914                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.45                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 60                           
REMARK   3   BIN FREE R VALUE                    : 0.3150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3521                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 118                                     
REMARK   3   SOLVENT ATOMS            : 129                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : -1.24000                                             
REMARK   3    B33 (A**2) : 0.82000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.16000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.133         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.360         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.306         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.126        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.919                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.877                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3748 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3536 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5047 ; 1.345 ; 2.002       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8180 ; 0.962 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   443 ; 6.624 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   174 ;37.207 ;24.368       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   670 ;16.071 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;14.142 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   530 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4134 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   837 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  : 8                                          
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    -5        A    43                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.8324   1.8709  17.6891              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4318 T22:   0.1628                                     
REMARK   3      T33:   0.2788 T12:  -0.0242                                     
REMARK   3      T13:   0.0084 T23:   0.2103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7186 L22:   1.3193                                     
REMARK   3      L33:   6.4001 L12:  -1.8481                                     
REMARK   3      L13:  -1.8779 L23:   1.0412                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3290 S12:   0.3820 S13:   0.5406                       
REMARK   3      S21:  -0.2798 S22:   0.0358 S23:   0.0108                       
REMARK   3      S31:  -1.5712 S32:  -0.1444 S33:  -0.3649                       
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    44        A   142                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.9620 -18.7271   7.7733              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1068 T22:   0.1976                                     
REMARK   3      T33:   0.0735 T12:   0.0350                                     
REMARK   3      T13:  -0.0073 T23:  -0.0764                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1591 L22:   2.3413                                     
REMARK   3      L33:   4.6239 L12:   0.4235                                     
REMARK   3      L13:  -1.3265 L23:   0.6841                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1454 S12:   0.5086 S13:  -0.4703                       
REMARK   3      S21:  -0.2634 S22:   0.0843 S23:  -0.1446                       
REMARK   3      S31:   0.1869 S32:   0.1330 S33:   0.0611                       
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   143        A   182                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.7712 -17.0922  15.1126              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0988 T22:   0.5757                                     
REMARK   3      T33:   0.2313 T12:   0.0996                                     
REMARK   3      T13:  -0.0173 T23:  -0.0212                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7339 L22:   7.1349                                     
REMARK   3      L33:   1.6438 L12:  -0.6752                                     
REMARK   3      L13:  -2.0554 L23:   0.9683                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0393 S12:  -0.2134 S13:  -0.6113                       
REMARK   3      S21:  -0.4108 S22:  -0.1193 S23:  -0.7611                       
REMARK   3      S31:   0.0837 S32:   0.6884 S33:   0.0800                       
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   183        A   270                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.2531  -7.5406  28.3277              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1137 T22:   0.0523                                     
REMARK   3      T33:   0.0400 T12:  -0.0061                                     
REMARK   3      T13:  -0.0290 T23:  -0.0373                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3118 L22:   1.7356                                     
REMARK   3      L33:   6.1015 L12:  -0.5046                                     
REMARK   3      L13:  -2.7966 L23:   1.0244                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1139 S12:  -0.3165 S13:   0.1625                       
REMARK   3      S21:   0.2141 S22:   0.1136 S23:  -0.0998                       
REMARK   3      S31:  -0.3998 S32:   0.4879 S33:  -0.2275                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   271        A   311                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.5540 -22.7405  48.0261              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7002 T22:   0.8005                                     
REMARK   3      T33:   0.2793 T12:   0.2004                                     
REMARK   3      T13:  -0.1174 T23:   0.1325                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3455 L22:   6.6129                                     
REMARK   3      L33:   1.9263 L12:   1.6307                                     
REMARK   3      L13:   1.0496 L23:   0.9522                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4582 S12:  -0.2879 S13:  -0.4822                       
REMARK   3      S21:   0.3305 S22:  -0.1107 S23:  -0.2233                       
REMARK   3      S31:   0.4609 S32:   0.5628 S33:  -0.3475                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   312        A   355                          
REMARK   3    ORIGIN FOR THE GROUP (A): -40.2283 -31.1733  40.2159              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0087 T22:   0.2331                                     
REMARK   3      T33:   0.4858 T12:   0.3775                                     
REMARK   3      T13:   0.6648 T23:   0.2060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8657 L22:   3.1112                                     
REMARK   3      L33:   6.2646 L12:   1.1004                                     
REMARK   3      L13:   3.3868 L23:   3.5831                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0604 S12:  -0.4881 S13:  -0.8358                       
REMARK   3      S21:   1.8553 S22:   0.4412 S23:   0.1040                       
REMARK   3      S31:   1.9894 S32:  -0.0971 S33:  -0.3808                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   356        A   397                          
REMARK   3    ORIGIN FOR THE GROUP (A): -51.5469 -22.6820  33.8885              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3872 T22:   0.2750                                     
REMARK   3      T33:   0.3554 T12:  -0.1392                                     
REMARK   3      T13:   0.3228 T23:  -0.1106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5006 L22:   3.6017                                     
REMARK   3      L33:   7.6534 L12:  -0.0402                                     
REMARK   3      L13:   1.5411 L23:  -0.4387                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2996 S12:   0.0229 S13:  -0.6410                       
REMARK   3      S21:   0.5857 S22:  -0.0023 S23:   0.6171                       
REMARK   3      S31:   1.0204 S32:  -0.9404 S33:   0.3020                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   398        A   432                          
REMARK   3    ORIGIN FOR THE GROUP (A): -57.7046 -16.6447  23.2628              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2397 T22:   0.8356                                     
REMARK   3      T33:   0.5386 T12:  -0.1707                                     
REMARK   3      T13:   0.0478 T23:  -0.2808                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7812 L22:   8.6468                                     
REMARK   3      L33:   1.4368 L12:   3.0210                                     
REMARK   3      L13:   0.9063 L23:  -0.5443                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3139 S12:   0.0041 S13:  -0.1712                       
REMARK   3      S21:  -0.8046 S22:   0.3637 S23:   1.1188                       
REMARK   3      S31:   0.2428 S32:  -0.8280 S33:  -0.0498                       
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 U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 5V3H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000226826.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-SEP-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95369                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300-HS                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17477                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.350                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% V/V ETHANOL, 0.1 M TRIS PH 7.5, 26%   
REMARK 280  W/V PEG3350, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       78.78000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       27.38750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       78.78000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       27.38750            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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     SER A   -10                                                      
REMARK 465     ILE A    -9                                                      
REMARK 465     ALA A    -8                                                      
REMARK 465     ASP A    -7                                                      
REMARK 465     TYR A    -6                                                      
REMARK 465     HIS A   433                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    VAL A   215     O4   PEG A   508              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    GLN A  70       43.17   -140.02                                   
REMARK 500    LYS A  87      -33.53    -37.43                                   
REMARK 500    ASN A 143       43.35    -81.36                                   
REMARK 500    VAL A 277       53.86   -115.96                                   
REMARK 500    LYS A 281       76.99   -104.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TYR A  311     LYS A  312                 -145.31                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  52   SG                                                     
REMARK 620 2 CYS A  55   SG  109.5                                              
REMARK 620 3 CYS A  74   SG  101.4  96.4                                        
REMARK 620 4 CYS A  78   SG  113.5 117.0 116.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  65   SG                                                     
REMARK 620 2 CYS A  68   SG  105.8                                              
REMARK 620 3 HIS A  86   NE2 123.6 105.2                                        
REMARK 620 4 CYS A  90   SG  114.5 105.0 101.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 209   SG                                                     
REMARK 620 2 CYS A 262   SG  114.7                                              
REMARK 620 3 CYS A 264   SG  111.1 104.6                                        
REMARK 620 4 CYS A 267   SG   92.2 116.1 118.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8WG A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8WG A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 511                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5V37   RELATED DB: PDB                                   
DBREF  5V3H A    1   433  UNP    Q9NRG4   SMYD2_HUMAN      1    433             
SEQADV 5V3H SER A  -10  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 5V3H ILE A   -9  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 5V3H ALA A   -8  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 5V3H ASP A   -7  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 5V3H TYR A   -6  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 5V3H LYS A   -5  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 5V3H ASP A   -4  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 5V3H ASP A   -3  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 5V3H ASP A   -2  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 5V3H ASP A   -1  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 5V3H LYS A    0  UNP  Q9NRG4              EXPRESSION TAG                 
SEQRES   1 A  444  SER ILE ALA ASP TYR LYS ASP ASP ASP ASP LYS MET ARG          
SEQRES   2 A  444  ALA GLU GLY LEU GLY GLY LEU GLU ARG PHE CYS SER PRO          
SEQRES   3 A  444  GLY LYS GLY ARG GLY LEU ARG ALA LEU GLN PRO PHE GLN          
SEQRES   4 A  444  VAL GLY ASP LEU LEU PHE SER CYS PRO ALA TYR ALA TYR          
SEQRES   5 A  444  VAL LEU THR VAL ASN GLU ARG GLY ASN HIS CYS GLU TYR          
SEQRES   6 A  444  CYS PHE THR ARG LYS GLU GLY LEU SER LYS CYS GLY ARG          
SEQRES   7 A  444  CYS LYS GLN ALA PHE TYR CYS ASN VAL GLU CYS GLN LYS          
SEQRES   8 A  444  GLU ASP TRP PRO MET HIS LYS LEU GLU CYS SER PRO MET          
SEQRES   9 A  444  VAL VAL PHE GLY GLU ASN TRP ASN PRO SER GLU THR VAL          
SEQRES  10 A  444  ARG LEU THR ALA ARG ILE LEU ALA LYS GLN LYS ILE HIS          
SEQRES  11 A  444  PRO GLU ARG THR PRO SER GLU LYS LEU LEU ALA VAL LYS          
SEQRES  12 A  444  GLU PHE GLU SER HIS LEU ASP LYS LEU ASP ASN GLU LYS          
SEQRES  13 A  444  LYS ASP LEU ILE GLN SER ASP ILE ALA ALA LEU HIS HIS          
SEQRES  14 A  444  PHE TYR SER LYS HIS LEU GLY PHE PRO ASP ASN ASP SER          
SEQRES  15 A  444  LEU VAL VAL LEU PHE ALA GLN VAL ASN CYS ASN GLY PHE          
SEQRES  16 A  444  THR ILE GLU ASP GLU GLU LEU SER HIS LEU GLY SER ALA          
SEQRES  17 A  444  ILE PHE PRO ASP VAL ALA LEU MET ASN HIS SER CYS CYS          
SEQRES  18 A  444  PRO ASN VAL ILE VAL THR TYR LYS GLY THR LEU ALA GLU          
SEQRES  19 A  444  VAL ARG ALA VAL GLN GLU ILE LYS PRO GLY GLU GLU VAL          
SEQRES  20 A  444  PHE THR SER TYR ILE ASP LEU LEU TYR PRO THR GLU ASP          
SEQRES  21 A  444  ARG ASN ASP ARG LEU ARG ASP SER TYR PHE PHE THR CYS          
SEQRES  22 A  444  GLU CYS GLN GLU CYS THR THR LYS ASP LYS ASP LYS ALA          
SEQRES  23 A  444  LYS VAL GLU ILE ARG LYS LEU SER ASP PRO PRO LYS ALA          
SEQRES  24 A  444  GLU ALA ILE ARG ASP MET VAL ARG TYR ALA ARG ASN VAL          
SEQRES  25 A  444  ILE GLU GLU PHE ARG ARG ALA LYS HIS TYR LYS SER PRO          
SEQRES  26 A  444  SER GLU LEU LEU GLU ILE CYS GLU LEU SER GLN GLU LYS          
SEQRES  27 A  444  MET SER SER VAL PHE GLU ASP SER ASN VAL TYR MET LEU          
SEQRES  28 A  444  HIS MET MET TYR GLN ALA MET GLY VAL CYS LEU TYR MET          
SEQRES  29 A  444  GLN ASP TRP GLU GLY ALA LEU GLN TYR GLY GLN LYS ILE          
SEQRES  30 A  444  ILE LYS PRO TYR SER LYS HIS TYR PRO LEU TYR SER LEU          
SEQRES  31 A  444  ASN VAL ALA SER MET TRP LEU LYS LEU GLY ARG LEU TYR          
SEQRES  32 A  444  MET GLY LEU GLU HIS LYS ALA ALA GLY GLU LYS ALA LEU          
SEQRES  33 A  444  LYS LYS ALA ILE ALA ILE MET GLU VAL ALA HIS GLY LYS          
SEQRES  34 A  444  ASP HIS PRO TYR ILE SER GLU ILE LYS GLN GLU ILE GLU          
SEQRES  35 A  444  SER HIS                                                      
HET    SAM  A 501      27                                                       
HET     ZN  A 502       1                                                       
HET     ZN  A 503       1                                                       
HET     ZN  A 504       1                                                       
HET    8WG  A 505      29                                                       
HET    8WG  A 506      29                                                       
HET    PEG  A 507       7                                                       
HET    PEG  A 508       7                                                       
HET    EDO  A 509       4                                                       
HET    GOL  A 510       6                                                       
HET    GOL  A 511       6                                                       
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM      ZN ZINC ION                                                         
HETNAM     8WG N-[1-({1-[(4-CHLOROPHENYL)METHYL]-1H-PYRAZOL-4-                  
HETNAM   2 8WG  YL}METHYL)AZETIDIN-3-YL]-1-CYCLOPROPYL-1H-1,2,3-                
HETNAM   3 8WG  TRIAZOLE-4-CARBOXAMIDE                                          
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     GOL GLYCEROL                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  SAM    C15 H22 N6 O5 S                                              
FORMUL   3   ZN    3(ZN 2+)                                                     
FORMUL   6  8WG    2(C20 H22 CL N7 O)                                           
FORMUL   8  PEG    2(C4 H10 O3)                                                 
FORMUL  10  EDO    C2 H6 O2                                                     
FORMUL  11  GOL    2(C3 H8 O3)                                                  
FORMUL  13  HOH   *129(H2 O)                                                    
HELIX    1 AA1 LYS A   -5  GLY A    5  1                                  11    
HELIX    2 AA2 VAL A   45  ARG A   48  5                                   4    
HELIX    3 AA3 ASN A   75  ASP A   82  1                                   8    
HELIX    4 AA4 ASP A   82  LYS A   87  1                                   6    
HELIX    5 AA5 GLU A   89  GLY A   97  1                                   9    
HELIX    6 AA6 SER A  103  HIS A  119  1                                  17    
HELIX    7 AA7 THR A  123  LYS A  127  5                                   5    
HELIX    8 AA8 ALA A  130  PHE A  134  5                                   5    
HELIX    9 AA9 HIS A  137  LEU A  141  5                                   5    
HELIX   10 AB1 GLU A  144  SER A  161  1                                  18    
HELIX   11 AB2 ASP A  168  GLY A  183  1                                  16    
HELIX   12 AB3 ASP A  201  MET A  205  5                                   5    
HELIX   13 AB4 PRO A  246  PHE A  259  1                                  14    
HELIX   14 AB5 CYS A  264  LYS A  270  1                                   7    
HELIX   15 AB6 LYS A  272  VAL A  277  1                                   6    
HELIX   16 AB7 LYS A  287  LYS A  312  1                                  26    
HELIX   17 AB8 SER A  313  SER A  329  1                                  17    
HELIX   18 AB9 ASN A  336  MET A  353  1                                  18    
HELIX   19 AC1 ASP A  355  TYR A  374  1                                  20    
HELIX   20 AC2 SER A  378  LEU A  395  1                                  18    
HELIX   21 AC3 HIS A  397  HIS A  416  1                                  20    
HELIX   22 AC4 HIS A  420  GLU A  431  1                                  12    
SHEET    1 AA1 2 LEU A   9  CYS A  13  0                                        
SHEET    2 AA1 2 ARG A  19  ALA A  23 -1  O  GLY A  20   N  PHE A  12           
SHEET    1 AA2 3 LEU A  32  PRO A  37  0                                        
SHEET    2 AA2 3 LEU A 221  ALA A 226 -1  O  VAL A 224   N  LEU A  33           
SHEET    3 AA2 3 VAL A 213  LYS A 218 -1  N  LYS A 218   O  LEU A 221           
SHEET    1 AA3 3 ALA A  40  LEU A  43  0                                        
SHEET    2 AA3 3 HIS A 193  ILE A 198 -1  O  ILE A 198   N  ALA A  40           
SHEET    3 AA3 3 PHE A 184  GLU A 187 -1  N  ILE A 186   O  LEU A 194           
SHEET    1 AA4 2 SER A  63  LYS A  64  0                                        
SHEET    2 AA4 2 PHE A  72  TYR A  73 -1  O  TYR A  73   N  SER A  63           
SHEET    1 AA5 2 ASN A 206  HIS A 207  0                                        
SHEET    2 AA5 2 PHE A 237  THR A 238  1  O  THR A 238   N  ASN A 206           
LINK         SG  CYS A  52                ZN    ZN A 503     1555   1555  2.34  
LINK         SG  CYS A  55                ZN    ZN A 503     1555   1555  2.38  
LINK         SG  CYS A  65                ZN    ZN A 504     1555   1555  2.35  
LINK         SG  CYS A  68                ZN    ZN A 504     1555   1555  2.34  
LINK         SG  CYS A  74                ZN    ZN A 503     1555   1555  2.34  
LINK         SG  CYS A  78                ZN    ZN A 503     1555   1555  2.35  
LINK         NE2 HIS A  86                ZN    ZN A 504     1555   1555  2.18  
LINK         SG  CYS A  90                ZN    ZN A 504     1555   1555  2.35  
LINK         SG  CYS A 209                ZN    ZN A 502     1555   1555  2.35  
LINK         SG  CYS A 262                ZN    ZN A 502     1555   1555  2.33  
LINK         SG  CYS A 264                ZN    ZN A 502     1555   1555  2.35  
LINK         SG  CYS A 267                ZN    ZN A 502     1555   1555  2.33  
SITE     1 AC1 14 LYS A  17  ARG A  19  GLU A 135  HIS A 137                    
SITE     2 AC1 14 CYS A 181  ASN A 182  ALA A 203  LEU A 204                    
SITE     3 AC1 14 ASN A 206  HIS A 207  TYR A 240  TYR A 258                    
SITE     4 AC1 14 PHE A 260  HOH A 622                                          
SITE     1 AC2  4 CYS A 209  CYS A 262  CYS A 264  CYS A 267                    
SITE     1 AC3  4 CYS A  52  CYS A  55  CYS A  74  CYS A  78                    
SITE     1 AC4  4 CYS A  65  CYS A  68  HIS A  86  CYS A  90                    
SITE     1 AC5 15 GLY A 183  PHE A 184  THR A 185  GLU A 187                    
SITE     2 AC5 15 ASP A 188  GLU A 189  VAL A 215  TYR A 217                    
SITE     3 AC5 15 TYR A 240  TYR A 258  LEU A 379  HIS A 416                    
SITE     4 AC5 15 8WG A 506  PEG A 508  GOL A 511                               
SITE     1 AC6 11 LEU A 108  GLY A 183  PHE A 184  THR A 185                    
SITE     2 AC6 11 SER A 196  ILE A 241  ASP A 242  TYR A 245                    
SITE     3 AC6 11 ARG A 253  HIS A 341  8WG A 505                               
SITE     1 AC7  7 PRO A 211  VAL A 213  VAL A 215  THR A 238                    
SITE     2 AC7  7 SER A 239  PEG A 508  GOL A 511                               
SITE     1 AC8  8 ILE A 214  VAL A 215  SER A 378  LEU A 379                    
SITE     2 AC8  8 ASN A 380  8WG A 505  PEG A 507  GOL A 511                    
SITE     1 AC9  5 ALA A  38  TYR A  39  LYS A 115  HOH A 636                    
SITE     2 AC9  5 HOH A 652                                                     
SITE     1 AD1  1 GLU A 104                                                     
SITE     1 AD2  7 SER A 239  TYR A 240  ILE A 241  ASP A 242                    
SITE     2 AD2  7 8WG A 505  PEG A 507  PEG A 508                               
CRYST1  157.560   54.775   79.702  90.00 114.22  90.00 C 1 2 1       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      0.006347  0.000000  0.002855        0.00000                         
SCALE2      0.000000  0.018257  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013757        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system