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Database: PDB
Entry: 2BE6
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HEADER    MEMBRANE PROTEIN                        23-OCT-05   2BE6              
TITLE     2.0 A CRYSTAL STRUCTURE OF THE CAV1.2 IQ DOMAIN-CA/CAM COMPLEX        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN 2;                                              
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL ALPHA-1C SUBUNIT; 
COMPND   7 CHAIN: D, E, F;                                                      
COMPND   8 FRAGMENT: IQ DOMAIN, RESIDUES 1659-1692;                             
COMPND   9 SYNONYM: VOLTAGE-GATED CALCIUM CHANNEL ALPHA SUBUNIT CAV1.2, CALCIUM 
COMPND  10 CHANNEL, L TYPE, ALPHA-1 POLYPEPTIDE, ISOFORM 1, CARDIAC MUSCLE;     
COMPND  11 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: CALM2;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PEGST;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: CACNA1C, CACH2, CACN2, CACNL1A1, CCHL1A1;                      
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PEGST                                     
KEYWDS    CALMODULIN, CALCIUM CHANNEL, IQ DOMAIN, INACTIVATION, FACILITATION,   
KEYWDS   2 CALCIUM-DEPENDENT, GATING, VOLTAGE-GATED, MEMBRANE PROTEIN           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.VAN PETEGEM,F.C.CHATELAIN,D.L.MINOR JR.                             
REVDAT   5   18-OCT-17 2BE6    1       REMARK                                   
REVDAT   4   13-JUL-11 2BE6    1       VERSN                                    
REVDAT   3   24-FEB-09 2BE6    1       VERSN                                    
REVDAT   2   20-DEC-05 2BE6    1       JRNL                                     
REVDAT   1   15-NOV-05 2BE6    0                                                
JRNL        AUTH   F.VAN PETEGEM,F.C.CHATELAIN,D.L.MINOR JR.                    
JRNL        TITL   INSIGHTS INTO VOLTAGE-GATED CALCIUM CHANNEL REGULATION FROM  
JRNL        TITL 2 THE STRUCTURE OF THE CA(V)1.2 IQ DOMAIN-CA(2+)/CALMODULIN    
JRNL        TITL 3 COMPLEX                                                      
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  12  1108 2005              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   16299511                                                     
JRNL        DOI    10.1038/NSMB1027                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 35999                          
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) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1810                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2553                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.90                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 144                          
REMARK   3   BIN FREE R VALUE                    : 0.2770                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3773                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 254                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.86000                                              
REMARK   3    B22 (A**2) : -1.76000                                             
REMARK   3    B33 (A**2) : 1.04000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.51000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.200         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.182         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.130         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.165         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.923                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3901 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5243 ; 1.350 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   481 ; 4.804 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   211 ;33.214 ;25.640       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   708 ;17.989 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;19.676 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   582 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2973 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2124 ; 0.229 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2779 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   268 ; 0.237 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    53 ; 0.206 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    67 ; 0.219 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    21 ; 0.142 ; 0.200       
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):  2488 ; 0.806 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3852 ; 1.171 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1565 ; 2.052 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1391 ; 3.089 ; 4.500       
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  : 9                                          
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     3        A    77                          
REMARK   3    ORIGIN FOR THE GROUP (A): -42.2580  -1.8350 -19.4490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1371 T22:   0.0520                                     
REMARK   3      T33:  -0.1193 T12:   0.0174                                     
REMARK   3      T13:   0.0297 T23:   0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1660 L22:   3.2780                                     
REMARK   3      L33:   8.7864 L12:  -0.6429                                     
REMARK   3      L13:  -4.5326 L23:  -0.2413                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0886 S12:  -0.4732 S13:  -0.0596                       
REMARK   3      S21:   0.2125 S22:  -0.0015 S23:  -0.2601                       
REMARK   3      S31:  -0.2827 S32:   0.4880 S33:   0.0901                       
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  1612        D  1640                          
REMARK   3    ORIGIN FOR THE GROUP (A): -48.1330   8.7160 -29.6420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2506 T22:   0.0360                                     
REMARK   3      T33:  -0.1066 T12:   0.0670                                     
REMARK   3      T13:   0.1178 T23:  -0.0340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.2470 L22:   2.7234                                     
REMARK   3      L33:  20.4256 L12:  -1.7028                                     
REMARK   3      L13:  10.9809 L23:  -6.6559                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2858 S12:  -0.2929 S13:   0.4111                       
REMARK   3      S21:   0.7646 S22:   0.1783 S23:   0.4085                       
REMARK   3      S31:  -0.8627 S32:  -0.9359 S33:   0.1075                       
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    81        A   146                          
REMARK   3    ORIGIN FOR THE GROUP (A): -40.8570  13.8100 -35.7330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1009 T22:   0.0012                                     
REMARK   3      T33:  -0.1424 T12:  -0.0082                                     
REMARK   3      T13:   0.0161 T23:  -0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9770 L22:   5.6783                                     
REMARK   3      L33:   2.6255 L12:   0.4544                                     
REMARK   3      L13:  -0.0465 L23:   0.1372                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1213 S12:  -0.0641 S13:   0.0224                       
REMARK   3      S21:   0.4667 S22:  -0.0686 S23:   0.0512                       
REMARK   3      S31:   0.0343 S32:  -0.1763 S33:  -0.0527                       
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 :   B     4        B    78                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.5580  16.4640   3.8980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1730 T22:   0.1071                                     
REMARK   3      T33:  -0.0389 T12:  -0.0250                                     
REMARK   3      T13:   0.0763 T23:   0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8335 L22:   6.5426                                     
REMARK   3      L33:  11.8453 L12:  -1.0490                                     
REMARK   3      L13:  -5.5366 L23:  -6.0032                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0089 S12:   0.2281 S13:  -0.4419                       
REMARK   3      S21:   0.0184 S22:  -0.8070 S23:  -1.0877                       
REMARK   3      S31:   0.0571 S32:   0.0867 S33:   0.7981                       
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 :   E  1612        E  1625                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.9740   8.0210   2.1450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3967 T22:   0.2117                                     
REMARK   3      T33:   0.1935 T12:  -0.0207                                     
REMARK   3      T13:   0.1881 T23:  -0.0231                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  37.2406 L22:  10.6577                                     
REMARK   3      L33:   8.7286 L12:  -4.0968                                     
REMARK   3      L13: -12.6648 L23:   2.2159                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4373 S12:   0.3203 S13:  -1.3392                       
REMARK   3      S21:  -0.6781 S22:   0.2099 S23:  -0.2368                       
REMARK   3      S31:   0.6004 S32:   0.1467 S33:   0.2273                       
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    82        B   146                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.4300   0.8980   3.1850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1714 T22:   0.1896                                     
REMARK   3      T33:   0.1765 T12:   0.0218                                     
REMARK   3      T13:  -0.0558 T23:   0.0783                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.5284 L22:   6.6175                                     
REMARK   3      L33:   3.3117 L12:   0.5340                                     
REMARK   3      L13:   3.1929 L23:  -0.3870                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0700 S12:  -0.9875 S13:   0.1763                       
REMARK   3      S21:   0.4662 S22:   0.0758 S23:   0.5749                       
REMARK   3      S31:  -0.1433 S32:  -0.2960 S33:  -0.0058                       
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 :   C     4        C    75                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.9240  13.9360 -26.6330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0241 T22:   0.1073                                     
REMARK   3      T33:   0.0119 T12:   0.0292                                     
REMARK   3      T13:  -0.1174 T23:  -0.0314                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4349 L22:   2.7960                                     
REMARK   3      L33:   5.0060 L12:  -1.4486                                     
REMARK   3      L13:  -0.8582 L23:  -0.8188                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1507 S12:  -0.3761 S13:   0.1757                       
REMARK   3      S21:   0.4225 S22:   0.0598 S23:  -0.4468                       
REMARK   3      S31:  -0.0822 S32:   0.0339 S33:   0.0909                       
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 :   C    82        C   146                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0770   1.7290 -37.0420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1106 T22:   0.0317                                     
REMARK   3      T33:   0.0915 T12:   0.0121                                     
REMARK   3      T13:   0.0184 T23:   0.0213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7070 L22:   6.6887                                     
REMARK   3      L33:   3.4329 L12:  -1.6796                                     
REMARK   3      L13:  -2.2679 L23:   0.4506                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2703 S12:  -0.5320 S13:  -0.2570                       
REMARK   3      S21:   0.2672 S22:  -0.0111 S23:  -0.2322                       
REMARK   3      S31:   0.1071 S32:   0.2569 S33:   0.2815                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F  1615        F  1636                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.0580   6.7290 -28.1140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0011 T22:   0.3058                                     
REMARK   3      T33:   0.1331 T12:   0.0373                                     
REMARK   3      T13:  -0.0530 T23:  -0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  25.1901 L22:   5.1531                                     
REMARK   3      L33:   8.1294 L12:  -4.5688                                     
REMARK   3      L13:  -2.3947 L23:   0.1024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4993 S12:  -2.6045 S13:  -0.1979                       
REMARK   3      S21:   0.3326 S22:   0.5351 S23:  -0.4570                       
REMARK   3      S31:  -0.0823 S32:   0.9729 S33:  -0.0358                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2BE6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000034988.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-04; 21-NOV-04               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : ALS; ALS                           
REMARK 200  BEAMLINE                       : 8.3.1; 8.3.1                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.116; 0.97972                     
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL; DOUBLE CRYSTAL     
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210; ADSC QUANTUM     
REMARK 200                                   210                                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38548                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M BIS-TRIS, PH 6.5, 10-15%           
REMARK 280  PEG4000, 0.25MM PROTEIN, VAPOR DIFFUSION, HANGING DROP,             
REMARK 280  TEMPERATURE 284K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       18.62050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8860 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8390 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8310 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -163.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E, C, 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 A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     ASP A    78                                                      
REMARK 465     THR A    79                                                      
REMARK 465     ASP A    80                                                      
REMARK 465     ALA A   147                                                      
REMARK 465     LYS A   148                                                      
REMARK 465     LEU A   149                                                      
REMARK 465     GLY D  1608                                                      
REMARK 465     HIS D  1609                                                      
REMARK 465     MET D  1610                                                      
REMARK 465     ASP D  1611                                                      
REMARK 465     GLY D  1641                                                      
REMARK 465     LYS D  1642                                                      
REMARK 465     PRO D  1643                                                      
REMARK 465     SER D  1644                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     THR B    79                                                      
REMARK 465     ASP B    80                                                      
REMARK 465     SER B    81                                                      
REMARK 465     ALA B   147                                                      
REMARK 465     LYS B   148                                                      
REMARK 465     LEU B   149                                                      
REMARK 465     GLY E  1608                                                      
REMARK 465     HIS E  1609                                                      
REMARK 465     MET E  1610                                                      
REMARK 465     ASP E  1611                                                      
REMARK 465     GLU E  1626                                                      
REMARK 465     TYR E  1627                                                      
REMARK 465     PHE E  1628                                                      
REMARK 465     ARG E  1629                                                      
REMARK 465     LYS E  1630                                                      
REMARK 465     PHE E  1631                                                      
REMARK 465     LYS E  1632                                                      
REMARK 465     LYS E  1633                                                      
REMARK 465     ARG E  1634                                                      
REMARK 465     LYS E  1635                                                      
REMARK 465     GLU E  1636                                                      
REMARK 465     GLN E  1637                                                      
REMARK 465     GLY E  1638                                                      
REMARK 465     LEU E  1639                                                      
REMARK 465     VAL E  1640                                                      
REMARK 465     GLY E  1641                                                      
REMARK 465     LYS E  1642                                                      
REMARK 465     PRO E  1643                                                      
REMARK 465     SER E  1644                                                      
REMARK 465     MET C     0                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     ASP C     2                                                      
REMARK 465     GLN C     3                                                      
REMARK 465     MET C    76                                                      
REMARK 465     LYS C    77                                                      
REMARK 465     ASP C    78                                                      
REMARK 465     THR C    79                                                      
REMARK 465     ASP C    80                                                      
REMARK 465     SER C    81                                                      
REMARK 465     ALA C   147                                                      
REMARK 465     LYS C   148                                                      
REMARK 465     LEU C   149                                                      
REMARK 465     GLY F  1608                                                      
REMARK 465     HIS F  1609                                                      
REMARK 465     MET F  1610                                                      
REMARK 465     ASP F  1611                                                      
REMARK 465     GLU F  1612                                                      
REMARK 465     VAL F  1613                                                      
REMARK 465     THR F  1614                                                      
REMARK 465     GLN F  1637                                                      
REMARK 465     GLY F  1638                                                      
REMARK 465     LEU F  1639                                                      
REMARK 465     VAL F  1640                                                      
REMARK 465     GLY F  1641                                                      
REMARK 465     LYS F  1642                                                      
REMARK 465     PRO F  1643                                                      
REMARK 465     SER F  1644                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A   7    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  30    CG   CD   CE   NZ                                   
REMARK 470     GLU A  45    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  47    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 115    CD   CE   NZ                                        
REMARK 470     GLU D1612    CG   CD   OE1  OE2                                  
REMARK 470     VAL D1613    CG1  CG2                                            
REMARK 470     THR D1614    OG1  CG2                                            
REMARK 470     LYS D1630    CG   CD   CE   NZ                                   
REMARK 470     LYS D1633    CG   CD   CE   NZ                                   
REMARK 470     GLU B   6    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  37    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  54    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  77    CD   CE   NZ                                        
REMARK 470     ASP B  78    CG   OD1  OD2                                       
REMARK 470     GLU B  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  87    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 115    CG   CD   CE   NZ                                   
REMARK 470     GLU B 119    CG   CD   OE1  OE2                                  
REMARK 470     GLU E1612    CG   CD   OE1  OE2                                  
REMARK 470     GLN E1625    CG   CD   OE1  NE2                                  
REMARK 470     GLU C   7    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  30    CD   CE   NZ                                        
REMARK 470     GLU C  82    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  83    CG   CD   OE1  OE2                                  
REMARK 470     VAL F1615    CG1  CG2                                            
REMARK 470     GLU F1636    CG   CD   OE1  OE2                                  
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  CA     CA B   507     O    HOH B   542              1.34            
REMARK 500   OE1  GLN C   135     O    HOH C   581              1.71            
REMARK 500   O    HOH B   546     O    HOH B   547              1.87            
REMARK 500   O    HOH A   564     O    HOH A   576              1.95            
REMARK 500   OE1  GLN C    49     O    HOH C   528              2.01            
REMARK 500   OE1  GLN C    49     O    HOH C   579              2.04            
REMARK 500   OE1  GLU C    11     NH2  ARG F  1629              2.07            
REMARK 500   OD1  ASN B    60     O    HOH B   542              2.09            
REMARK 500   O    HOH C   595     O    HOH C   606              2.13            
REMARK 500   O    HOH A   527     O    HOH A   560              2.14            
REMARK 500   O    HOH C   583     O    HOH C   601              2.15            
REMARK 500   O    HOH C   584     O    HOH C   599              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASN B  42   CG    ASN B  42   OD1     0.143                       
REMARK 500    ASN B  42   CG    ASN B  42   ND2     0.378                       
REMARK 500    GLU F1636   C     GLU F1636   O       0.765                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 CALCIUM 501, 502, 503, 504 ARE ASSOCIATED WITH CHAIN A,              
REMARK 600 CA 506, 507, 508, 509 WITH CHAIN B AND CA 511, 512, 513,             
REMARK 600 514 WITH CHAIN C. NI 505 IS ASSOCIATED WITH CHAIN A, 510             
REMARK 600 WITH CHAIN B AND 515 WITH CHAIN C.                                   
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                              CA A 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  22   OD1                                                    
REMARK 620 2 ASP A  24   OD2  76.1                                              
REMARK 620 3 HOH A 507   O    86.7  85.6                                        
REMARK 620 4 ASP A  20   OD1  77.3  85.1 163.0                                  
REMARK 620 5 THR A  26   O   149.8  82.7 113.1  79.7                            
REMARK 620 6 GLU A  31   OE1 130.0 151.2  84.3 110.4  76.7                      
REMARK 620 7 GLU A  31   OE2  77.2 152.0  84.6  97.2 125.2  53.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  67   OE2                                                    
REMARK 620 2 HOH A 577   O    80.4                                              
REMARK 620 3 HOH A 552   O   130.4  73.1                                        
REMARK 620 4 ASP A  56   OD2  78.6 142.5 142.7                                  
REMARK 620 5 ASP A  58   OD2  70.8  69.5 132.1  74.3                            
REMARK 620 6 ASN A  60   OD1 142.8  98.2  83.0  80.9  74.0                      
REMARK 620 7 THR A  62   O   123.5 143.7  70.6  73.3 140.2  78.6                
REMARK 620 8 GLU A  67   OE1  51.8  98.2  91.2  92.7 122.6 160.1  81.5          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 104   OE1                                                    
REMARK 620 2 GLU A 104   OE2  51.1                                              
REMARK 620 3 ASP A  93   OD2  97.0 105.7                                        
REMARK 620 4 TYR A  99   O   127.2  76.6  89.6                                  
REMARK 620 5 HOH A 508   O    88.7  90.4 162.9  99.9                            
REMARK 620 6 ASP A  95   OD1  76.6 127.6  81.3 155.6  84.4                      
REMARK 620 7 ASN A  97   OD1 150.4 156.3  84.5  82.2  82.7  74.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 129   OD2                                                    
REMARK 620 2 ASP A 133   OD2  91.0                                              
REMARK 620 3 GLN A 135   O    90.9  76.9                                        
REMARK 620 4 HOH A 512   O   160.6  78.4 102.3                                  
REMARK 620 5 GLU A 140   OE1 105.8 151.3  79.7  90.7                            
REMARK 620 6 ASP A 131   OD1  82.1  79.2 154.9  79.9 125.4                      
REMARK 620 7 GLU A 140   OE2  90.9 152.4 130.6  91.2  52.6  73.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI A 505  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 107   NE2                                                    
REMARK 620 2 HIS A 107   NE2  15.0                                              
REMARK 620 3 HOH A 569   O    94.9  81.1                                        
REMARK 620 4 HOH A 564   O   101.9 106.8  87.4                                  
REMARK 620 5 HOH A 572   O   170.3 155.3  75.8  80.8                            
REMARK 620 6 HOH A 570   O   113.9 105.4  79.0 142.5  62.0                      
REMARK 620 7 HOH A 565   O   104.8 119.0 159.9  84.9  84.6  96.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 506  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B  26   O                                                      
REMARK 620 2 GLU B  31   OE1  74.4                                              
REMARK 620 3 ASP B  20   OD1  84.1 115.4                                        
REMARK 620 4 ASP B  24   OD2  79.1 146.4  81.5                                  
REMARK 620 5 ASP B  22   OD1 153.6 131.7  86.3  75.2                            
REMARK 620 6 GLU B  31   OE2 128.6  55.5 105.6 151.5  77.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 507  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  56   OD2                                                    
REMARK 620 2 THR B  62   O    76.9                                              
REMARK 620 3 GLU B  67   OE2 115.3  82.8                                        
REMARK 620 4 ASN B  60   OD1  79.5  75.3 150.2                                  
REMARK 620 5 ASP B  58   OD2  80.2 143.5 133.1  72.8                            
REMARK 620 6 GLU B  67   OE1 101.4 132.2  54.2 152.3  80.0                      
REMARK 620 7 HOH B 548   O   157.2 116.2  85.9  85.9  78.8  83.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 508  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  95   OD1                                                    
REMARK 620 2 ASN B  97   OD1  76.2                                              
REMARK 620 3 ASP B  93   OD1  85.6  85.2                                        
REMARK 620 4 GLU B 104   OE2 122.3 159.0 105.0                                  
REMARK 620 5 GLU B 104   OE1  69.3 144.6  99.6  53.0                            
REMARK 620 6 TYR B  99   O   156.9  80.7  92.3  80.5 133.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 509  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 140   OE2                                                    
REMARK 620 2 GLU B 140   OE1  50.9                                              
REMARK 620 3 ASP B 131   OD1  79.6 127.3                                        
REMARK 620 4 ASP B 129   OD2  96.8 120.3  77.1                                  
REMARK 620 5 HOH B 511   O    94.1  84.4  82.0 154.2                            
REMARK 620 6 GLN B 135   O   133.8  87.3 145.3  87.8 101.3                      
REMARK 620 7 ASP B 133   OD2 149.6 154.2  70.1  79.6  79.3  76.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 510  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 546   O                                                      
REMARK 620 2 HOH B 547   O    52.1                                              
REMARK 620 3 HOH B 544   O    67.8 110.6                                        
REMARK 620 4 HIS B 107   NE2  73.7  94.3  99.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 511  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  22   OD1                                                    
REMARK 620 2 ASP C  20   OD1  75.7                                              
REMARK 620 3 GLU C  31   OE2 125.7 110.3                                        
REMARK 620 4 GLU C  31   OE1  75.3  92.3  51.0                                  
REMARK 620 5 HOH C 520   O    85.0 159.0  87.4  90.4                            
REMARK 620 6 THR C  26   O   157.3  85.4  72.7 118.7 111.3                      
REMARK 620 7 ASP C  24   OD2  82.4  86.7 149.3 157.2  82.7  84.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 512  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 607   O                                                      
REMARK 620 2 ASN C  60   OD1  64.0                                              
REMARK 620 3 HOH C 527   O    61.4  92.7                                        
REMARK 620 4 GLU C  67   OE2 131.4 144.3  75.8                                  
REMARK 620 5 GLU C  67   OE1  99.9 161.3  87.0  53.4                            
REMARK 620 6 THR C  62   O    64.6  80.7 122.3 134.0  83.6                      
REMARK 620 7 ASP C  58   OD1 117.7  76.4  75.5  68.1 121.4 151.8                
REMARK 620 8 ASP C  56   OD1 138.5  84.2 151.1  90.0 104.8  85.6  75.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 513  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 532   O                                                      
REMARK 620 2 GLU C 104   OE2  83.4                                              
REMARK 620 3 GLU C 104   OE1  86.1  52.8                                        
REMARK 620 4 ASP C  95   OD2  84.6 126.2  74.2                                  
REMARK 620 5 TYR C  99   O    96.5  74.2 126.4 159.4                            
REMARK 620 6 ASN C  97   OD1  83.1 150.0 151.8  78.8  80.9                      
REMARK 620 7 ASP C  93   OD1 166.5 109.0  97.0  83.7  92.2  88.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 514  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 129   OD2                                                    
REMARK 620 2 ASP C 133   OD1  87.0                                              
REMARK 620 3 GLN C 135   O    83.5  73.6                                        
REMARK 620 4 GLU C 140   OE2  93.3 155.4 130.8                                  
REMARK 620 5 GLU C 140   OE1 103.5 151.1  80.8  52.2                            
REMARK 620 6 HOH C 517   O   160.7  81.3 107.5  91.2  94.1                      
REMARK 620 7 ASP C 131   OD1  81.4  79.9 150.1  75.9 127.9  81.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI C 515  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 107   NE2                                                    
REMARK 620 2 HOH C 594   O   108.4                                              
REMARK 620 3 HOH C 595   O   170.3  63.2                                        
REMARK 620 4 HOH C 596   O   103.6  81.3  71.2                                  
REMARK 620 5 HOH C 584   O    90.0 160.1  97.8  87.3                            
REMARK 620 6 HOH C 583   O   103.2  90.2  82.2 153.2  92.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 510                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 511                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 512                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 513                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 514                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 515                  
DBREF  2BE6 A    0   148  UNP    Q53S29   Q53S29_HUMAN     1    149             
DBREF  2BE6 D 1611  1644  UNP    Q13933   CAC1C_HUMAN   1659   1692             
DBREF  2BE6 B    0   148  UNP    Q53S29   Q53S29_HUMAN     1    149             
DBREF  2BE6 E 1611  1644  UNP    Q13933   CAC1C_HUMAN   1659   1692             
DBREF  2BE6 C    0   148  UNP    Q53S29   Q53S29_HUMAN     1    149             
DBREF  2BE6 F 1611  1644  UNP    Q13933   CAC1C_HUMAN   1659   1692             
SEQADV 2BE6 GLY D 1608  UNP  Q13933              CLONING ARTIFACTS              
SEQADV 2BE6 HIS D 1609  UNP  Q13933              CLONING ARTIFACTS              
SEQADV 2BE6 MET D 1610  UNP  Q13933              CLONING ARTIFACTS              
SEQADV 2BE6 GLY E 1608  UNP  Q13933              CLONING ARTIFACTS              
SEQADV 2BE6 HIS E 1609  UNP  Q13933              CLONING ARTIFACTS              
SEQADV 2BE6 MET E 1610  UNP  Q13933              CLONING ARTIFACTS              
SEQADV 2BE6 GLY F 1608  UNP  Q13933              CLONING ARTIFACTS              
SEQADV 2BE6 HIS F 1609  UNP  Q13933              CLONING ARTIFACTS              
SEQADV 2BE6 MET F 1610  UNP  Q13933              CLONING ARTIFACTS              
SEQRES   1 A  150  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 A  150  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 A  150  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 A  150  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 A  150  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 A  150  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 A  150  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 A  150  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 A  150  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 A  150  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 A  150  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 A  150  GLN MET MET THR ALA LYS LEU                                  
SEQRES   1 D   37  GLY HIS MET ASP GLU VAL THR VAL GLY LYS PHE TYR ALA          
SEQRES   2 D   37  THR PHE LEU ILE GLN GLU TYR PHE ARG LYS PHE LYS LYS          
SEQRES   3 D   37  ARG LYS GLU GLN GLY LEU VAL GLY LYS PRO SER                  
SEQRES   1 B  150  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 B  150  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 B  150  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 B  150  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 B  150  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 B  150  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 B  150  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 B  150  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 B  150  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 B  150  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 B  150  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 B  150  GLN MET MET THR ALA LYS LEU                                  
SEQRES   1 E   37  GLY HIS MET ASP GLU VAL THR VAL GLY LYS PHE TYR ALA          
SEQRES   2 E   37  THR PHE LEU ILE GLN GLU TYR PHE ARG LYS PHE LYS LYS          
SEQRES   3 E   37  ARG LYS GLU GLN GLY LEU VAL GLY LYS PRO SER                  
SEQRES   1 C  150  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 C  150  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 C  150  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 C  150  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 C  150  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 C  150  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 C  150  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 C  150  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 C  150  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 C  150  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 C  150  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 C  150  GLN MET MET THR ALA LYS LEU                                  
SEQRES   1 F   37  GLY HIS MET ASP GLU VAL THR VAL GLY LYS PHE TYR ALA          
SEQRES   2 F   37  THR PHE LEU ILE GLN GLU TYR PHE ARG LYS PHE LYS LYS          
SEQRES   3 F   37  ARG LYS GLU GLN GLY LEU VAL GLY LYS PRO SER                  
HET     CA  A 501       1                                                       
HET     CA  A 502       1                                                       
HET     CA  A 503       1                                                       
HET     CA  A 504       1                                                       
HET     NI  A 505       1                                                       
HET     CA  B 506       1                                                       
HET     CA  B 507       1                                                       
HET     CA  B 508       1                                                       
HET     CA  B 509       1                                                       
HET     NI  B 510       1                                                       
HET     CA  C 511       1                                                       
HET     CA  C 512       1                                                       
HET     CA  C 513       1                                                       
HET     CA  C 514       1                                                       
HET     NI  C 515       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      NI NICKEL (II) ION                                                  
FORMUL   7   CA    12(CA 2+)                                                    
FORMUL  11   NI    3(NI 2+)                                                     
FORMUL  22  HOH   *254(H2 O)                                                    
HELIX    1   1 THR A    5  ASP A   20  1                                  16    
HELIX    2   2 THR A   28  LEU A   39  1                                  12    
HELIX    3   3 THR A   44  ASP A   56  1                                  13    
HELIX    4   4 PHE A   65  MET A   76  1                                  12    
HELIX    5   5 SER A   81  ASP A   93  1                                  13    
HELIX    6   6 SER A  101  LEU A  112  1                                  12    
HELIX    7   7 THR A  117  ASP A  129  1                                  13    
HELIX    8   8 TYR A  138  THR A  146  1                                   9    
HELIX    9   9 VAL D 1615  GLY D 1638  1                                  24    
HELIX   10  10 THR B    5  ASP B   20  1                                  16    
HELIX   11  11 THR B   28  LEU B   39  1                                  12    
HELIX   12  12 THR B   44  ASP B   56  1                                  13    
HELIX   13  13 PHE B   65  ASP B   78  1                                  14    
HELIX   14  14 GLU B   82  ASP B   93  1                                  12    
HELIX   15  15 SER B  101  GLY B  113  1                                  13    
HELIX   16  16 THR B  117  ASP B  129  1                                  13    
HELIX   17  17 TYR B  138  MET B  145  1                                   8    
HELIX   18  18 GLU E 1612  GLN E 1625  1                                  14    
HELIX   19  19 THR C    5  ASP C   20  1                                  16    
HELIX   20  20 THR C   28  LEU C   39  1                                  12    
HELIX   21  21 THR C   44  ASP C   56  1                                  13    
HELIX   22  22 PHE C   65  LYS C   75  1                                  11    
HELIX   23  23 GLU C   82  ASP C   93  1                                  12    
HELIX   24  24 SER C  101  LEU C  112  1                                  12    
HELIX   25  25 THR C  117  ASP C  129  1                                  13    
HELIX   26  26 TYR C  138  MET C  145  1                                   8    
HELIX   27  27 LYS F 1617  GLU F 1636  1                                  20    
SHEET    1   A 2 THR A  26  ILE A  27  0                                        
SHEET    2   A 2 ILE A  63  ASP A  64 -1  O  ILE A  63   N  ILE A  27           
SHEET    1   B 2 TYR A  99  ILE A 100  0                                        
SHEET    2   B 2 VAL A 136  ASN A 137 -1  O  VAL A 136   N  ILE A 100           
SHEET    1   C 2 THR B  26  ILE B  27  0                                        
SHEET    2   C 2 ILE B  63  ASP B  64 -1  O  ILE B  63   N  ILE B  27           
SHEET    1   D 2 TYR B  99  ILE B 100  0                                        
SHEET    2   D 2 VAL B 136  ASN B 137 -1  O  VAL B 136   N  ILE B 100           
SHEET    1   E 2 THR C  26  ILE C  27  0                                        
SHEET    2   E 2 ILE C  63  ASP C  64 -1  O  ILE C  63   N  ILE C  27           
SHEET    1   F 2 TYR C  99  ILE C 100  0                                        
SHEET    2   F 2 VAL C 136  ASN C 137 -1  O  VAL C 136   N  ILE C 100           
LINK        CA    CA A 501                 OD1 ASP A  22     1555   1555  2.36  
LINK        CA    CA A 501                 OD2 ASP A  24     1555   1555  2.48  
LINK        CA    CA A 501                 O   HOH A 507     1555   1555  2.34  
LINK        CA    CA A 501                 OD1 ASP A  20     1555   1555  2.26  
LINK        CA    CA A 501                 O   THR A  26     1555   1555  2.36  
LINK        CA    CA A 501                 OE1 GLU A  31     1555   1555  2.53  
LINK        CA    CA A 501                 OE2 GLU A  31     1555   1555  2.40  
LINK        CA    CA A 502                 OE2 GLU A  67     1555   1555  2.55  
LINK        CA    CA A 502                 O   HOH A 577     1555   1555  2.34  
LINK        CA    CA A 502                 O   HOH A 552     1555   1555  2.53  
LINK        CA    CA A 502                 OD2 ASP A  56     1555   1555  2.32  
LINK        CA    CA A 502                 OD2 ASP A  58     1555   1555  2.55  
LINK        CA    CA A 502                 OD1 ASN A  60     1555   1555  2.51  
LINK        CA    CA A 502                 O   THR A  62     1555   1555  2.40  
LINK        CA    CA A 502                 OE1 GLU A  67     1555   1555  2.46  
LINK        CA    CA A 503                 OE1 GLU A 104     1555   1555  2.56  
LINK        CA    CA A 503                 OE2 GLU A 104     1555   1555  2.40  
LINK        CA    CA A 503                 OD2 ASP A  93     1555   1555  2.19  
LINK        CA    CA A 503                 O   TYR A  99     1555   1555  2.32  
LINK        CA    CA A 503                 O   HOH A 508     1555   1555  2.27  
LINK        CA    CA A 503                 OD1 ASP A  95     1555   1555  2.39  
LINK        CA    CA A 503                 OD1 ASN A  97     1555   1555  2.42  
LINK        CA    CA A 504                 OD2 ASP A 129     1555   1555  2.27  
LINK        CA    CA A 504                 OD2 ASP A 133     1555   1555  2.41  
LINK        CA    CA A 504                 O   GLN A 135     1555   1555  2.36  
LINK        CA    CA A 504                 O   HOH A 512     1555   1555  2.30  
LINK        CA    CA A 504                 OE1 GLU A 140     1555   1555  2.37  
LINK        CA    CA A 504                 OD1 ASP A 131     1555   1555  2.37  
LINK        CA    CA A 504                 OE2 GLU A 140     1555   1555  2.57  
LINK        NI    NI A 505                 NE2AHIS A 107     1555   1555  2.10  
LINK        NI    NI A 505                 NE2BHIS A 107     1555   1555  2.15  
LINK        NI    NI A 505                 O   HOH A 569     1555   1555  2.04  
LINK        NI    NI A 505                 O   HOH A 564     1555   1555  2.23  
LINK        NI    NI A 505                 O   HOH A 572     1555   1555  2.40  
LINK        NI    NI A 505                 O   HOH A 570     1555   1555  2.50  
LINK        NI    NI A 505                 O   HOH A 565     1555   1555  2.38  
LINK        CA    CA B 506                 O   THR B  26     1555   1555  2.40  
LINK        CA    CA B 506                 OE1 GLU B  31     1555   1555  2.40  
LINK        CA    CA B 506                 OD1 ASP B  20     1555   1555  2.26  
LINK        CA    CA B 506                 OD2 ASP B  24     1555   1555  2.67  
LINK        CA    CA B 506                 OD1 ASP B  22     1555   1555  2.51  
LINK        CA    CA B 506                 OE2 GLU B  31     1555   1555  2.31  
LINK        CA    CA B 507                 OD2 ASP B  56     1555   1555  2.13  
LINK        CA    CA B 507                 O   THR B  62     1555   1555  2.59  
LINK        CA    CA B 507                 OE2 GLU B  67     1555   1555  2.28  
LINK        CA    CA B 507                 OD1 ASN B  60     1555   1555  2.77  
LINK        CA    CA B 507                 OD2 ASP B  58     1555   1555  2.39  
LINK        CA    CA B 507                 OE1 GLU B  67     1555   1555  2.54  
LINK        CA    CA B 507                 O   HOH B 548     1555   1555  2.90  
LINK        CA    CA B 508                 OD1 ASP B  95     1555   1555  2.36  
LINK        CA    CA B 508                 OD1 ASN B  97     1555   1555  2.40  
LINK        CA    CA B 508                 OD1 ASP B  93     1555   1555  2.25  
LINK        CA    CA B 508                 OE2 GLU B 104     1555   1555  2.27  
LINK        CA    CA B 508                 OE1 GLU B 104     1555   1555  2.58  
LINK        CA    CA B 508                 O   TYR B  99     1555   1555  2.32  
LINK        CA    CA B 509                 OE2 GLU B 140     1555   1555  2.63  
LINK        CA    CA B 509                 OE1 GLU B 140     1555   1555  2.40  
LINK        CA    CA B 509                 OD1 ASP B 131     1555   1555  2.51  
LINK        CA    CA B 509                 OD2 ASP B 129     1555   1555  2.30  
LINK        CA    CA B 509                 O   HOH B 511     1555   1555  2.32  
LINK        CA    CA B 509                 O   GLN B 135     1555   1555  2.38  
LINK        CA    CA B 509                 OD2 ASP B 133     1555   1555  2.40  
LINK        NI    NI B 510                 O   HOH B 546     1555   1555  1.99  
LINK        NI    NI B 510                 O   HOH B 547     1555   1555  2.25  
LINK        NI    NI B 510                 O   HOH B 544     1555   1555  2.22  
LINK        CA    CA C 511                 OD1 ASP C  22     1555   1555  2.42  
LINK        CA    CA C 511                 OD1 ASP C  20     1555   1555  2.18  
LINK        CA    CA C 511                 OE2 GLU C  31     1555   1555  2.62  
LINK        CA    CA C 511                 OE1 GLU C  31     1555   1555  2.47  
LINK        CA    CA C 511                 O   HOH C 520     1555   1555  2.60  
LINK        CA    CA C 511                 O   THR C  26     1555   1555  2.34  
LINK        CA    CA C 511                 OD2 ASP C  24     1555   1555  2.29  
LINK        CA    CA C 512                 O   HOH C 607     1555   1555  1.84  
LINK        CA    CA C 512                 OD1 ASN C  60     1555   1555  2.29  
LINK        CA    CA C 512                 O   HOH C 527     1555   1555  2.65  
LINK        CA    CA C 512                 OE2 GLU C  67     1555   1555  2.53  
LINK        CA    CA C 512                 OE1 GLU C  67     1555   1555  2.35  
LINK        CA    CA C 512                 O   THR C  62     1555   1555  2.36  
LINK        CA    CA C 512                 OD1 ASP C  58     1555   1555  2.53  
LINK        CA    CA C 512                 OD1 ASP C  56     1555   1555  2.48  
LINK        CA    CA C 513                 O   HOH C 532     1555   1555  2.46  
LINK        CA    CA C 513                 OE2 GLU C 104     1555   1555  2.42  
LINK        CA    CA C 513                 OE1 GLU C 104     1555   1555  2.49  
LINK        CA    CA C 513                 OD2 ASP C  95     1555   1555  2.42  
LINK        CA    CA C 513                 O   TYR C  99     1555   1555  2.18  
LINK        CA    CA C 513                 OD1 ASN C  97     1555   1555  2.43  
LINK        CA    CA C 513                 OD1 ASP C  93     1555   1555  2.31  
LINK        CA    CA C 514                 OD2 ASP C 129     1555   1555  2.24  
LINK        CA    CA C 514                 OD1 ASP C 133     1555   1555  2.43  
LINK        CA    CA C 514                 O   GLN C 135     1555   1555  2.35  
LINK        CA    CA C 514                 OE2 GLU C 140     1555   1555  2.52  
LINK        CA    CA C 514                 OE1 GLU C 140     1555   1555  2.44  
LINK        CA    CA C 514                 O   HOH C 517     1555   1555  2.11  
LINK        CA    CA C 514                 OD1 ASP C 131     1555   1555  2.44  
LINK        NI    NI C 515                 NE2 HIS C 107     1555   1555  2.08  
LINK        NI    NI C 515                 O   HOH C 594     1555   1555  1.88  
LINK        NI    NI C 515                 O   HOH C 595     1555   1555  2.44  
LINK        NI    NI C 515                 O   HOH C 596     1555   1555  2.36  
LINK        NI    NI C 515                 O   HOH C 584     1555   1555  2.24  
LINK        NI    NI C 515                 O   HOH C 583     1555   1555  2.47  
LINK         NE2BHIS B 107                NI    NI B 510     1555   1555  2.27  
SITE     1 AC1  6 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC1  6 GLU A  31  HOH A 507                                          
SITE     1 AC2  7 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC2  7 GLU A  67  HOH A 552  HOH A 577                               
SITE     1 AC3  6 ASP A  93  ASP A  95  ASN A  97  TYR A  99                    
SITE     2 AC3  6 GLU A 104  HOH A 508                                          
SITE     1 AC4  6 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC4  6 GLU A 140  HOH A 512                                          
SITE     1 AC5  6 HIS A 107  HOH A 564  HOH A 565  HOH A 569                    
SITE     2 AC5  6 HOH A 570  HOH A 572                                          
SITE     1 AC6  5 ASP B  20  ASP B  22  ASP B  24  THR B  26                    
SITE     2 AC6  5 GLU B  31                                                     
SITE     1 AC7  7 ASP B  56  ASP B  58  ASN B  60  THR B  62                    
SITE     2 AC7  7 GLU B  67  HOH B 542  HOH B 548                               
SITE     1 AC8  5 ASP B  93  ASP B  95  ASN B  97  TYR B  99                    
SITE     2 AC8  5 GLU B 104                                                     
SITE     1 AC9  6 ASP B 129  ASP B 131  ASP B 133  GLN B 135                    
SITE     2 AC9  6 GLU B 140  HOH B 511                                          
SITE     1 BC1  6 HIS B 107  HOH B 529  HOH B 543  HOH B 544                    
SITE     2 BC1  6 HOH B 546  HOH B 547                                          
SITE     1 BC2  6 ASP C  20  ASP C  22  ASP C  24  THR C  26                    
SITE     2 BC2  6 GLU C  31  HOH C 520                                          
SITE     1 BC3  7 ASP C  56  ASP C  58  ASN C  60  THR C  62                    
SITE     2 BC3  7 GLU C  67  HOH C 527  HOH C 607                               
SITE     1 BC4  6 ASP C  93  ASP C  95  ASN C  97  TYR C  99                    
SITE     2 BC4  6 GLU C 104  HOH C 532                                          
SITE     1 BC5  6 ASP C 129  ASP C 131  ASP C 133  GLN C 135                    
SITE     2 BC5  6 GLU C 140  HOH C 517                                          
SITE     1 BC6  7 HIS C 107  HOH C 583  HOH C 584  HOH C 594                    
SITE     2 BC6  7 HOH C 595  HOH C 596  HOH C 599                               
CRYST1   84.731   37.241   86.860  90.00  97.77  90.00 P 1 21 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011802  0.000000  0.001610        0.00000                         
SCALE2      0.000000  0.026852  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011619        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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