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Database: PDB
Entry: 2W2C
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HEADER    TRANSFERASE                             28-OCT-08   2W2C              
TITLE     STRUCTURE OF THE TETRADECAMERIC OLIGOMERISATION DOMAIN OF CALCIUM-    
TITLE    2 CALMODULIN DEPENDENT PROTEIN KINASE II DELTA                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA  
COMPND   3 CHAIN;                                                               
COMPND   4 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N;                     
COMPND   5 FRAGMENT: OLIGOMERISATION DOMAIN, RESIDUES 334-475;                  
COMPND   6 SYNONYM: CALCIUM CAMOLDULIN DEPENDENT KINASE 2D;                     
COMPND   7 EC: 2.7.11.17;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;                                
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    SERINE/THREONINE-PROTEIN KINASE, KINASE, TRANSFERASE, ATP-BINDING,    
KEYWDS   2 PHOSPHOPROTEIN, CALMODULIN-BINDING, NUCLEOTIDE-BINDING               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.W.PIKE,P.RELLOS,R.SETHI,E.SALAH,N.BURGESS-BROWN,L.SHRESTHA,       
AUTHOR   2 A.ROOS,J.W.MURRAY,F.VON DELFT,A.EDWARDS,C.H.ARROWSMITH,J.WEIGELT,    
AUTHOR   3 C.BOUNTRA,S.KNAPP                                                    
REVDAT   5   20-DEC-17 2W2C    1       AUTHOR JRNL                              
REVDAT   4   10-AUG-11 2W2C    1       JRNL   REMARK                            
REVDAT   3   13-JUL-11 2W2C    1       VERSN                                    
REVDAT   2   30-DEC-08 2W2C    1       REMARK                                   
REVDAT   1   23-DEC-08 2W2C    0                                                
JRNL        AUTH   P.RELLOS,A.C.W.PIKE,F.H.NIESEN,E.SALAH,W.H.LEE,F.VON DELFT,  
JRNL        AUTH 2 S.KNAPP                                                      
JRNL        TITL   STRUCTURE OF THE CAMKIIDELTA/CALMODULIN COMPLEX REVEALS THE  
JRNL        TITL 2 MOLECULAR MECHANISM OF CAMKII KINASE ACTIVATION.             
JRNL        REF    PLOS BIOL.                    V.   8   426 2010              
JRNL        REFN                   ISSN 1544-9173                               
JRNL        PMID   20668654                                                     
JRNL        DOI    10.1371/JOURNAL.PBIO.1000426                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0055                                      
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 68546                          
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) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2134                            
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4950                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3770                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 176                          
REMARK   3   BIN FREE R VALUE                    : 0.3690                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13912                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 62                                      
REMARK   3   SOLVENT ATOMS            : 93                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 84.77                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.22000                                             
REMARK   3    B22 (A**2) : -2.28000                                             
REMARK   3    B33 (A**2) : 2.08000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.90000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.619         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.303         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.225         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.450        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 14290 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  9184 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 19397 ; 1.362 ; 1.918       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 22274 ; 0.898 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1759 ; 6.480 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   737 ;36.304 ;24.193       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2135 ;14.463 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    81 ;18.693 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2094 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 16307 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2994 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  8893 ; 0.608 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14162 ; 1.198 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5397 ; 2.082 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5235 ; 3.508 ; 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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A D E F G H I J K L N           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    343       A     402      1                      
REMARK   3           1     D    343       D     402      1                      
REMARK   3           1     E    343       E     402      1                      
REMARK   3           1     F    343       F     402      1                      
REMARK   3           1     G    343       G     402      1                      
REMARK   3           1     H    343       H     402      1                      
REMARK   3           1     I    343       I     402      1                      
REMARK   3           1     J    343       J     402      1                      
REMARK   3           1     K    343       K     402      1                      
REMARK   3           1     L    343       L     402      1                      
REMARK   3           1     N    343       N     402      1                      
REMARK   3           2     A    409       A     471      1                      
REMARK   3           2     D    409       D     471      1                      
REMARK   3           2     E    409       E     471      1                      
REMARK   3           2     F    409       F     471      1                      
REMARK   3           2     G    409       G     471      1                      
REMARK   3           2     H    409       H     471      1                      
REMARK   3           2     I    409       I     471      1                      
REMARK   3           2     J    409       J     471      1                      
REMARK   3           2     K    409       K     471      1                      
REMARK   3           2     L    409       L     471      1                      
REMARK   3           2     N    409       N     471      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1556 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   1556 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    E    (A):   1556 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    F    (A):   1556 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    G    (A):   1556 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    H    (A):   1556 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    I    (A):   1556 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    J    (A):   1556 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    K    (A):   1556 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    L    (A):   1556 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    N    (A):   1556 ;  0.03 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1556 ;  1.84 ;  5.00           
REMARK   3   TIGHT THERMAL      1    D (A**2):   1556 ;  1.82 ;  5.00           
REMARK   3   TIGHT THERMAL      1    E (A**2):   1556 ;  1.60 ;  5.00           
REMARK   3   TIGHT THERMAL      1    F (A**2):   1556 ;  1.50 ;  5.00           
REMARK   3   TIGHT THERMAL      1    G (A**2):   1556 ;  1.14 ;  5.00           
REMARK   3   TIGHT THERMAL      1    H (A**2):   1556 ;  1.16 ;  5.00           
REMARK   3   TIGHT THERMAL      1    I (A**2):   1556 ;  1.20 ;  5.00           
REMARK   3   TIGHT THERMAL      1    J (A**2):   1556 ;  1.43 ;  5.00           
REMARK   3   TIGHT THERMAL      1    K (A**2):   1556 ;  1.67 ;  5.00           
REMARK   3   TIGHT THERMAL      1    L (A**2):   1556 ;  1.95 ;  5.00           
REMARK   3   TIGHT THERMAL      1    N (A**2):   1556 ;  1.61 ;  5.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B C M                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B    343       B     402      1                      
REMARK   3           1     C    343       C     402      1                      
REMARK   3           1     M    343       M     402      1                      
REMARK   3           2     B    409       B     471      1                      
REMARK   3           2     C    409       C     471      1                      
REMARK   3           2     M    409       M     471      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):   1598 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    C    (A):   1598 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    M    (A):   1598 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      2    B (A**2):   1598 ;  1.48 ;  5.00           
REMARK   3   TIGHT THERMAL      2    C (A**2):   1598 ;  1.62 ;  5.00           
REMARK   3   TIGHT THERMAL      2    M (A**2):   1598 ;  2.15 ;  5.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
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   339        A   471                          
REMARK   3    ORIGIN FOR THE GROUP (A): -42.5432  63.9511  12.6764              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1563 T22:   0.0922                                     
REMARK   3      T33:   0.0430 T12:   0.0101                                     
REMARK   3      T13:   0.0004 T23:   0.0260                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8205 L22:   4.4545                                     
REMARK   3      L33:   4.3508 L12:   1.4173                                     
REMARK   3      L13:   0.4340 L23:  -0.2606                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2429 S12:   0.4447 S13:   0.3185                       
REMARK   3      S21:  -0.5094 S22:   0.0348 S23:   0.0792                       
REMARK   3      S31:  -0.3824 S32:   0.0193 S33:   0.2081                       
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 :   B   340        B   471                          
REMARK   3    ORIGIN FOR THE GROUP (A): -51.7778  32.6386   4.6694              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0849 T22:   0.1561                                     
REMARK   3      T33:   0.0564 T12:  -0.0280                                     
REMARK   3      T13:   0.0382 T23:  -0.0407                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6650 L22:   4.3511                                     
REMARK   3      L33:   4.2996 L12:   0.2293                                     
REMARK   3      L13:   0.4040 L23:  -0.5521                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0357 S12:   0.5810 S13:  -0.0292                       
REMARK   3      S21:  -0.4465 S22:   0.0646 S23:   0.0302                       
REMARK   3      S31:   0.1588 S32:  -0.0280 S33:  -0.1004                       
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 :   C   341        C   471                          
REMARK   3    ORIGIN FOR THE GROUP (A): -55.9774   7.1299  30.0281              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0700 T22:   0.1985                                     
REMARK   3      T33:   0.1450 T12:  -0.0307                                     
REMARK   3      T13:   0.0755 T23:   0.0394                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2473 L22:   4.1220                                     
REMARK   3      L33:   5.8783 L12:  -0.8589                                     
REMARK   3      L13:   0.8385 L23:  -0.5388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0731 S12:  -0.1220 S13:  -0.3326                       
REMARK   3      S21:   0.3487 S22:   0.0701 S23:   0.5329                       
REMARK   3      S31:   0.1309 S32:  -0.5968 S33:  -0.1432                       
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 :   D   342        D   471                          
REMARK   3    ORIGIN FOR THE GROUP (A): -38.9908   3.5920  15.4671              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1171 T22:   0.0973                                     
REMARK   3      T33:   0.1163 T12:   0.0464                                     
REMARK   3      T13:   0.0088 T23:  -0.0488                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3457 L22:   4.9510                                     
REMARK   3      L33:   5.2615 L12:  -0.6917                                     
REMARK   3      L13:   0.0706 L23:  -1.3609                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1944 S12:   0.2298 S13:  -0.4104                       
REMARK   3      S21:  -0.3743 S22:  -0.0989 S23:   0.0099                       
REMARK   3      S31:   0.4571 S32:   0.2024 S33:  -0.0955                       
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   338        E   471                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.5243  49.7121  69.0274              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2943 T22:   0.2002                                     
REMARK   3      T33:   0.0517 T12:  -0.0627                                     
REMARK   3      T13:   0.0149 T23:   0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9044 L22:   4.2869                                     
REMARK   3      L33:   3.6292 L12:  -1.4330                                     
REMARK   3      L13:   0.2335 L23:  -0.4125                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0935 S12:  -0.7033 S13:   0.1428                       
REMARK   3      S21:   0.8637 S22:  -0.1420 S23:  -0.0082                       
REMARK   3      S31:  -0.4031 S32:  -0.0759 S33:   0.2355                       
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 :   F   341        F   471                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.5537  73.4646  33.0343              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1799 T22:   0.1075                                     
REMARK   3      T33:   0.2036 T12:  -0.0323                                     
REMARK   3      T13:  -0.0422 T23:   0.0882                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0127 L22:   3.0232                                     
REMARK   3      L33:   5.1166 L12:  -0.6214                                     
REMARK   3      L13:   0.3013 L23:  -0.2615                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0207 S12:   0.5341 S13:   0.4533                       
REMARK   3      S21:  -0.2039 S22:  -0.1053 S23:  -0.3165                       
REMARK   3      S31:  -0.4231 S32:   0.3248 S33:   0.1260                       
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 :   G   341        G   471                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.7753  -1.7482  36.7319              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1742 T22:   0.1272                                     
REMARK   3      T33:   0.3195 T12:   0.1222                                     
REMARK   3      T13:  -0.0755 T23:  -0.0576                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2329 L22:   2.9157                                     
REMARK   3      L33:   4.5617 L12:   0.8156                                     
REMARK   3      L13:  -0.3170 L23:   0.8896                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1435 S12:   0.2657 S13:  -0.4357                       
REMARK   3      S21:  -0.1368 S22:   0.1111 S23:  -0.6023                       
REMARK   3      S31:   0.5855 S32:   0.5074 S33:  -0.2546                       
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 :   H   339        H   471                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.2509  54.1804  50.7229              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0802 T22:   0.2213                                     
REMARK   3      T33:   0.2013 T12:  -0.0909                                     
REMARK   3      T13:   0.0125 T23:   0.1332                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8186 L22:   6.6483                                     
REMARK   3      L33:   4.3855 L12:  -1.7969                                     
REMARK   3      L13:   0.0262 L23:  -0.5044                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0037 S12:   0.2862 S13:   0.2042                       
REMARK   3      S21:  -0.0076 S22:  -0.3379 S23:  -0.6312                       
REMARK   3      S31:  -0.3331 S32:   0.6430 S33:   0.3415                       
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 :   I   338        I   471                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.6352  21.1579  52.9381              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0165 T22:   0.1797                                     
REMARK   3      T33:   0.4549 T12:   0.0123                                     
REMARK   3      T13:  -0.0044 T23:  -0.0734                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8513 L22:   4.9341                                     
REMARK   3      L33:   5.3909 L12:  -0.0567                                     
REMARK   3      L13:   0.2242 L23:   1.2269                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1593 S12:   0.3100 S13:  -0.0732                       
REMARK   3      S21:   0.1078 S22:   0.0085 S23:  -0.9204                       
REMARK   3      S31:  -0.0600 S32:   0.6302 S33:  -0.1678                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J   342        J   471                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.9937  72.3353  52.9332              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3313 T22:   0.0974                                     
REMARK   3      T33:   0.1614 T12:  -0.0059                                     
REMARK   3      T13:   0.0099 T23:  -0.0987                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5296 L22:   2.5454                                     
REMARK   3      L33:   4.5847 L12:  -0.2235                                     
REMARK   3      L13:   0.3102 L23:  -0.2790                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0678 S12:  -0.4564 S13:   0.3417                       
REMARK   3      S21:   0.6409 S22:  -0.0287 S23:   0.2682                       
REMARK   3      S31:  -0.4806 S32:  -0.2015 S33:   0.0965                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K   342        K   471                          
REMARK   3    ORIGIN FOR THE GROUP (A): -53.2340  66.4763  32.2959              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1810 T22:   0.2158                                     
REMARK   3      T33:   0.1564 T12:   0.0816                                     
REMARK   3      T13:   0.0940 T23:  -0.0830                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1636 L22:   5.6373                                     
REMARK   3      L33:   4.1634 L12:   1.4351                                     
REMARK   3      L13:   0.1484 L23:   0.5159                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0331 S12:  -0.4779 S13:   0.3280                       
REMARK   3      S21:   0.3104 S22:  -0.1853 S23:   0.4708                       
REMARK   3      S31:  -0.4515 S32:  -0.5645 S33:   0.2184                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   340        L   471                          
REMARK   3    ORIGIN FOR THE GROUP (A): -65.4282  37.8326  22.0234              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0506 T22:   0.2904                                     
REMARK   3      T33:   0.0778 T12:   0.0323                                     
REMARK   3      T13:   0.0601 T23:   0.0490                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1402 L22:   5.5484                                     
REMARK   3      L33:   5.1591 L12:   0.5754                                     
REMARK   3      L13:  -0.4822 L23:  -0.9225                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1948 S12:  -0.3700 S13:   0.1787                       
REMARK   3      S21:   0.3424 S22:   0.0746 S23:   0.4104                       
REMARK   3      S31:  -0.1416 S32:  -0.8634 S33:  -0.2693                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M   343        M   471                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.6530  -2.5475  50.4661              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2986 T22:   0.0966                                     
REMARK   3      T33:   0.2119 T12:  -0.1019                                     
REMARK   3      T13:  -0.0504 T23:   0.0872                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8200 L22:   2.7834                                     
REMARK   3      L33:   4.0696 L12:  -0.3652                                     
REMARK   3      L13:   0.7545 L23:   0.3345                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2701 S12:  -0.4789 S13:  -0.5567                       
REMARK   3      S21:   0.5008 S22:  -0.0321 S23:   0.1489                       
REMARK   3      S31:   0.5616 S32:  -0.3773 S33:  -0.2381                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   N   336        N   471                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.7902  15.7943  67.6527              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2946 T22:   0.1539                                     
REMARK   3      T33:   0.2060 T12:  -0.0362                                     
REMARK   3      T13:  -0.0290 T23:   0.0363                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7661 L22:   4.6268                                     
REMARK   3      L33:   3.3588 L12:  -0.5518                                     
REMARK   3      L13:   0.0666 L23:   0.6687                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1637 S12:  -0.4747 S13:  -0.0679                       
REMARK   3      S21:   0.8944 S22:  -0.0507 S23:  -0.0198                       
REMARK   3      S31:   0.3792 S32:  -0.2787 S33:  -0.1129                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. U VALUES RESIDUAL ONLY. A BOUND ACETATE ION HAS BEEN     
REMARK   3  MODELLED IN EACH MONOMER HOWEVER THE DIFFERENCE DENSITY SUGGESTS    
REMARK   3  THAT THE TRUE BOUND MOIETY IS A LARGER CARBOXYLATE CONTAINING       
REMARK   3  ENTITY. STRONG DIFFERENCE DENSITY BETWEEN SYMMETRY-RELATED          
REMARK   3  OLIGOMERIC RINGS HAS BEEN MODELLED BY PARTIALLY-OCCUPIED CADMIUM    
REMARK   3  IONS WHICH WERE PRESENT IN THE CRYSTALLIZATION SOLUTION.            
REMARK   4                                                                      
REMARK   4 2W2C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-OCT-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290037996.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUL-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97888                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 323492                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.860                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.76000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 1HKX,2UX0,2F86                           
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG400, 0.1M CADMIUM CHLORIDE,       
REMARK 280  0.1M SODIUM ACETATE PH4.6                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       74.77300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.90150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       74.77300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       58.90150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRADECAMERIC                    
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRADECAMERIC             
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 34340 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 76090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -224.4 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   332                                                      
REMARK 465     MET A   333                                                      
REMARK 465     SER A   334                                                      
REMARK 465     ASN A   335                                                      
REMARK 465     THR A   336                                                      
REMARK 465     THR A   337                                                      
REMARK 465     ILE A   338                                                      
REMARK 465     LEU A   403                                                      
REMARK 465     SER A   404                                                      
REMARK 465     LYS A   405                                                      
REMARK 465     SER A   406                                                      
REMARK 465     ASN A   407                                                      
REMARK 465     SER A   472                                                      
REMARK 465     PRO A   473                                                      
REMARK 465     THR A   474                                                      
REMARK 465     VAL A   475                                                      
REMARK 465     SER B   332                                                      
REMARK 465     MET B   333                                                      
REMARK 465     SER B   334                                                      
REMARK 465     ASN B   335                                                      
REMARK 465     THR B   336                                                      
REMARK 465     THR B   337                                                      
REMARK 465     ILE B   338                                                      
REMARK 465     GLU B   339                                                      
REMARK 465     SER B   404                                                      
REMARK 465     LYS B   405                                                      
REMARK 465     SER B   406                                                      
REMARK 465     ASN B   407                                                      
REMARK 465     SER B   472                                                      
REMARK 465     PRO B   473                                                      
REMARK 465     THR B   474                                                      
REMARK 465     VAL B   475                                                      
REMARK 465     SER C   332                                                      
REMARK 465     MET C   333                                                      
REMARK 465     SER C   334                                                      
REMARK 465     ASN C   335                                                      
REMARK 465     THR C   336                                                      
REMARK 465     THR C   337                                                      
REMARK 465     ILE C   338                                                      
REMARK 465     GLU C   339                                                      
REMARK 465     ASP C   340                                                      
REMARK 465     LEU C   403                                                      
REMARK 465     SER C   404                                                      
REMARK 465     LYS C   405                                                      
REMARK 465     SER C   406                                                      
REMARK 465     SER C   472                                                      
REMARK 465     PRO C   473                                                      
REMARK 465     THR C   474                                                      
REMARK 465     VAL C   475                                                      
REMARK 465     SER D   332                                                      
REMARK 465     MET D   333                                                      
REMARK 465     SER D   334                                                      
REMARK 465     ASN D   335                                                      
REMARK 465     THR D   336                                                      
REMARK 465     THR D   337                                                      
REMARK 465     ILE D   338                                                      
REMARK 465     GLU D   339                                                      
REMARK 465     ASP D   340                                                      
REMARK 465     GLU D   341                                                      
REMARK 465     LEU D   403                                                      
REMARK 465     SER D   404                                                      
REMARK 465     LYS D   405                                                      
REMARK 465     SER D   406                                                      
REMARK 465     ASN D   407                                                      
REMARK 465     SER D   472                                                      
REMARK 465     PRO D   473                                                      
REMARK 465     THR D   474                                                      
REMARK 465     VAL D   475                                                      
REMARK 465     SER E   332                                                      
REMARK 465     MET E   333                                                      
REMARK 465     SER E   334                                                      
REMARK 465     ASN E   335                                                      
REMARK 465     THR E   336                                                      
REMARK 465     THR E   337                                                      
REMARK 465     LEU E   403                                                      
REMARK 465     SER E   404                                                      
REMARK 465     LYS E   405                                                      
REMARK 465     SER E   406                                                      
REMARK 465     ASN E   407                                                      
REMARK 465     SER E   472                                                      
REMARK 465     PRO E   473                                                      
REMARK 465     THR E   474                                                      
REMARK 465     VAL E   475                                                      
REMARK 465     SER F   332                                                      
REMARK 465     MET F   333                                                      
REMARK 465     SER F   334                                                      
REMARK 465     ASN F   335                                                      
REMARK 465     THR F   336                                                      
REMARK 465     THR F   337                                                      
REMARK 465     ILE F   338                                                      
REMARK 465     GLU F   339                                                      
REMARK 465     ASP F   340                                                      
REMARK 465     LEU F   403                                                      
REMARK 465     SER F   404                                                      
REMARK 465     LYS F   405                                                      
REMARK 465     SER F   406                                                      
REMARK 465     ASN F   407                                                      
REMARK 465     SER F   472                                                      
REMARK 465     PRO F   473                                                      
REMARK 465     THR F   474                                                      
REMARK 465     VAL F   475                                                      
REMARK 465     SER G   332                                                      
REMARK 465     MET G   333                                                      
REMARK 465     SER G   334                                                      
REMARK 465     ASN G   335                                                      
REMARK 465     THR G   336                                                      
REMARK 465     THR G   337                                                      
REMARK 465     ILE G   338                                                      
REMARK 465     GLU G   339                                                      
REMARK 465     ASP G   340                                                      
REMARK 465     LEU G   403                                                      
REMARK 465     SER G   404                                                      
REMARK 465     LYS G   405                                                      
REMARK 465     SER G   406                                                      
REMARK 465     SER G   472                                                      
REMARK 465     PRO G   473                                                      
REMARK 465     THR G   474                                                      
REMARK 465     VAL G   475                                                      
REMARK 465     SER H   332                                                      
REMARK 465     MET H   333                                                      
REMARK 465     SER H   334                                                      
REMARK 465     ASN H   335                                                      
REMARK 465     THR H   336                                                      
REMARK 465     THR H   337                                                      
REMARK 465     ILE H   338                                                      
REMARK 465     LYS H   405                                                      
REMARK 465     SER H   406                                                      
REMARK 465     SER H   472                                                      
REMARK 465     PRO H   473                                                      
REMARK 465     THR H   474                                                      
REMARK 465     VAL H   475                                                      
REMARK 465     SER I   332                                                      
REMARK 465     MET I   333                                                      
REMARK 465     SER I   334                                                      
REMARK 465     ASN I   335                                                      
REMARK 465     THR I   336                                                      
REMARK 465     THR I   337                                                      
REMARK 465     LEU I   403                                                      
REMARK 465     SER I   404                                                      
REMARK 465     LYS I   405                                                      
REMARK 465     SER I   406                                                      
REMARK 465     ASN I   407                                                      
REMARK 465     LYS I   408                                                      
REMARK 465     SER I   472                                                      
REMARK 465     PRO I   473                                                      
REMARK 465     THR I   474                                                      
REMARK 465     VAL I   475                                                      
REMARK 465     SER J   332                                                      
REMARK 465     MET J   333                                                      
REMARK 465     SER J   334                                                      
REMARK 465     ASN J   335                                                      
REMARK 465     THR J   336                                                      
REMARK 465     THR J   337                                                      
REMARK 465     ILE J   338                                                      
REMARK 465     GLU J   339                                                      
REMARK 465     ASP J   340                                                      
REMARK 465     GLU J   341                                                      
REMARK 465     LEU J   403                                                      
REMARK 465     SER J   404                                                      
REMARK 465     LYS J   405                                                      
REMARK 465     SER J   406                                                      
REMARK 465     ASN J   407                                                      
REMARK 465     SER J   472                                                      
REMARK 465     PRO J   473                                                      
REMARK 465     THR J   474                                                      
REMARK 465     VAL J   475                                                      
REMARK 465     SER K   332                                                      
REMARK 465     MET K   333                                                      
REMARK 465     SER K   334                                                      
REMARK 465     ASN K   335                                                      
REMARK 465     THR K   336                                                      
REMARK 465     THR K   337                                                      
REMARK 465     ILE K   338                                                      
REMARK 465     GLU K   339                                                      
REMARK 465     ASP K   340                                                      
REMARK 465     GLU K   341                                                      
REMARK 465     LEU K   403                                                      
REMARK 465     SER K   404                                                      
REMARK 465     LYS K   405                                                      
REMARK 465     SER K   472                                                      
REMARK 465     PRO K   473                                                      
REMARK 465     THR K   474                                                      
REMARK 465     VAL K   475                                                      
REMARK 465     SER L   332                                                      
REMARK 465     MET L   333                                                      
REMARK 465     SER L   334                                                      
REMARK 465     ASN L   335                                                      
REMARK 465     THR L   336                                                      
REMARK 465     THR L   337                                                      
REMARK 465     ILE L   338                                                      
REMARK 465     GLU L   339                                                      
REMARK 465     LYS L   405                                                      
REMARK 465     SER L   406                                                      
REMARK 465     SER L   472                                                      
REMARK 465     PRO L   473                                                      
REMARK 465     THR L   474                                                      
REMARK 465     VAL L   475                                                      
REMARK 465     SER M   332                                                      
REMARK 465     MET M   333                                                      
REMARK 465     SER M   334                                                      
REMARK 465     ASN M   335                                                      
REMARK 465     THR M   336                                                      
REMARK 465     THR M   337                                                      
REMARK 465     ILE M   338                                                      
REMARK 465     GLU M   339                                                      
REMARK 465     ASP M   340                                                      
REMARK 465     GLU M   341                                                      
REMARK 465     ASP M   342                                                      
REMARK 465     LEU M   403                                                      
REMARK 465     SER M   404                                                      
REMARK 465     LYS M   405                                                      
REMARK 465     SER M   406                                                      
REMARK 465     SER M   472                                                      
REMARK 465     PRO M   473                                                      
REMARK 465     THR M   474                                                      
REMARK 465     VAL M   475                                                      
REMARK 465     SER N   332                                                      
REMARK 465     MET N   333                                                      
REMARK 465     SER N   334                                                      
REMARK 465     ASN N   335                                                      
REMARK 465     LEU N   403                                                      
REMARK 465     SER N   404                                                      
REMARK 465     LYS N   405                                                      
REMARK 465     SER N   406                                                      
REMARK 465     ASN N   407                                                      
REMARK 465     SER N   472                                                      
REMARK 465     PRO N   473                                                      
REMARK 465     THR N   474                                                      
REMARK 465     VAL N   475                                                      
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 339    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 340    CG   OD1  OD2                                       
REMARK 470     GLU A 341    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 343    CG1  CG2                                            
REMARK 470     LYS A 344    CE   NZ                                             
REMARK 470     LYS A 352    NZ                                                  
REMARK 470     LYS A 371    CD   CE   NZ                                        
REMARK 470     LYS A 408    CG   CD   CE   NZ                                   
REMARK 470     ASP A 424    CG   OD1  OD2                                       
REMARK 470     SER A 441    OG                                                  
REMARK 470     LYS A 445    CG   CD   CE   NZ                                   
REMARK 470     ARG A 458    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 461    CG   CD   CE   NZ                                   
REMARK 470     GLU B 341    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 344    CE   NZ                                             
REMARK 470     LYS B 352    CD   CE   NZ                                        
REMARK 470     LYS B 371    CE   NZ                                             
REMARK 470     LEU B 403    CD1  CD2                                            
REMARK 470     LYS B 408    CG   CD   CE   NZ                                   
REMARK 470     SER B 441    OG                                                  
REMARK 470     LYS B 445    CD   CE   NZ                                        
REMARK 470     ARG B 458    NE   CZ   NH1  NH2                                  
REMARK 470     GLU C 341    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 344    CD   CE   NZ                                        
REMARK 470     LYS C 352    CD   CE   NZ                                        
REMARK 470     LYS C 371    CE   NZ                                             
REMARK 470     LYS C 408    CG   CD   CE   NZ                                   
REMARK 470     ASP C 424    CG   OD1  OD2                                       
REMARK 470     SER C 441    OG                                                  
REMARK 470     LYS C 445    CD   CE   NZ                                        
REMARK 470     ARG C 458    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 459    CG   OD1  OD2                                       
REMARK 470     LYS C 461    CG   CD   CE   NZ                                   
REMARK 470     LYS D 344    CG   CD   CE   NZ                                   
REMARK 470     LYS D 352    CD   CE   NZ                                        
REMARK 470     LYS D 408    CG   CD   CE   NZ                                   
REMARK 470     ASP D 424    CG   OD1  OD2                                       
REMARK 470     SER D 441    OG                                                  
REMARK 470     ARG D 458    NE   CZ   NH1  NH2                                  
REMARK 470     LYS D 461    CG   CD   CE   NZ                                   
REMARK 470     ILE E 338    CG1  CG2  CD1                                       
REMARK 470     GLU E 339    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 341    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 344    CG   CD   CE   NZ                                   
REMARK 470     LYS E 352    CG   CD   CE   NZ                                   
REMARK 470     GLU E 367    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 371    CG   CD   CE   NZ                                   
REMARK 470     LYS E 408    CG   CD   CE   NZ                                   
REMARK 470     ASP E 424    CG   OD1  OD2                                       
REMARK 470     SER E 441    OG                                                  
REMARK 470     MET E 443    SD   CE                                             
REMARK 470     LYS E 445    CG   CD   CE   NZ                                   
REMARK 470     ARG E 458    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E 461    CG   CD   CE   NZ                                   
REMARK 470     GLU F 341    CG   CD   OE1  OE2                                  
REMARK 470     VAL F 343    CG1  CG2                                            
REMARK 470     LYS F 344    CD   CE   NZ                                        
REMARK 470     LYS F 352    CD   CE   NZ                                        
REMARK 470     GLU F 367    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 371    CG   CD   CE   NZ                                   
REMARK 470     SER F 441    OG                                                  
REMARK 470     LYS F 445    CD   CE   NZ                                        
REMARK 470     ARG F 458    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F 461    CG   CD   CE   NZ                                   
REMARK 470     GLU G 341    CG   CD   OE1  OE2                                  
REMARK 470     VAL G 343    CG1  CG2                                            
REMARK 470     LYS G 344    CG   CD   CE   NZ                                   
REMARK 470     LYS G 352    CD   CE   NZ                                        
REMARK 470     GLU G 367    CG   CD   OE1  OE2                                  
REMARK 470     LYS G 371    CG   CD   CE   NZ                                   
REMARK 470     LYS G 408    CG   CD   CE   NZ                                   
REMARK 470     SER G 441    OG                                                  
REMARK 470     MET G 443    CG   SD   CE                                        
REMARK 470     LYS G 445    CD   CE   NZ                                        
REMARK 470     ARG G 458    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU H 339    CG   CD   OE1  OE2                                  
REMARK 470     ASP H 340    CG   OD1  OD2                                       
REMARK 470     GLU H 341    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 344    CG   CD   CE   NZ                                   
REMARK 470     LYS H 352    CD   CE   NZ                                        
REMARK 470     GLU H 367    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 371    CE   NZ                                             
REMARK 470     LEU H 403    CG   CD1  CD2                                       
REMARK 470     LYS H 408    CG   CD   CE   NZ                                   
REMARK 470     SER H 441    OG                                                  
REMARK 470     MET H 443    CG   SD   CE                                        
REMARK 470     LYS H 445    CG   CD   CE   NZ                                   
REMARK 470     ARG H 458    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS H 461    CG   CD   CE   NZ                                   
REMARK 470     ILE I 338    CG1  CG2  CD1                                       
REMARK 470     GLU I 339    CG   CD   OE1  OE2                                  
REMARK 470     GLU I 341    CG   CD   OE1  OE2                                  
REMARK 470     LYS I 344    CD   CE   NZ                                        
REMARK 470     ARG I 346    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS I 352    CE   NZ                                             
REMARK 470     LYS I 371    CG   CD   CE   NZ                                   
REMARK 470     ASP I 424    CG   OD1  OD2                                       
REMARK 470     ASP I 425    CG   OD1  OD2                                       
REMARK 470     SER I 441    OG                                                  
REMARK 470     MET I 443    SD   CE                                             
REMARK 470     LYS I 445    CD   CE   NZ                                        
REMARK 470     ARG I 458    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP I 459    CG   OD1  OD2                                       
REMARK 470     LYS I 461    CG   CD   CE   NZ                                   
REMARK 470     ASP J 342    CG   OD1  OD2                                       
REMARK 470     LYS J 344    CG   CD   CE   NZ                                   
REMARK 470     ARG J 346    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS J 352    CD   CE   NZ                                        
REMARK 470     LYS J 371    CG   CD   CE   NZ                                   
REMARK 470     LYS J 408    CG   CD   CE   NZ                                   
REMARK 470     SER J 441    OG                                                  
REMARK 470     LYS J 445    CE   NZ                                             
REMARK 470     ARG J 458    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP J 459    CG   OD1  OD2                                       
REMARK 470     LYS J 461    CG   CD   CE   NZ                                   
REMARK 470     ASP K 342    CG   OD1  OD2                                       
REMARK 470     LYS K 344    CG   CD   CE   NZ                                   
REMARK 470     LYS K 352    CD   CE   NZ                                        
REMARK 470     GLU K 367    CG   CD   OE1  OE2                                  
REMARK 470     SER K 406    OG                                                  
REMARK 470     ASN K 407    CG   OD1  ND2                                       
REMARK 470     LYS K 408    CG   CD   CE   NZ                                   
REMARK 470     ASP K 424    CG   OD1  OD2                                       
REMARK 470     SER K 441    OG                                                  
REMARK 470     LYS K 445    CD   CE   NZ                                        
REMARK 470     ARG K 458    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP K 459    CG   OD1  OD2                                       
REMARK 470     LYS K 461    CG   CD   CE   NZ                                   
REMARK 470     ASP L 340    CG   OD1  OD2                                       
REMARK 470     GLU L 341    CG   CD   OE1  OE2                                  
REMARK 470     LYS L 344    CD   CE   NZ                                        
REMARK 470     LYS L 352    CE   NZ                                             
REMARK 470     LYS L 371    CG   CD   CE   NZ                                   
REMARK 470     LEU L 403    CG   CD1  CD2                                       
REMARK 470     ASN L 407    CG   OD1  ND2                                       
REMARK 470     LYS L 408    CG   CD   CE   NZ                                   
REMARK 470     SER L 441    OG                                                  
REMARK 470     ARG L 458    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS L 461    CG   CD   CE   NZ                                   
REMARK 470     LYS M 344    CD   CE   NZ                                        
REMARK 470     LYS M 352    CE   NZ                                             
REMARK 470     GLU M 367    CG   CD   OE1  OE2                                  
REMARK 470     LYS M 371    CE   NZ                                             
REMARK 470     ASN M 407    CG   OD1  ND2                                       
REMARK 470     LYS M 408    CD   CE   NZ                                        
REMARK 470     SER M 441    OG                                                  
REMARK 470     MET M 443    SD   CE                                             
REMARK 470     LYS M 445    CD   CE   NZ                                        
REMARK 470     ARG M 458    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP M 459    CG   OD1  OD2                                       
REMARK 470     LYS M 461    CG   CD   CE   NZ                                   
REMARK 470     THR N 336    OG1  CG2                                            
REMARK 470     GLU N 339    CD   OE1  OE2                                       
REMARK 470     LYS N 344    CG   CD   CE   NZ                                   
REMARK 470     ARG N 346    NE   CZ   NH1  NH2                                  
REMARK 470     LYS N 352    CD   CE   NZ                                        
REMARK 470     GLU N 367    CG   CD   OE1  OE2                                  
REMARK 470     LYS N 371    CD   CE   NZ                                        
REMARK 470     LYS N 408    CG   CD   CE   NZ                                   
REMARK 470     ASP N 424    CG   OD1  OD2                                       
REMARK 470     SER N 441    OG                                                  
REMARK 470     ARG N 458    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP N 459    CG   OD1  OD2                                       
REMARK 470     LYS N 461    CG   CD   CE   NZ                                   
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   ND1  HIS F   420     O    HOH F  2003              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD2  ASP C   365     OE2  GLU H   359     3445     2.11            
REMARK 500   O    GLU I   400     NZ   LYS K   371     3545     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    CYS M 428   CB    CYS M 428   SG     -0.119                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 441        6.12    -69.74                                   
REMARK 500    ASP A 459       45.23     38.38                                   
REMARK 500    SER B 441        7.36    -62.55                                   
REMARK 500    ASP B 459       56.35     27.51                                   
REMARK 500    SER C 441        7.03    -64.68                                   
REMARK 500    ASP C 459       56.30     25.72                                   
REMARK 500    SER D 441        3.86    -68.89                                   
REMARK 500    SER E 441        0.76    -67.02                                   
REMARK 500    SER F 441        3.03    -68.48                                   
REMARK 500    ASP F 459       45.71     38.24                                   
REMARK 500    SER G 441        2.95    -68.11                                   
REMARK 500    SER H 441        3.58    -67.88                                   
REMARK 500    ASP H 459       44.76     40.00                                   
REMARK 500    SER I 441        3.54    -68.11                                   
REMARK 500    ASP I 459       44.07     38.85                                   
REMARK 500    SER J 441        4.24    -68.67                                   
REMARK 500    ASN K 407       42.68    -99.04                                   
REMARK 500    SER K 441        4.28    -69.22                                   
REMARK 500    ASP K 459       45.70     39.55                                   
REMARK 500    LEU L 403      -97.86    -97.37                                   
REMARK 500    SER L 441        5.33    -69.51                                   
REMARK 500    ASP L 459       44.97     38.33                                   
REMARK 500    SER M 441        5.76    -64.67                                   
REMARK 500    ASP M 459       52.17     25.15                                   
REMARK 500    SER N 441        1.23    -67.34                                   
REMARK 500    ASP N 459       46.35     39.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD B1472  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 425   OD1                                                    
REMARK 620 2 ASP B 425   OD2  49.2                                              
REMARK 620 3 ASP L 425   OD2  67.0  58.7                                        
REMARK 620 4 HOH B2006   O   118.6  70.8  94.9                                  
REMARK 620 5 HOH B2009   O    97.0 145.1 122.3 137.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD F1472  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 425   OD1                                                    
REMARK 620 2 ASP F 425   OD2  51.6                                              
REMARK 620 3 ASP G 425   OD2 126.3 103.9                                        
REMARK 620 4 HOH G2005   O   113.3  62.5  59.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD H1472  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP N 425   OD1                                                    
REMARK 620 2 ASP H 424   OD2 137.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD J1472  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP J 425   OD2                                                    
REMARK 620 2 ASP M 425   OD2 106.4                                              
REMARK 620 3  CD J1474  CD    59.6  75.3                                        
REMARK 620 4 ASP J 425   OD1  50.0 141.0  65.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD J1473  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP J 424   OD1                                                    
REMARK 620 2 ASP J 424   OD2  53.7                                              
REMARK 620 3 ASP G 424   OD2  83.7  84.8                                        
REMARK 620 4 ASP G 424   OD1 112.3  72.2  51.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT G 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT H 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT I 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT J 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT K 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT L 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT M 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT N 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD H 1472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD F 1472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD J 1472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD J 1473                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD J 1474                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VN9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CALCIUM CALMODULIN DEPENDENT PROTEIN      
REMARK 900 KINASE II DELTA ISOFORM 1, CAMKD                                     
DBREF  2W2C A  332   333  PDB    2W2C     2W2C           332    333             
DBREF  2W2C A  334   475  UNP    Q13557   KCC2D_HUMAN    334    475             
DBREF  2W2C B  332   333  PDB    2W2C     2W2C           332    333             
DBREF  2W2C B  334   475  UNP    Q13557   KCC2D_HUMAN    334    475             
DBREF  2W2C C  332   333  PDB    2W2C     2W2C           332    333             
DBREF  2W2C C  334   475  UNP    Q13557   KCC2D_HUMAN    334    475             
DBREF  2W2C D  332   333  PDB    2W2C     2W2C           332    333             
DBREF  2W2C D  334   475  UNP    Q13557   KCC2D_HUMAN    334    475             
DBREF  2W2C E  332   333  PDB    2W2C     2W2C           332    333             
DBREF  2W2C E  334   475  UNP    Q13557   KCC2D_HUMAN    334    475             
DBREF  2W2C F  332   333  PDB    2W2C     2W2C           332    333             
DBREF  2W2C F  334   475  UNP    Q13557   KCC2D_HUMAN    334    475             
DBREF  2W2C G  332   333  PDB    2W2C     2W2C           332    333             
DBREF  2W2C G  334   475  UNP    Q13557   KCC2D_HUMAN    334    475             
DBREF  2W2C H  332   333  PDB    2W2C     2W2C           332    333             
DBREF  2W2C H  334   475  UNP    Q13557   KCC2D_HUMAN    334    475             
DBREF  2W2C I  332   333  PDB    2W2C     2W2C           332    333             
DBREF  2W2C I  334   475  UNP    Q13557   KCC2D_HUMAN    334    475             
DBREF  2W2C J  332   333  PDB    2W2C     2W2C           332    333             
DBREF  2W2C J  334   475  UNP    Q13557   KCC2D_HUMAN    334    475             
DBREF  2W2C K  332   333  PDB    2W2C     2W2C           332    333             
DBREF  2W2C K  334   475  UNP    Q13557   KCC2D_HUMAN    334    475             
DBREF  2W2C L  332   333  PDB    2W2C     2W2C           332    333             
DBREF  2W2C L  334   475  UNP    Q13557   KCC2D_HUMAN    334    475             
DBREF  2W2C M  332   333  PDB    2W2C     2W2C           332    333             
DBREF  2W2C M  334   475  UNP    Q13557   KCC2D_HUMAN    334    475             
DBREF  2W2C N  332   333  PDB    2W2C     2W2C           332    333             
DBREF  2W2C N  334   475  UNP    Q13557   KCC2D_HUMAN    334    475             
SEQRES   1 A  144  SER MET SER ASN THR THR ILE GLU ASP GLU ASP VAL LYS          
SEQRES   2 A  144  ALA ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 A  144  ILE GLU ALA ILE ASN ASN GLY ASP PHE GLU ALA TYR THR          
SEQRES   4 A  144  LYS ILE CYS ASP PRO GLY LEU THR ALA PHE GLU PRO GLU          
SEQRES   5 A  144  ALA LEU GLY ASN LEU VAL GLU GLY MET ASP PHE HIS ARG          
SEQRES   6 A  144  PHE TYR PHE GLU ASN ALA LEU SER LYS SER ASN LYS PRO          
SEQRES   7 A  144  ILE HIS THR ILE ILE LEU ASN PRO HIS VAL HIS LEU VAL          
SEQRES   8 A  144  GLY ASP ASP ALA ALA CYS ILE ALA TYR ILE ARG LEU THR          
SEQRES   9 A  144  GLN TYR MET ASP GLY SER GLY MET PRO LYS THR MET GLN          
SEQRES  10 A  144  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 A  144  TRP GLN ASN VAL HIS PHE HIS ARG SER GLY SER PRO THR          
SEQRES  12 A  144  VAL                                                          
SEQRES   1 B  144  SER MET SER ASN THR THR ILE GLU ASP GLU ASP VAL LYS          
SEQRES   2 B  144  ALA ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 B  144  ILE GLU ALA ILE ASN ASN GLY ASP PHE GLU ALA TYR THR          
SEQRES   4 B  144  LYS ILE CYS ASP PRO GLY LEU THR ALA PHE GLU PRO GLU          
SEQRES   5 B  144  ALA LEU GLY ASN LEU VAL GLU GLY MET ASP PHE HIS ARG          
SEQRES   6 B  144  PHE TYR PHE GLU ASN ALA LEU SER LYS SER ASN LYS PRO          
SEQRES   7 B  144  ILE HIS THR ILE ILE LEU ASN PRO HIS VAL HIS LEU VAL          
SEQRES   8 B  144  GLY ASP ASP ALA ALA CYS ILE ALA TYR ILE ARG LEU THR          
SEQRES   9 B  144  GLN TYR MET ASP GLY SER GLY MET PRO LYS THR MET GLN          
SEQRES  10 B  144  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 B  144  TRP GLN ASN VAL HIS PHE HIS ARG SER GLY SER PRO THR          
SEQRES  12 B  144  VAL                                                          
SEQRES   1 C  144  SER MET SER ASN THR THR ILE GLU ASP GLU ASP VAL LYS          
SEQRES   2 C  144  ALA ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 C  144  ILE GLU ALA ILE ASN ASN GLY ASP PHE GLU ALA TYR THR          
SEQRES   4 C  144  LYS ILE CYS ASP PRO GLY LEU THR ALA PHE GLU PRO GLU          
SEQRES   5 C  144  ALA LEU GLY ASN LEU VAL GLU GLY MET ASP PHE HIS ARG          
SEQRES   6 C  144  PHE TYR PHE GLU ASN ALA LEU SER LYS SER ASN LYS PRO          
SEQRES   7 C  144  ILE HIS THR ILE ILE LEU ASN PRO HIS VAL HIS LEU VAL          
SEQRES   8 C  144  GLY ASP ASP ALA ALA CYS ILE ALA TYR ILE ARG LEU THR          
SEQRES   9 C  144  GLN TYR MET ASP GLY SER GLY MET PRO LYS THR MET GLN          
SEQRES  10 C  144  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 C  144  TRP GLN ASN VAL HIS PHE HIS ARG SER GLY SER PRO THR          
SEQRES  12 C  144  VAL                                                          
SEQRES   1 D  144  SER MET SER ASN THR THR ILE GLU ASP GLU ASP VAL LYS          
SEQRES   2 D  144  ALA ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 D  144  ILE GLU ALA ILE ASN ASN GLY ASP PHE GLU ALA TYR THR          
SEQRES   4 D  144  LYS ILE CYS ASP PRO GLY LEU THR ALA PHE GLU PRO GLU          
SEQRES   5 D  144  ALA LEU GLY ASN LEU VAL GLU GLY MET ASP PHE HIS ARG          
SEQRES   6 D  144  PHE TYR PHE GLU ASN ALA LEU SER LYS SER ASN LYS PRO          
SEQRES   7 D  144  ILE HIS THR ILE ILE LEU ASN PRO HIS VAL HIS LEU VAL          
SEQRES   8 D  144  GLY ASP ASP ALA ALA CYS ILE ALA TYR ILE ARG LEU THR          
SEQRES   9 D  144  GLN TYR MET ASP GLY SER GLY MET PRO LYS THR MET GLN          
SEQRES  10 D  144  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 D  144  TRP GLN ASN VAL HIS PHE HIS ARG SER GLY SER PRO THR          
SEQRES  12 D  144  VAL                                                          
SEQRES   1 E  144  SER MET SER ASN THR THR ILE GLU ASP GLU ASP VAL LYS          
SEQRES   2 E  144  ALA ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 E  144  ILE GLU ALA ILE ASN ASN GLY ASP PHE GLU ALA TYR THR          
SEQRES   4 E  144  LYS ILE CYS ASP PRO GLY LEU THR ALA PHE GLU PRO GLU          
SEQRES   5 E  144  ALA LEU GLY ASN LEU VAL GLU GLY MET ASP PHE HIS ARG          
SEQRES   6 E  144  PHE TYR PHE GLU ASN ALA LEU SER LYS SER ASN LYS PRO          
SEQRES   7 E  144  ILE HIS THR ILE ILE LEU ASN PRO HIS VAL HIS LEU VAL          
SEQRES   8 E  144  GLY ASP ASP ALA ALA CYS ILE ALA TYR ILE ARG LEU THR          
SEQRES   9 E  144  GLN TYR MET ASP GLY SER GLY MET PRO LYS THR MET GLN          
SEQRES  10 E  144  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 E  144  TRP GLN ASN VAL HIS PHE HIS ARG SER GLY SER PRO THR          
SEQRES  12 E  144  VAL                                                          
SEQRES   1 F  144  SER MET SER ASN THR THR ILE GLU ASP GLU ASP VAL LYS          
SEQRES   2 F  144  ALA ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 F  144  ILE GLU ALA ILE ASN ASN GLY ASP PHE GLU ALA TYR THR          
SEQRES   4 F  144  LYS ILE CYS ASP PRO GLY LEU THR ALA PHE GLU PRO GLU          
SEQRES   5 F  144  ALA LEU GLY ASN LEU VAL GLU GLY MET ASP PHE HIS ARG          
SEQRES   6 F  144  PHE TYR PHE GLU ASN ALA LEU SER LYS SER ASN LYS PRO          
SEQRES   7 F  144  ILE HIS THR ILE ILE LEU ASN PRO HIS VAL HIS LEU VAL          
SEQRES   8 F  144  GLY ASP ASP ALA ALA CYS ILE ALA TYR ILE ARG LEU THR          
SEQRES   9 F  144  GLN TYR MET ASP GLY SER GLY MET PRO LYS THR MET GLN          
SEQRES  10 F  144  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 F  144  TRP GLN ASN VAL HIS PHE HIS ARG SER GLY SER PRO THR          
SEQRES  12 F  144  VAL                                                          
SEQRES   1 G  144  SER MET SER ASN THR THR ILE GLU ASP GLU ASP VAL LYS          
SEQRES   2 G  144  ALA ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 G  144  ILE GLU ALA ILE ASN ASN GLY ASP PHE GLU ALA TYR THR          
SEQRES   4 G  144  LYS ILE CYS ASP PRO GLY LEU THR ALA PHE GLU PRO GLU          
SEQRES   5 G  144  ALA LEU GLY ASN LEU VAL GLU GLY MET ASP PHE HIS ARG          
SEQRES   6 G  144  PHE TYR PHE GLU ASN ALA LEU SER LYS SER ASN LYS PRO          
SEQRES   7 G  144  ILE HIS THR ILE ILE LEU ASN PRO HIS VAL HIS LEU VAL          
SEQRES   8 G  144  GLY ASP ASP ALA ALA CYS ILE ALA TYR ILE ARG LEU THR          
SEQRES   9 G  144  GLN TYR MET ASP GLY SER GLY MET PRO LYS THR MET GLN          
SEQRES  10 G  144  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 G  144  TRP GLN ASN VAL HIS PHE HIS ARG SER GLY SER PRO THR          
SEQRES  12 G  144  VAL                                                          
SEQRES   1 H  144  SER MET SER ASN THR THR ILE GLU ASP GLU ASP VAL LYS          
SEQRES   2 H  144  ALA ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 H  144  ILE GLU ALA ILE ASN ASN GLY ASP PHE GLU ALA TYR THR          
SEQRES   4 H  144  LYS ILE CYS ASP PRO GLY LEU THR ALA PHE GLU PRO GLU          
SEQRES   5 H  144  ALA LEU GLY ASN LEU VAL GLU GLY MET ASP PHE HIS ARG          
SEQRES   6 H  144  PHE TYR PHE GLU ASN ALA LEU SER LYS SER ASN LYS PRO          
SEQRES   7 H  144  ILE HIS THR ILE ILE LEU ASN PRO HIS VAL HIS LEU VAL          
SEQRES   8 H  144  GLY ASP ASP ALA ALA CYS ILE ALA TYR ILE ARG LEU THR          
SEQRES   9 H  144  GLN TYR MET ASP GLY SER GLY MET PRO LYS THR MET GLN          
SEQRES  10 H  144  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 H  144  TRP GLN ASN VAL HIS PHE HIS ARG SER GLY SER PRO THR          
SEQRES  12 H  144  VAL                                                          
SEQRES   1 I  144  SER MET SER ASN THR THR ILE GLU ASP GLU ASP VAL LYS          
SEQRES   2 I  144  ALA ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 I  144  ILE GLU ALA ILE ASN ASN GLY ASP PHE GLU ALA TYR THR          
SEQRES   4 I  144  LYS ILE CYS ASP PRO GLY LEU THR ALA PHE GLU PRO GLU          
SEQRES   5 I  144  ALA LEU GLY ASN LEU VAL GLU GLY MET ASP PHE HIS ARG          
SEQRES   6 I  144  PHE TYR PHE GLU ASN ALA LEU SER LYS SER ASN LYS PRO          
SEQRES   7 I  144  ILE HIS THR ILE ILE LEU ASN PRO HIS VAL HIS LEU VAL          
SEQRES   8 I  144  GLY ASP ASP ALA ALA CYS ILE ALA TYR ILE ARG LEU THR          
SEQRES   9 I  144  GLN TYR MET ASP GLY SER GLY MET PRO LYS THR MET GLN          
SEQRES  10 I  144  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 I  144  TRP GLN ASN VAL HIS PHE HIS ARG SER GLY SER PRO THR          
SEQRES  12 I  144  VAL                                                          
SEQRES   1 J  144  SER MET SER ASN THR THR ILE GLU ASP GLU ASP VAL LYS          
SEQRES   2 J  144  ALA ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 J  144  ILE GLU ALA ILE ASN ASN GLY ASP PHE GLU ALA TYR THR          
SEQRES   4 J  144  LYS ILE CYS ASP PRO GLY LEU THR ALA PHE GLU PRO GLU          
SEQRES   5 J  144  ALA LEU GLY ASN LEU VAL GLU GLY MET ASP PHE HIS ARG          
SEQRES   6 J  144  PHE TYR PHE GLU ASN ALA LEU SER LYS SER ASN LYS PRO          
SEQRES   7 J  144  ILE HIS THR ILE ILE LEU ASN PRO HIS VAL HIS LEU VAL          
SEQRES   8 J  144  GLY ASP ASP ALA ALA CYS ILE ALA TYR ILE ARG LEU THR          
SEQRES   9 J  144  GLN TYR MET ASP GLY SER GLY MET PRO LYS THR MET GLN          
SEQRES  10 J  144  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 J  144  TRP GLN ASN VAL HIS PHE HIS ARG SER GLY SER PRO THR          
SEQRES  12 J  144  VAL                                                          
SEQRES   1 K  144  SER MET SER ASN THR THR ILE GLU ASP GLU ASP VAL LYS          
SEQRES   2 K  144  ALA ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 K  144  ILE GLU ALA ILE ASN ASN GLY ASP PHE GLU ALA TYR THR          
SEQRES   4 K  144  LYS ILE CYS ASP PRO GLY LEU THR ALA PHE GLU PRO GLU          
SEQRES   5 K  144  ALA LEU GLY ASN LEU VAL GLU GLY MET ASP PHE HIS ARG          
SEQRES   6 K  144  PHE TYR PHE GLU ASN ALA LEU SER LYS SER ASN LYS PRO          
SEQRES   7 K  144  ILE HIS THR ILE ILE LEU ASN PRO HIS VAL HIS LEU VAL          
SEQRES   8 K  144  GLY ASP ASP ALA ALA CYS ILE ALA TYR ILE ARG LEU THR          
SEQRES   9 K  144  GLN TYR MET ASP GLY SER GLY MET PRO LYS THR MET GLN          
SEQRES  10 K  144  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 K  144  TRP GLN ASN VAL HIS PHE HIS ARG SER GLY SER PRO THR          
SEQRES  12 K  144  VAL                                                          
SEQRES   1 L  144  SER MET SER ASN THR THR ILE GLU ASP GLU ASP VAL LYS          
SEQRES   2 L  144  ALA ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 L  144  ILE GLU ALA ILE ASN ASN GLY ASP PHE GLU ALA TYR THR          
SEQRES   4 L  144  LYS ILE CYS ASP PRO GLY LEU THR ALA PHE GLU PRO GLU          
SEQRES   5 L  144  ALA LEU GLY ASN LEU VAL GLU GLY MET ASP PHE HIS ARG          
SEQRES   6 L  144  PHE TYR PHE GLU ASN ALA LEU SER LYS SER ASN LYS PRO          
SEQRES   7 L  144  ILE HIS THR ILE ILE LEU ASN PRO HIS VAL HIS LEU VAL          
SEQRES   8 L  144  GLY ASP ASP ALA ALA CYS ILE ALA TYR ILE ARG LEU THR          
SEQRES   9 L  144  GLN TYR MET ASP GLY SER GLY MET PRO LYS THR MET GLN          
SEQRES  10 L  144  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 L  144  TRP GLN ASN VAL HIS PHE HIS ARG SER GLY SER PRO THR          
SEQRES  12 L  144  VAL                                                          
SEQRES   1 M  144  SER MET SER ASN THR THR ILE GLU ASP GLU ASP VAL LYS          
SEQRES   2 M  144  ALA ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 M  144  ILE GLU ALA ILE ASN ASN GLY ASP PHE GLU ALA TYR THR          
SEQRES   4 M  144  LYS ILE CYS ASP PRO GLY LEU THR ALA PHE GLU PRO GLU          
SEQRES   5 M  144  ALA LEU GLY ASN LEU VAL GLU GLY MET ASP PHE HIS ARG          
SEQRES   6 M  144  PHE TYR PHE GLU ASN ALA LEU SER LYS SER ASN LYS PRO          
SEQRES   7 M  144  ILE HIS THR ILE ILE LEU ASN PRO HIS VAL HIS LEU VAL          
SEQRES   8 M  144  GLY ASP ASP ALA ALA CYS ILE ALA TYR ILE ARG LEU THR          
SEQRES   9 M  144  GLN TYR MET ASP GLY SER GLY MET PRO LYS THR MET GLN          
SEQRES  10 M  144  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 M  144  TRP GLN ASN VAL HIS PHE HIS ARG SER GLY SER PRO THR          
SEQRES  12 M  144  VAL                                                          
SEQRES   1 N  144  SER MET SER ASN THR THR ILE GLU ASP GLU ASP VAL LYS          
SEQRES   2 N  144  ALA ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 N  144  ILE GLU ALA ILE ASN ASN GLY ASP PHE GLU ALA TYR THR          
SEQRES   4 N  144  LYS ILE CYS ASP PRO GLY LEU THR ALA PHE GLU PRO GLU          
SEQRES   5 N  144  ALA LEU GLY ASN LEU VAL GLU GLY MET ASP PHE HIS ARG          
SEQRES   6 N  144  PHE TYR PHE GLU ASN ALA LEU SER LYS SER ASN LYS PRO          
SEQRES   7 N  144  ILE HIS THR ILE ILE LEU ASN PRO HIS VAL HIS LEU VAL          
SEQRES   8 N  144  GLY ASP ASP ALA ALA CYS ILE ALA TYR ILE ARG LEU THR          
SEQRES   9 N  144  GLN TYR MET ASP GLY SER GLY MET PRO LYS THR MET GLN          
SEQRES  10 N  144  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 N  144  TRP GLN ASN VAL HIS PHE HIS ARG SER GLY SER PRO THR          
SEQRES  12 N  144  VAL                                                          
HET    ACT  A 632       4                                                       
HET    ACT  B 632       4                                                       
HET     CD  B1472       1                                                       
HET    ACT  C 632       4                                                       
HET    ACT  D 632       4                                                       
HET    ACT  E 632       4                                                       
HET    ACT  F 632       4                                                       
HET     CD  F1472       1                                                       
HET    ACT  G 632       4                                                       
HET    ACT  H 632       4                                                       
HET     CD  H1472       1                                                       
HET    ACT  I 632       4                                                       
HET    ACT  J 632       4                                                       
HET     CD  J1472       1                                                       
HET     CD  J1473       1                                                       
HET     CD  J1474       1                                                       
HET    ACT  K 632       4                                                       
HET    ACT  L 632       4                                                       
HET    ACT  M 632       4                                                       
HET    ACT  N 632       4                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM      CD CADMIUM ION                                                      
FORMUL  15  ACT    14(C2 H3 O2 1-)                                              
FORMUL  17   CD    6(CD 2+)                                                     
FORMUL  35  HOH   *93(H2 O)                                                     
HELIX    1   1 GLU A  339  GLY A  364  1                                  26    
HELIX    2   2 ASP A  365  ILE A  372  1                                   8    
HELIX    3   3 GLU A  381  LEU A  385  5                                   5    
HELIX    4   4 MET A  392  ALA A  402  1                                  11    
HELIX    5   5 ASP B  340  GLY B  364  1                                  25    
HELIX    6   6 ASP B  365  ILE B  372  1                                   8    
HELIX    7   7 GLU B  381  LEU B  385  5                                   5    
HELIX    8   8 MET B  392  ALA B  402  1                                  11    
HELIX    9   9 GLU C  341  GLY C  364  1                                  24    
HELIX   10  10 ASP C  365  ILE C  372  1                                   8    
HELIX   11  11 GLU C  381  LEU C  385  5                                   5    
HELIX   12  12 MET C  392  ASN C  401  1                                  10    
HELIX   13  13 ASP D  342  GLY D  364  1                                  23    
HELIX   14  14 ASP D  365  ILE D  372  1                                   8    
HELIX   15  15 GLU D  381  LEU D  385  5                                   5    
HELIX   16  16 MET D  392  ALA D  402  1                                  11    
HELIX   17  17 ILE E  338  GLY E  364  1                                  27    
HELIX   18  18 ASP E  365  ILE E  372  1                                   8    
HELIX   19  19 GLU E  381  LEU E  385  5                                   5    
HELIX   20  20 MET E  392  ALA E  402  1                                  11    
HELIX   21  21 GLU F  341  GLY F  364  1                                  24    
HELIX   22  22 ASP F  365  ILE F  372  1                                   8    
HELIX   23  23 GLU F  381  LEU F  385  5                                   5    
HELIX   24  24 MET F  392  ALA F  402  1                                  11    
HELIX   25  25 GLU G  341  GLY G  364  1                                  24    
HELIX   26  26 ASP G  365  ILE G  372  1                                   8    
HELIX   27  27 GLU G  381  LEU G  385  5                                   5    
HELIX   28  28 MET G  392  ALA G  402  1                                  11    
HELIX   29  29 GLU H  339  GLY H  364  1                                  26    
HELIX   30  30 ASP H  365  ILE H  372  1                                   8    
HELIX   31  31 GLU H  381  LEU H  385  5                                   5    
HELIX   32  32 MET H  392  ALA H  402  1                                  11    
HELIX   33  33 GLU I  339  GLY I  364  1                                  26    
HELIX   34  34 ASP I  365  ILE I  372  1                                   8    
HELIX   35  35 GLU I  381  LEU I  385  5                                   5    
HELIX   36  36 MET I  392  ALA I  402  1                                  11    
HELIX   37  37 ASP J  342  GLY J  364  1                                  23    
HELIX   38  38 ASP J  365  ILE J  372  1                                   8    
HELIX   39  39 GLU J  381  LEU J  385  5                                   5    
HELIX   40  40 MET J  392  ALA J  402  1                                  11    
HELIX   41  41 ASP K  342  ASN K  363  1                                  22    
HELIX   42  42 ASP K  365  ILE K  372  1                                   8    
HELIX   43  43 GLU K  381  LEU K  385  5                                   5    
HELIX   44  44 MET K  392  ASN K  401  1                                  10    
HELIX   45  45 ASP L  340  GLY L  364  1                                  25    
HELIX   46  46 ASP L  365  ILE L  372  1                                   8    
HELIX   47  47 GLU L  381  LEU L  385  5                                   5    
HELIX   48  48 MET L  392  ALA L  402  1                                  11    
HELIX   49  49 VAL M  343  GLY M  364  1                                  22    
HELIX   50  50 ASP M  365  ILE M  372  1                                   8    
HELIX   51  51 GLU M  381  LEU M  385  5                                   5    
HELIX   52  52 MET M  392  ALA M  402  1                                  11    
HELIX   53  53 THR N  336  GLY N  364  1                                  29    
HELIX   54  54 ASP N  365  ILE N  372  1                                   8    
HELIX   55  55 GLU N  381  LEU N  385  5                                   5    
HELIX   56  56 MET N  392  ALA N  402  1                                  11    
SHEET    1  AA 6 VAL A 389  GLU A 390  0                                        
SHEET    2  AA 6 CYS A 373  PHE A 380 -1  O  ALA A 379   N  VAL A 389           
SHEET    3  AA 6 LYS A 461  SER A 470  1  O  ASN A 464   N  ASP A 374           
SHEET    4  AA 6 PRO A 444  ARG A 458 -1  O  GLU A 450   N  SER A 470           
SHEET    5  AA 6 ALA A 426  MET A 438 -1  O  ALA A 427   N  TRP A 455           
SHEET    6  AA 6 ILE A 410  LEU A 421 -1  O  HIS A 411   N  GLN A 436           
SHEET    1  BA 6 VAL B 389  GLU B 390  0                                        
SHEET    2  BA 6 CYS B 373  PHE B 380 -1  O  ALA B 379   N  VAL B 389           
SHEET    3  BA 6 LYS B 461  SER B 470  1  O  ASN B 464   N  ASP B 374           
SHEET    4  BA 6 PRO B 444  ARG B 458 -1  O  GLU B 450   N  SER B 470           
SHEET    5  BA 6 ALA B 426  MET B 438 -1  O  ALA B 427   N  TRP B 455           
SHEET    6  BA 6 HIS B 411  LEU B 421 -1  O  HIS B 411   N  GLN B 436           
SHEET    1  CA 6 VAL C 389  GLU C 390  0                                        
SHEET    2  CA 6 CYS C 373  PHE C 380 -1  O  ALA C 379   N  VAL C 389           
SHEET    3  CA 6 LYS C 461  SER C 470  1  O  ASN C 464   N  ASP C 374           
SHEET    4  CA 6 PRO C 444  ARG C 458 -1  O  GLU C 450   N  SER C 470           
SHEET    5  CA 6 ALA C 426  MET C 438 -1  O  ALA C 427   N  TRP C 455           
SHEET    6  CA 6 HIS C 411  LEU C 421 -1  O  HIS C 411   N  GLN C 436           
SHEET    1  DA 6 VAL D 389  GLU D 390  0                                        
SHEET    2  DA 6 CYS D 373  PHE D 380 -1  O  ALA D 379   N  VAL D 389           
SHEET    3  DA 6 LYS D 461  SER D 470  1  O  ASN D 464   N  ASP D 374           
SHEET    4  DA 6 PRO D 444  ARG D 458 -1  O  GLU D 450   N  SER D 470           
SHEET    5  DA 6 ALA D 426  MET D 438 -1  O  ALA D 427   N  TRP D 455           
SHEET    6  DA 6 ILE D 410  LEU D 421 -1  O  HIS D 411   N  GLN D 436           
SHEET    1  EA 6 VAL E 389  GLU E 390  0                                        
SHEET    2  EA 6 CYS E 373  PHE E 380 -1  O  ALA E 379   N  VAL E 389           
SHEET    3  EA 6 LYS E 461  SER E 470  1  O  ASN E 464   N  ASP E 374           
SHEET    4  EA 6 PRO E 444  ARG E 458 -1  O  GLU E 450   N  SER E 470           
SHEET    5  EA 6 ALA E 426  MET E 438 -1  O  ALA E 427   N  TRP E 455           
SHEET    6  EA 6 HIS E 411  LEU E 421 -1  O  HIS E 411   N  GLN E 436           
SHEET    1  FA 6 VAL F 389  GLU F 390  0                                        
SHEET    2  FA 6 CYS F 373  PHE F 380 -1  O  ALA F 379   N  VAL F 389           
SHEET    3  FA 6 LYS F 461  SER F 470  1  O  ASN F 464   N  ASP F 374           
SHEET    4  FA 6 PRO F 444  ARG F 458 -1  O  GLU F 450   N  SER F 470           
SHEET    5  FA 6 ALA F 426  MET F 438 -1  O  ALA F 427   N  TRP F 455           
SHEET    6  FA 6 ILE F 410  LEU F 421 -1  O  HIS F 411   N  GLN F 436           
SHEET    1  GA 6 VAL G 389  GLU G 390  0                                        
SHEET    2  GA 6 CYS G 373  PHE G 380 -1  O  ALA G 379   N  VAL G 389           
SHEET    3  GA 6 LYS G 461  SER G 470  1  O  ASN G 464   N  ASP G 374           
SHEET    4  GA 6 PRO G 444  ARG G 458 -1  O  GLU G 450   N  SER G 470           
SHEET    5  GA 6 ALA G 426  MET G 438 -1  O  ALA G 427   N  TRP G 455           
SHEET    6  GA 6 ILE G 410  LEU G 421 -1  O  HIS G 411   N  GLN G 436           
SHEET    1  HA 6 VAL H 389  GLU H 390  0                                        
SHEET    2  HA 6 CYS H 373  PHE H 380 -1  O  ALA H 379   N  VAL H 389           
SHEET    3  HA 6 LYS H 461  SER H 470  1  O  ASN H 464   N  ASP H 374           
SHEET    4  HA 6 PRO H 444  ARG H 458 -1  O  GLU H 450   N  SER H 470           
SHEET    5  HA 6 ALA H 426  MET H 438 -1  O  ALA H 427   N  TRP H 455           
SHEET    6  HA 6 HIS H 411  LEU H 421 -1  O  HIS H 411   N  GLN H 436           
SHEET    1  IA 6 VAL I 389  GLU I 390  0                                        
SHEET    2  IA 6 CYS I 373  PHE I 380 -1  O  ALA I 379   N  VAL I 389           
SHEET    3  IA 6 LYS I 461  SER I 470  1  O  ASN I 464   N  ASP I 374           
SHEET    4  IA 6 PRO I 444  ARG I 458 -1  O  GLU I 450   N  SER I 470           
SHEET    5  IA 6 ALA I 426  MET I 438 -1  O  ALA I 427   N  TRP I 455           
SHEET    6  IA 6 ILE I 410  LEU I 421 -1  O  HIS I 411   N  GLN I 436           
SHEET    1  JA 6 VAL J 389  GLU J 390  0                                        
SHEET    2  JA 6 CYS J 373  PHE J 380 -1  O  ALA J 379   N  VAL J 389           
SHEET    3  JA 6 LYS J 461  SER J 470  1  O  ASN J 464   N  ASP J 374           
SHEET    4  JA 6 PRO J 444  ARG J 458 -1  O  GLU J 450   N  SER J 470           
SHEET    5  JA 6 ALA J 426  MET J 438 -1  O  ALA J 427   N  TRP J 455           
SHEET    6  JA 6 HIS J 411  LEU J 421 -1  O  HIS J 411   N  GLN J 436           
SHEET    1  KA 6 VAL K 389  GLU K 390  0                                        
SHEET    2  KA 6 CYS K 373  PHE K 380 -1  O  ALA K 379   N  VAL K 389           
SHEET    3  KA 6 LYS K 461  SER K 470  1  O  ASN K 464   N  ASP K 374           
SHEET    4  KA 6 PRO K 444  ARG K 458 -1  O  GLU K 450   N  SER K 470           
SHEET    5  KA 6 ALA K 426  MET K 438 -1  O  ALA K 427   N  TRP K 455           
SHEET    6  KA 6 HIS K 411  LEU K 421 -1  O  HIS K 411   N  GLN K 436           
SHEET    1  LA 6 VAL L 389  GLU L 390  0                                        
SHEET    2  LA 6 CYS L 373  PHE L 380 -1  O  ALA L 379   N  VAL L 389           
SHEET    3  LA 6 LYS L 461  SER L 470  1  O  ASN L 464   N  ASP L 374           
SHEET    4  LA 6 PRO L 444  ARG L 458 -1  O  GLU L 450   N  SER L 470           
SHEET    5  LA 6 ALA L 426  MET L 438 -1  O  ALA L 427   N  TRP L 455           
SHEET    6  LA 6 ILE L 410  LEU L 421 -1  O  HIS L 411   N  GLN L 436           
SHEET    1  MA 6 VAL M 389  GLU M 390  0                                        
SHEET    2  MA 6 CYS M 373  PHE M 380 -1  O  ALA M 379   N  VAL M 389           
SHEET    3  MA 6 LYS M 461  SER M 470  1  O  ASN M 464   N  ASP M 374           
SHEET    4  MA 6 PRO M 444  ARG M 458 -1  O  GLU M 450   N  SER M 470           
SHEET    5  MA 6 ALA M 426  MET M 438 -1  O  ALA M 427   N  TRP M 455           
SHEET    6  MA 6 HIS M 411  LEU M 421 -1  O  HIS M 411   N  GLN M 436           
SHEET    1  NA 6 VAL N 389  GLU N 390  0                                        
SHEET    2  NA 6 CYS N 373  PHE N 380 -1  O  ALA N 379   N  VAL N 389           
SHEET    3  NA 6 LYS N 461  SER N 470  1  O  ASN N 464   N  ASP N 374           
SHEET    4  NA 6 PRO N 444  ARG N 458 -1  O  GLU N 450   N  SER N 470           
SHEET    5  NA 6 ALA N 426  MET N 438 -1  O  ALA N 427   N  TRP N 455           
SHEET    6  NA 6 ILE N 410  LEU N 421 -1  O  HIS N 411   N  GLN N 436           
LINK        CD    CD B1472                 OD1 ASP B 425     1555   1555  2.82  
LINK        CD    CD B1472                 OD2 ASP B 425     1555   1555  2.47  
LINK        CD    CD B1472                 OD2 ASP L 425     1555   2455  2.40  
LINK        CD    CD B1472                 O   HOH B2006     1555   1555  1.94  
LINK        CD    CD B1472                 O   HOH B2009     1555   1555  2.08  
LINK        CD    CD F1472                 OD1 ASP F 425     1555   1555  2.80  
LINK        CD    CD F1472                 OD2 ASP F 425     1555   1555  2.13  
LINK        CD    CD F1472                 OD2 ASP G 425     1555   1565  2.07  
LINK        CD    CD F1472                 O   HOH G2005     1555   1565  2.86  
LINK        CD    CD H1472                 OD1 ASP N 425     1555   4556  2.68  
LINK        CD    CD H1472                 OD2 ASP H 424     1555   1555  2.51  
LINK        CD    CD J1472                 OD2 ASP J 425     1555   1555  2.32  
LINK        CD    CD J1472                 OD2 ASP M 425     1555   1565  1.84  
LINK        CD    CD J1472                CD    CD J1474     1555   1555  2.85  
LINK        CD    CD J1472                 OD1 ASP J 425     1555   1555  2.88  
LINK        CD    CD J1473                 OD1 ASP J 424     1555   1555  2.52  
LINK        CD    CD J1473                 OD2 ASP J 424     1555   1555  2.37  
LINK        CD    CD J1473                 OD2 ASP G 424     1555   1565  2.01  
LINK        CD    CD J1473                 OD1 ASP G 424     1555   1565  2.84  
LINK        CD    CD J1474                 OD2 ASP J 425     1555   1555  2.61  
SITE     1 AC1  6 ILE A 361  TYR A 369  ARG A 433  ARG A 453                    
SITE     2 AC1  6 PHE A 467  ARG A 469                                          
SITE     1 AC2  6 ILE B 361  TYR B 369  ARG B 433  ARG B 453                    
SITE     2 AC2  6 PHE B 467  ARG B 469                                          
SITE     1 AC3  6 ILE C 361  TYR C 369  ARG C 433  ARG C 453                    
SITE     2 AC3  6 PHE C 467  ARG C 469                                          
SITE     1 AC4  6 ILE D 361  TYR D 369  ARG D 433  ARG D 453                    
SITE     2 AC4  6 PHE D 467  ARG D 469                                          
SITE     1 AC5  5 ILE E 361  TYR E 369  ARG E 453  PHE E 467                    
SITE     2 AC5  5 ARG E 469                                                     
SITE     1 AC6  5 ILE F 361  TYR F 369  ARG F 453  PHE F 467                    
SITE     2 AC6  5 ARG F 469                                                     
SITE     1 AC7  6 ILE G 361  TYR G 369  ARG G 433  ARG G 453                    
SITE     2 AC7  6 PHE G 467  ARG G 469                                          
SITE     1 AC8  5 ILE H 361  TYR H 369  ARG H 453  PHE H 467                    
SITE     2 AC8  5 ARG H 469                                                     
SITE     1 AC9  6 ILE I 361  TYR I 369  ARG I 433  ARG I 453                    
SITE     2 AC9  6 PHE I 467  ARG I 469                                          
SITE     1 BC1  6 ILE J 361  TYR J 369  ARG J 433  ARG J 453                    
SITE     2 BC1  6 PHE J 467  ARG J 469                                          
SITE     1 BC2  6 ILE K 361  TYR K 369  ARG K 453  PHE K 467                    
SITE     2 BC2  6 ARG K 469  HOH K2001                                          
SITE     1 BC3  6 ILE L 361  TYR L 369  ARG L 433  ARG L 453                    
SITE     2 BC3  6 PHE L 467  ARG L 469                                          
SITE     1 BC4  6 ILE M 361  TYR M 369  ARG M 433  ARG M 453                    
SITE     2 BC4  6 PHE M 467  ARG M 469                                          
SITE     1 BC5  6 ILE N 361  TYR N 369  ARG N 433  ARG N 453                    
SITE     2 BC5  6 PHE N 467  ARG N 469                                          
SITE     1 BC6  4 ASP B 425  HOH B2006  HOH B2009  ASP L 425                    
SITE     1 BC7  3 ASP H 424  ASP N 425  ARG N 457                               
SITE     1 BC8  3 ASP F 425  ASP G 425  HOH G2005                               
SITE     1 BC9  3 ASP J 425   CD J1474  ASP M 425                               
SITE     1 CC1  2 ASP G 424  ASP J 424                                          
SITE     1 CC2  4 ASP J 424  ASP J 425   CD J1472  ASP M 425                    
CRYST1  149.546  117.803  160.761  90.00 111.92  90.00 C 1 2 1      56          
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      0.006687  0.000000  0.002691        0.00000                         
SCALE2      0.000000  0.008489  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006705        0.00000                         
MTRIX1   1  0.791600  0.586600 -0.171100      -19.84000    1                    
MTRIX2   1 -0.583400  0.642100 -0.497300       15.22000    1                    
MTRIX3   1 -0.181900  0.493500  0.850500      -16.87000    1                    
MTRIX1   2  0.184400  0.030810  0.982400      -61.56000    1                    
MTRIX2   2 -0.006621 -0.999400  0.032580       69.51000    1                    
MTRIX3   2  0.982800 -0.012510 -0.184100       73.36000    1                    
MTRIX1   3  0.299100  0.745300 -0.595900      -23.92000    1                    
MTRIX2   3 -0.748500 -0.204100 -0.631000       45.16000    1                    
MTRIX3   3 -0.591900  0.634700  0.496800      -20.28000    1                    
MTRIX1   4 -0.939500  0.338600  0.052180      -71.19000    1                    
MTRIX2   4  0.339500  0.900100  0.273000        3.25000    1                    
MTRIX3   4  0.045480  0.274200 -0.960600       65.84000    1                    
MTRIX1   5  0.756600 -0.627100 -0.185300       23.16000    1                    
MTRIX2   5  0.622500  0.603900  0.497800       13.88000    1                    
MTRIX3   5 -0.200300 -0.492000  0.847300       17.45000    1                    
MTRIX1   6 -0.114000  0.352400 -0.928900       -9.13100    1                    
MTRIX2   6 -0.323500 -0.897200 -0.300700       69.00000    1                    
MTRIX3   6 -0.939300  0.266200  0.216200       -7.69100    1                    
MTRIX1   7  0.234500 -0.756300 -0.610800       28.86000    1                    
MTRIX2   7  0.752600 -0.256500  0.606500       44.59000    1                    
MTRIX3   7 -0.615300 -0.601900  0.509000       21.42000    1                    
MTRIX1   8 -0.131300 -0.318400 -0.938800       14.47000    1                    
MTRIX2   8  0.331100 -0.906700  0.261200       67.65000    1                    
MTRIX3   8 -0.934400 -0.276600  0.224500       11.12000    1                    
MTRIX1   9 -0.934200 -0.352600  0.055050      -45.48000    1                    
MTRIX2   9 -0.353000  0.890700 -0.286300        4.55800    1                    
MTRIX3   9  0.051900 -0.286900 -0.956600       85.76000    1                    
MTRIX1  10 -0.488700 -0.775400  0.399800      -29.36000    1                    
MTRIX2  10 -0.771700  0.170500 -0.612700       31.10000    1                    
MTRIX3  10  0.407000 -0.608000 -0.681700       96.86000    1                    
MTRIX1  11 -0.014710 -0.589200  0.807800      -38.65000    1                    
MTRIX2  11 -0.602100 -0.639800 -0.477700       59.02000    1                    
MTRIX3  11  0.798300 -0.493400 -0.345300       91.13000    1                    
MTRIX1  12 -0.053650  0.615600  0.786200      -81.86000    1                    
MTRIX2  12  0.601200 -0.608700  0.517700       55.11000    1                    
MTRIX3  12  0.797300  0.500500 -0.337500       56.39000    1                    
MTRIX1  13 -0.568500  0.740000  0.359500      -85.27000    1                    
MTRIX2  13  0.728400  0.249700  0.638000       24.46000    1                    
MTRIX3  13  0.382300  0.624500 -0.681000       52.93000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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