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Database: PDB
Entry: 6BZ1
LinkDB: 6BZ1
Original site: 6BZ1 
HEADER    TRANSCRIPTION/DNA                       21-DEC-17   6BZ1              
TITLE     MEF2 CHIMERA D83V MUTANT/DNA COMPLEX                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MEF2 CHIMERA;                                              
COMPND   3 CHAIN: C, D, A, B;                                                   
COMPND   4 SYNONYM: SERUM RESPONSE FACTOR-LIKE PROTEIN 1,RSRFR2,SERUM RESPONSE  
COMPND   5 FACTOR-LIKE PROTEIN 2;                                               
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: DNA (5'-D(P*AP*AP*CP*TP*AP*TP*TP*TP*AP*TP*AP*AP*GP*A)-3'); 
COMPND  10 CHAIN: G, E;                                                         
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: DNA (5'-D(P*TP*TP*CP*TP*TP*AP*TP*AP*AP*AP*TP*AP*GP*TP*T)-  
COMPND  14 3');                                                                 
COMPND  15 CHAIN: H, F;                                                         
COMPND  16 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: MEF2A, MEF2, MEF2B, XMEF2;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 SYNTHETIC: YES;                                                      
SOURCE  15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  16 ORGANISM_COMMON: HUMAN;                                              
SOURCE  17 ORGANISM_TAXID: 9606                                                 
KEYWDS    MEF2, TRANSCRIPTION FACTOR, D83V MUTANT, CONFORMATION SWITCH,         
KEYWDS   2 TRANSCRIPTION-DNA COMPLEX                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.LEI,L.CHEN                                                          
REVDAT   5   18-DEC-19 6BZ1    1       REMARK                                   
REVDAT   4   11-APR-18 6BZ1    1       JRNL                                     
REVDAT   3   07-MAR-18 6BZ1    1       JRNL                                     
REVDAT   2   14-FEB-18 6BZ1    1       REMARK                                   
REVDAT   1   07-FEB-18 6BZ1    0                                                
JRNL        AUTH   X.LEI,Y.KOU,Y.FU,N.RAJASHEKAR,H.SHI,F.WU,J.XU,Y.LUO,L.CHEN   
JRNL        TITL   THE CANCER MUTATION D83V INDUCES AN ALPHA-HELIX TO           
JRNL        TITL 2 BETA-STRAND CONFORMATION SWITCH IN MEF2B.                    
JRNL        REF    J. MOL. BIOL.                 V. 430  1157 2018              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   29477338                                                     
JRNL        DOI    10.1016/J.JMB.2018.02.012                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.97 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 14964                          
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) : 0.141                           
REMARK   3   R VALUE            (WORKING SET) : 0.139                           
REMARK   3   FREE R VALUE                     : 0.190                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 756                             
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) : 2.97                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1099                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.66                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2530                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 70                           
REMARK   3   BIN FREE R VALUE                    : 0.3440                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2939                                    
REMARK   3   NUCLEIC ACID ATOMS       : 1087                                    
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 67.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 15.42000                                             
REMARK   3    B22 (A**2) : 15.42000                                             
REMARK   3    B33 (A**2) : -30.84000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.063         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.186         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.946        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4191 ; 0.010 ; 0.017       
REMARK   3   BOND LENGTHS OTHERS               (A):  3536 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5844 ; 1.525 ; 1.727       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8237 ; 1.190 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   351 ; 7.276 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   136 ;31.791 ;23.235       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   632 ;17.279 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;19.403 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   618 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3772 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   841 ; 0.002 ; 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):  1416 ; 0.864 ; 2.991       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1415 ; 0.864 ; 2.991       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1763 ; 1.503 ; 4.485       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1764 ; 1.502 ; 4.486       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2775 ; 0.820 ; 3.089       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2774 ; 0.820 ; 3.088       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4082 ; 1.343 ; 4.621       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 15761 ; 3.754 ;55.430       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 15760 ; 3.754 ;55.432       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 8                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     C     2     87       D     2     87    5022  0.07  0.05     
REMARK   3    2     C     2     89       A     2     89    5114  0.08  0.05     
REMARK   3    3     C     2     89       B     2     89    5056  0.09  0.05     
REMARK   3    4     D     2     87       A     2     87    5080  0.06  0.05     
REMARK   3    5     D     2     87       B     2     87    5024  0.06  0.05     
REMARK   3    6     G     3     14       E     2     13    1960  0.10  0.05     
REMARK   3    7     H     2     14       F     3     15    2126  0.14  0.05     
REMARK   3    8     A     2     90       B     2     90    5136  0.09  0.05     
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 4                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.281                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : -K, -H, -L                                      
REMARK   3      TWIN FRACTION : 0.206                                           
REMARK   3      TWIN DOMAIN   : 3                                               
REMARK   3      TWIN OPERATOR : -H,-K,L                                         
REMARK   3      TWIN FRACTION : 0.312                                           
REMARK   3      TWIN DOMAIN   : 4                                               
REMARK   3      TWIN OPERATOR : K, H, -L                                        
REMARK   3      TWIN FRACTION : 0.201                                           
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 :   C     2        C    91                          
REMARK   3    ORIGIN FOR THE GROUP (A):  77.3470  48.1190  -8.7550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2469 T22:   0.2560                                     
REMARK   3      T33:   0.3927 T12:  -0.0626                                     
REMARK   3      T13:   0.0614 T23:   0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8033 L22:   1.3462                                     
REMARK   3      L33:   3.1523 L12:   0.0938                                     
REMARK   3      L13:   0.1624 L23:   1.2222                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0001 S12:   0.2893 S13:   0.1842                       
REMARK   3      S21:   0.0728 S22:  -0.0351 S23:  -0.1570                       
REMARK   3      S31:  -0.2272 S32:   0.2107 S33:   0.0350                       
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 :   D     2        D    88                          
REMARK   3    ORIGIN FOR THE GROUP (A):  76.2840  44.0200  -0.1650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3544 T22:   0.2226                                     
REMARK   3      T33:   0.3529 T12:  -0.0274                                     
REMARK   3      T13:   0.0113 T23:  -0.0193                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0827 L22:   1.8519                                     
REMARK   3      L33:   1.8155 L12:  -0.2425                                     
REMARK   3      L13:   1.3341 L23:   0.1652                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0305 S12:   0.0507 S13:  -0.1664                       
REMARK   3      S21:   0.0606 S22:   0.0321 S23:  -0.1199                       
REMARK   3      S31:   0.1729 S32:  -0.1294 S33:  -0.0626                       
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 :   G     2        G    15                          
REMARK   3    ORIGIN FOR THE GROUP (A):  59.8880  54.0980  -4.9900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1568 T22:   0.1520                                     
REMARK   3      T33:   0.2327 T12:   0.0417                                     
REMARK   3      T13:   0.0146 T23:  -0.0594                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2386 L22:   5.7793                                     
REMARK   3      L33:   5.0028 L12:   2.3393                                     
REMARK   3      L13:  -0.1809 L23:  -3.2455                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1547 S12:   0.0957 S13:  -0.0158                       
REMARK   3      S21:  -0.4197 S22:   0.0883 S23:   0.2437                       
REMARK   3      S31:  -0.0352 S32:  -0.4114 S33:   0.0663                       
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 :   H     2        H    14                          
REMARK   3    ORIGIN FOR THE GROUP (A):  61.7140  56.7610  -3.3680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1609 T22:   0.1310                                     
REMARK   3      T33:   0.1833 T12:   0.0285                                     
REMARK   3      T13:   0.0089 T23:  -0.0281                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0453 L22:   5.5172                                     
REMARK   3      L33:   4.2456 L12:   2.3517                                     
REMARK   3      L13:  -1.3357 L23:  -0.7947                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0737 S12:  -0.0325 S13:   0.3597                       
REMARK   3      S21:   0.2163 S22:  -0.0586 S23:   0.3956                       
REMARK   3      S31:  -0.5868 S32:  -0.4375 S33:  -0.0151                       
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     2        A    90                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.5730  20.0110  -5.3070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3380 T22:   0.2823                                     
REMARK   3      T33:   0.4585 T12:  -0.0941                                     
REMARK   3      T13:  -0.0047 T23:  -0.0089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2264 L22:   1.5391                                     
REMARK   3      L33:   2.4757 L12:  -0.2252                                     
REMARK   3      L13:   0.5120 L23:  -1.2527                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0641 S12:   0.0248 S13:   0.1431                       
REMARK   3      S21:   0.1206 S22:   0.1570 S23:   0.1737                       
REMARK   3      S31:   0.0711 S32:  -0.1744 S33:  -0.0929                       
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 :   B     2        B    90                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.0420  23.4160   3.4440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3324 T22:   0.2980                                     
REMARK   3      T33:   0.4329 T12:   0.0163                                     
REMARK   3      T13:   0.0045 T23:  -0.0374                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3943 L22:   2.0290                                     
REMARK   3      L33:   3.2624 L12:   0.2325                                     
REMARK   3      L13:  -0.8886 L23:  -0.8890                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0155 S12:  -0.1247 S13:   0.0452                       
REMARK   3      S21:   0.1355 S22:   0.0814 S23:  -0.0189                       
REMARK   3      S31:  -0.3094 S32:   0.0515 S33:  -0.0659                       
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 :   E     2        E    14                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.5260  14.0650  -1.7030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6080 T22:   0.5317                                     
REMARK   3      T33:   0.6627 T12:  -0.0233                                     
REMARK   3      T13:  -0.0145 T23:   0.0298                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2557 L22:   2.9016                                     
REMARK   3      L33:   1.4895 L12:  -1.9023                                     
REMARK   3      L13:  -1.3612 L23:   2.0523                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0700 S12:  -0.2751 S13:   0.2821                       
REMARK   3      S21:   0.0138 S22:   0.3841 S23:  -0.5022                       
REMARK   3      S31:   0.1237 S32:   0.3563 S33:  -0.3142                       
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 :   F     3        F    15                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.4130  12.2630   0.1500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3489 T22:   0.5747                                     
REMARK   3      T33:   0.4742 T12:   0.0044                                     
REMARK   3      T13:   0.0283 T23:   0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0315 L22:   6.0868                                     
REMARK   3      L33:   3.2295 L12:   2.2232                                     
REMARK   3      L13:   1.7992 L23:   4.0016                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2423 S12:  -0.1225 S13:  -0.1813                       
REMARK   3      S21:   0.4428 S22:   0.0432 S23:  -0.5349                       
REMARK   3      S31:   0.3294 S32:   0.5189 S33:  -0.2855                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 1.00                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6BZ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000231819.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-FEB-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332                             
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 : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15258                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 67.930                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 41.6600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
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   (%): 63.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 5.94, 0.2 M NACL AND 18%     
REMARK 280  PEG2000MME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
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                                                                      
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       74.02733            
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       37.01367            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9790 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET C     1                                                      
REMARK 465     GLU C    92                                                      
REMARK 465     HIS C    93                                                      
REMARK 465     ARG C    94                                                      
REMARK 465     GLY C    95                                                      
REMARK 465     MET D     1                                                      
REMARK 465     LYS D    89                                                      
REMARK 465     ARG D    90                                                      
REMARK 465     ARG D    91                                                      
REMARK 465     GLU D    92                                                      
REMARK 465     HIS D    93                                                      
REMARK 465     ARG D    94                                                      
REMARK 465     GLY D    95                                                      
REMARK 465      DT H     1                                                      
REMARK 465      DT H    15                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ARG A    91                                                      
REMARK 465     GLU A    92                                                      
REMARK 465     HIS A    93                                                      
REMARK 465     ARG A    94                                                      
REMARK 465     GLY A    95                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B    91                                                      
REMARK 465     GLU B    92                                                      
REMARK 465     HIS B    93                                                      
REMARK 465     ARG B    94                                                      
REMARK 465     GLY B    95                                                      
REMARK 465      DA E     1                                                      
REMARK 465      DT F     2                                                      
REMARK 465      DT F    16                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DA E  11   O3'    DA E  12   P      -0.073                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DT H  11   C3' -  C2' -  C1' ANGL. DEV. =  -6.0 DEGREES          
REMARK 500     DA E  11   C3' -  C2' -  C1' ANGL. DEV. =  -5.3 DEGREES          
REMARK 500     DT F   3   C1' -  O4' -  C4' ANGL. DEV. =  -8.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
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 C  60      -71.35    -77.64                                   
REMARK 500    ASP C  61      120.77   -171.69                                   
REMARK 500    THR D  60      -72.39    -78.18                                   
REMARK 500    ASP D  61      119.79   -171.54                                   
REMARK 500    THR A  60      -72.14    -78.84                                   
REMARK 500    ASP A  61      119.43   -170.50                                   
REMARK 500    LYS A  89       42.55   -107.30                                   
REMARK 500    ILE B   8       77.30   -100.06                                   
REMARK 500    THR B  60      -72.23    -77.35                                   
REMARK 500    ASP B  61      120.17   -172.30                                   
REMARK 500    LYS B  89       51.25   -172.97                                   
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 THR A   87     LEU A   88                 -143.60                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6BZ1 C    1    64  UNP    Q02078   MEF2A_HUMAN      1     64             
DBREF  6BZ1 C   65    91  UNP    Q02080   MEF2B_HUMAN     65     91             
DBREF  6BZ1 C   92    95  UNP    Q02078   MEF2A_HUMAN     92     95             
DBREF  6BZ1 D    1    64  UNP    Q02078   MEF2A_HUMAN      1     64             
DBREF  6BZ1 D   65    91  UNP    Q02080   MEF2B_HUMAN     65     91             
DBREF  6BZ1 D   92    95  UNP    Q02078   MEF2A_HUMAN     92     95             
DBREF  6BZ1 G    2    15  PDB    6BZ1     6BZ1             2     15             
DBREF  6BZ1 H    1    15  PDB    6BZ1     6BZ1             1     15             
DBREF  6BZ1 A    1    64  UNP    Q02078   MEF2A_HUMAN      1     64             
DBREF  6BZ1 A   65    91  UNP    Q02080   MEF2B_HUMAN     65     91             
DBREF  6BZ1 A   92    95  UNP    Q02078   MEF2A_HUMAN     92     95             
DBREF  6BZ1 B    1    64  UNP    Q02078   MEF2A_HUMAN      1     64             
DBREF  6BZ1 B   65    91  UNP    Q02080   MEF2B_HUMAN     65     91             
DBREF  6BZ1 B   92    95  UNP    Q02078   MEF2A_HUMAN     92     95             
DBREF  6BZ1 E    1    14  PDB    6BZ1     6BZ1             1     14             
DBREF  6BZ1 F    2    16  PDB    6BZ1     6BZ1             2     16             
SEQADV 6BZ1 VAL C   83  UNP  Q02080    ASP    83 ENGINEERED MUTATION            
SEQADV 6BZ1 VAL D   83  UNP  Q02080    ASP    83 ENGINEERED MUTATION            
SEQADV 6BZ1 VAL A   83  UNP  Q02080    ASP    83 ENGINEERED MUTATION            
SEQADV 6BZ1 VAL B   83  UNP  Q02080    ASP    83 ENGINEERED MUTATION            
SEQRES   1 C   95  MET GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP          
SEQRES   2 C   95  GLU ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE          
SEQRES   3 C   95  GLY LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS          
SEQRES   4 C   95  ASP CYS GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN          
SEQRES   5 C   95  LYS LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL          
SEQRES   6 C   95  LEU LEU LYS TYR THR GLU TYR SER GLU PRO HIS GLU SER          
SEQRES   7 C   95  ARG THR ASN THR VAL ILE LEU GLU THR LEU LYS ARG ARG          
SEQRES   8 C   95  GLU HIS ARG GLY                                              
SEQRES   1 D   95  MET GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP          
SEQRES   2 D   95  GLU ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE          
SEQRES   3 D   95  GLY LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS          
SEQRES   4 D   95  ASP CYS GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN          
SEQRES   5 D   95  LYS LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL          
SEQRES   6 D   95  LEU LEU LYS TYR THR GLU TYR SER GLU PRO HIS GLU SER          
SEQRES   7 D   95  ARG THR ASN THR VAL ILE LEU GLU THR LEU LYS ARG ARG          
SEQRES   8 D   95  GLU HIS ARG GLY                                              
SEQRES   1 G   14   DA  DA  DC  DT  DA  DT  DT  DT  DA  DT  DA  DA  DG          
SEQRES   2 G   14   DA                                                          
SEQRES   1 H   15   DT  DT  DC  DT  DT  DA  DT  DA  DA  DA  DT  DA  DG          
SEQRES   2 H   15   DT  DT                                                      
SEQRES   1 A   95  MET GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP          
SEQRES   2 A   95  GLU ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE          
SEQRES   3 A   95  GLY LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS          
SEQRES   4 A   95  ASP CYS GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN          
SEQRES   5 A   95  LYS LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL          
SEQRES   6 A   95  LEU LEU LYS TYR THR GLU TYR SER GLU PRO HIS GLU SER          
SEQRES   7 A   95  ARG THR ASN THR VAL ILE LEU GLU THR LEU LYS ARG ARG          
SEQRES   8 A   95  GLU HIS ARG GLY                                              
SEQRES   1 B   95  MET GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP          
SEQRES   2 B   95  GLU ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE          
SEQRES   3 B   95  GLY LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS          
SEQRES   4 B   95  ASP CYS GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN          
SEQRES   5 B   95  LYS LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL          
SEQRES   6 B   95  LEU LEU LYS TYR THR GLU TYR SER GLU PRO HIS GLU SER          
SEQRES   7 B   95  ARG THR ASN THR VAL ILE LEU GLU THR LEU LYS ARG ARG          
SEQRES   8 B   95  GLU HIS ARG GLY                                              
SEQRES   1 E   14   DA  DA  DC  DT  DA  DT  DT  DT  DA  DT  DA  DA  DG          
SEQRES   2 E   14   DA                                                          
SEQRES   1 F   15   DT  DT  DC  DT  DT  DA  DT  DA  DA  DA  DT  DA  DG          
SEQRES   2 F   15   DT  DT                                                      
HELIX    1 AA1 ASP C   13  ASP C   40  1                                  28    
HELIX    2 AA2 ASP C   61  TYR C   72  1                                  12    
HELIX    3 AA3 ASP D   13  ASP D   40  1                                  28    
HELIX    4 AA4 ASP D   61  TYR D   72  1                                  12    
HELIX    5 AA5 ASP A   13  ASP A   40  1                                  28    
HELIX    6 AA6 ASP A   61  TYR A   72  1                                  12    
HELIX    7 AA7 ASP B   13  ASP B   40  1                                  28    
HELIX    8 AA8 ASP B   61  TYR B   72  1                                  12    
SHEET    1 AA1 6 GLU C  77  THR C  80  0                                        
SHEET    2 AA1 6 LEU D  54  ALA D  58  1  O  GLN D  56   N  ARG C  79           
SHEET    3 AA1 6 GLU D  42  PHE D  48 -1  N  LEU D  45   O  TYR D  57           
SHEET    4 AA1 6 GLU C  42  PHE C  48 -1  N  GLU C  42   O  PHE D  48           
SHEET    5 AA1 6 LEU C  54  ALA C  58 -1  O  TYR C  57   N  LEU C  45           
SHEET    6 AA1 6 GLU D  77  THR D  80  1  O  GLU D  77   N  GLN C  56           
SHEET    1 AA2 6 GLU A  77  ARG A  79  0                                        
SHEET    2 AA2 6 LEU B  54  ALA B  58  1  O  GLN B  56   N  GLU A  77           
SHEET    3 AA2 6 GLU B  42  PHE B  48 -1  N  LEU B  45   O  TYR B  57           
SHEET    4 AA2 6 GLU A  42  PHE A  48 -1  N  ILE A  46   O  ALA B  44           
SHEET    5 AA2 6 LEU A  54  ALA A  58 -1  O  TYR A  57   N  LEU A  45           
SHEET    6 AA2 6 GLU B  77  ARG B  79  1  O  GLU B  77   N  GLN A  56           
CRYST1   78.440   78.440  111.041  90.00  90.00 120.00 P 32         12          
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      0.012749  0.007360  0.000000        0.00000                         
SCALE2      0.000000  0.014721  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009006        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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