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Database: PDB
Entry: 1TFW
LinkDB: 1TFW
Original site: 1TFW 
HEADER    TRANSFERASE/RNA                         27-MAY-04   1TFW              
TITLE     HOW CCA IS ADDED TO THE 3' END OF IMMATURE TRNA WITHOUT THE USE OF AN 
TITLE    2 OLIGONUCLEOTIDE TEMPLATE                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-R(*GP*CP*GP*GP*AP*UP*CP*CP*GP*CP*AP*C)-3';              
COMPND   3 CHAIN: E;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: 5'-R(*GP*CP*GP*GP*AP*UP*CP*CP*GP*CP*AP*CP*C)-3';           
COMPND   7 CHAIN: H, I, G;                                                      
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: 5'-R(*GP*CP*GP*GP*AP*CP*CP*CP*GP*CP*AP*C)-3';              
COMPND  11 CHAIN: F;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: 5'-R(*CP*GP*CP*GP*GP*AP*UP*CP*CP*GP*CP*AP*C)-3';           
COMPND  15 CHAIN: J;                                                            
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 5;                                                           
COMPND  18 MOLECULE: TRNA NUCLEOTIDYLTRANSFERASE;                               
COMPND  19 CHAIN: A, B, C, D;                                                   
COMPND  20 SYNONYM: TRNA ADENYLYLTRANSFERASE, TRNA CCA-PYROPHOSPHORYLASE, CCA-  
COMPND  21 ADDING ENZYME;                                                       
COMPND  22 EC: 2.7.7.25;                                                        
COMPND  23 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 MOL_ID: 2;                                                           
SOURCE   4 SYNTHETIC: YES;                                                      
SOURCE   5 MOL_ID: 3;                                                           
SOURCE   6 SYNTHETIC: YES;                                                      
SOURCE   7 MOL_ID: 4;                                                           
SOURCE   8 SYNTHETIC: YES;                                                      
SOURCE   9 MOL_ID: 5;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;                         
SOURCE  11 ORGANISM_TAXID: 2234;                                                
SOURCE  12 GENE: CCA, AF2156;                                                   
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    CCA-ADDING COMPLEX, TRANSFERASE-RNA COMPLEX                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.XIONG,T.A.STEITZ                                                    
REVDAT   4   23-AUG-23 1TFW    1       REMARK LINK                              
REVDAT   3   13-JUL-11 1TFW    1       VERSN                                    
REVDAT   2   24-FEB-09 1TFW    1       VERSN                                    
REVDAT   1   10-AUG-04 1TFW    0                                                
JRNL        AUTH   Y.XIONG,T.A.STEITZ                                           
JRNL        TITL   MECHANISM OF TRANSFER RNA MATURATION BY CCA-ADDING ENZYME    
JRNL        TITL 2 WITHOUT USING AN OLIGONUCLEOTIDE TEMPLATE.                   
JRNL        REF    NATURE                        V. 430   640 2004              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   15295590                                                     
JRNL        DOI    10.1038/NATURE02711                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 122568                         
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) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6447                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.35                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 21803                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1125                         
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14520                                   
REMARK   3   NUCLEIC ACID ATOMS       : 1598                                    
REMARK   3   HETEROGEN ATOMS          : 64                                      
REMARK   3   SOLVENT ATOMS            : 1059                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.39000                                              
REMARK   3    B22 (A**2) : 0.21000                                              
REMARK   3    B33 (A**2) : -0.75000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.30000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.245         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.203         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.164         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.938        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 16697 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A): 14375 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 22820 ; 1.165 ; 2.096       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 33528 ; 0.956 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1744 ; 5.465 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   776 ;32.431 ;22.784       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2780 ;16.543 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   160 ;16.813 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2454 ; 0.066 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 17182 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  3372 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3237 ; 0.187 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 14494 ; 0.184 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  7693 ; 0.184 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  9024 ; 0.077 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   833 ; 0.147 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.032 ; 0.200       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.070 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     9 ; 0.120 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    37 ; 0.212 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.097 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 11403 ; 1.272 ; 2.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3540 ; 0.292 ; 2.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14056 ; 1.450 ; 4.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  9912 ; 2.450 ; 5.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  8764 ; 3.329 ; 8.000       
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 : 4                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      1       B     135      5                      
REMARK   3           1     D      1       D     135      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    795 ;  0.25 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   1378 ;  0.77 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):    795 ;  0.25 ;  2.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):   1378 ;  0.71 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A      90      2                      
REMARK   3           1     C      1       C      90      2                      
REMARK   3           2     A    101       A     135      5                      
REMARK   3           2     C    101       C     135      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    A    (A):    531 ;  0.03 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  2    A    (A):   1137 ;  0.35 ;  0.50           
REMARK   3   LOOSE POSITIONAL   2    A    (A):    336 ;  0.60 ;  5.00           
REMARK   3   TIGHT THERMAL      2    A (A**2):    531 ;  0.09 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    A (A**2):   1137 ;  0.48 ;  2.00           
REMARK   3   LOOSE THERMAL      2    A (A**2):    336 ;  0.91 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    136       A     437      5                      
REMARK   3           1     B    136       B     437      5                      
REMARK   3           1     C    136       C     437      5                      
REMARK   3           1     D    136       D     437      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    A    (A):   1781 ;  0.29 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    B    (A):   1781 ;  0.19 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    C    (A):   1781 ;  0.36 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    D    (A):   1781 ;  0.39 ;  0.50           
REMARK   3   LOOSE POSITIONAL   3    A    (A):   3110 ;  0.60 ;  5.00           
REMARK   3   LOOSE POSITIONAL   3    B    (A):   3110 ;  0.59 ;  5.00           
REMARK   3   LOOSE POSITIONAL   3    C    (A):   3110 ;  0.71 ;  5.00           
REMARK   3   LOOSE POSITIONAL   3    D    (A):   3110 ;  0.76 ;  5.00           
REMARK   3   MEDIUM THERMAL     3    A (A**2):   1781 ;  0.56 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    B (A**2):   1781 ;  0.58 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    C (A**2):   1781 ;  0.69 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    D (A**2):   1781 ;  0.62 ;  2.00           
REMARK   3   LOOSE THERMAL      3    A (A**2):   3110 ;  1.55 ; 10.00           
REMARK   3   LOOSE THERMAL      3    B (A**2):   3110 ;  1.60 ; 10.00           
REMARK   3   LOOSE THERMAL      3    C (A**2):   3110 ;  1.73 ; 10.00           
REMARK   3   LOOSE THERMAL      3    D (A**2):   3110 ;  1.84 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : E F                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     E      1       E      12      5                      
REMARK   3           1     F      1       F      12      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   4    E    (A):    322 ;  0.28 ;  5.00           
REMARK   3   LOOSE THERMAL      4    E (A**2):    322 ;  1.83 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 15                                         
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    17        A   124                          
REMARK   3    ORIGIN FOR THE GROUP (A):  77.7445  32.6165  35.4538              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1479 T22:  -0.0729                                     
REMARK   3      T33:   0.0121 T12:  -0.0457                                     
REMARK   3      T13:   0.0799 T23:   0.0805                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.5969 L22:   3.5513                                     
REMARK   3      L33:   4.3872 L12:  -3.7920                                     
REMARK   3      L13:  -1.0773 L23:  -0.5811                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1841 S12:  -0.6854 S13:   0.9710                       
REMARK   3      S21:   0.0023 S22:  -0.1097 S23:  -0.5199                       
REMARK   3      S31:  -0.1588 S32:   0.3430 S33:  -0.0744                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   125        A   258                          
REMARK   3    RESIDUE RANGE :   A     1        A    16                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.0302  33.4959  45.9387              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3102 T22:  -0.1216                                     
REMARK   3      T33:  -0.2355 T12:  -0.0331                                     
REMARK   3      T13:  -0.0207 T23:   0.0211                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9808 L22:   2.3821                                     
REMARK   3      L33:   2.9676 L12:  -0.1528                                     
REMARK   3      L13:  -0.5699 L23:   1.0346                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1060 S12:   0.2581 S13:   0.1501                       
REMARK   3      S21:  -0.1784 S22:  -0.2291 S23:   0.0134                       
REMARK   3      S31:  -0.0077 S32:  -0.4362 S33:   0.1231                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   259        A   437                          
REMARK   3    ORIGIN FOR THE GROUP (A):  63.0057  53.3518  77.4628              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2184 T22:  -0.2299                                     
REMARK   3      T33:  -0.0725 T12:  -0.0557                                     
REMARK   3      T13:  -0.0627 T23:   0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5268 L22:   0.5603                                     
REMARK   3      L33:   3.1554 L12:  -0.1312                                     
REMARK   3      L13:  -0.9623 L23:   0.2552                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0632 S12:  -0.0697 S13:   0.1569                       
REMARK   3      S21:   0.0116 S22:   0.0746 S23:  -0.2299                       
REMARK   3      S31:  -0.3391 S32:   0.1507 S33:  -0.1378                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    17        B   124                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.9274  39.5329 131.3273              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4717 T22:   0.4921                                     
REMARK   3      T33:   0.1831 T12:   0.3865                                     
REMARK   3      T13:   0.3438 T23:   0.3464                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1872 L22:   3.2277                                     
REMARK   3      L33:  10.3753 L12:   0.6353                                     
REMARK   3      L13:   2.6205 L23:   0.3812                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1788 S12:  -0.8034 S13:   0.0812                       
REMARK   3      S21:   0.9991 S22:   0.4790 S23:   0.8453                       
REMARK   3      S31:  -0.2771 S32:  -1.2438 S33:  -0.3002                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   125        B   258                          
REMARK   3    RESIDUE RANGE :   B     1        B    16                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.5938  37.3197 123.6952              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2461 T22:   0.1281                                     
REMARK   3      T33:  -0.2543 T12:   0.1793                                     
REMARK   3      T13:  -0.0728 T23:   0.1112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6131 L22:   3.6780                                     
REMARK   3      L33:   4.9382 L12:  -0.3699                                     
REMARK   3      L13:   0.3246 L23:  -1.9503                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1856 S12:  -0.5374 S13:  -0.0004                       
REMARK   3      S21:   0.9544 S22:   0.2163 S23:  -0.0800                       
REMARK   3      S31:  -0.4550 S32:  -0.0516 S33:  -0.0307                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   259        B   437                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.3399  54.3871  90.8262              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1713 T22:  -0.1682                                     
REMARK   3      T33:  -0.1951 T12:   0.0798                                     
REMARK   3      T13:  -0.0248 T23:   0.0700                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0524 L22:   0.9286                                     
REMARK   3      L33:   3.0665 L12:  -0.3845                                     
REMARK   3      L13:  -0.9475 L23:   0.2702                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0674 S12:  -0.1660 S13:   0.0621                       
REMARK   3      S21:   0.2689 S22:   0.1405 S23:  -0.0055                       
REMARK   3      S31:  -0.3854 S32:  -0.2250 S33:  -0.0731                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    17        C   124                          
REMARK   3    ORIGIN FOR THE GROUP (A):  67.4005  24.1667  97.8409              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0807 T22:   0.1328                                     
REMARK   3      T33:   0.0288 T12:   0.0714                                     
REMARK   3      T13:  -0.0009 T23:   0.0928                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5768 L22:  10.4886                                     
REMARK   3      L33:   3.4552 L12:  -3.8411                                     
REMARK   3      L13:  -1.9117 L23:   3.2568                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2565 S12:  -0.3117 S13:   0.1770                       
REMARK   3      S21:  -0.1577 S22:   0.4167 S23:  -0.8871                       
REMARK   3      S31:   0.0296 S32:   0.4126 S33:  -0.1602                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   125        C   258                          
REMARK   3    RESIDUE RANGE :   C     1        C    16                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.0406   4.6025  81.1417              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2175 T22:  -0.2421                                     
REMARK   3      T33:   0.0456 T12:  -0.0273                                     
REMARK   3      T13:   0.0914 T23:   0.1184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4851 L22:   3.1103                                     
REMARK   3      L33:   2.7692 L12:  -0.8419                                     
REMARK   3      L13:  -1.0134 L23:   0.5775                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2476 S12:  -0.1953 S13:  -0.6319                       
REMARK   3      S21:   0.3945 S22:   0.0846 S23:   0.4464                       
REMARK   3      S31:   0.3184 S32:  -0.2224 S33:   0.1630                       
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 :   C   259        C   437                          
REMARK   3    ORIGIN FOR THE GROUP (A):  98.3427  18.5962  60.8408              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2830 T22:  -0.3360                                     
REMARK   3      T33:  -0.1018 T12:  -0.0021                                     
REMARK   3      T13:   0.0068 T23:   0.0623                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3355 L22:   1.1129                                     
REMARK   3      L33:   1.4478 L12:  -0.2265                                     
REMARK   3      L13:  -0.0755 L23:   0.3030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0827 S12:   0.0169 S13:   0.1391                       
REMARK   3      S21:   0.0449 S22:  -0.1075 S23:  -0.2223                       
REMARK   3      S31:   0.0448 S32:   0.2075 S33:   0.0248                       
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 :   D    17        D   124                          
REMARK   3    ORIGIN FOR THE GROUP (A):  98.8265  -2.1139  -2.7093              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6203 T22:   0.5651                                     
REMARK   3      T33:   0.3047 T12:   0.3039                                     
REMARK   3      T13:  -0.0027 T23:  -0.0548                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3121 L22:   7.2228                                     
REMARK   3      L33:  10.6714 L12:   0.5024                                     
REMARK   3      L13:  -1.6687 L23:   0.6628                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0271 S12:   0.9176 S13:  -0.5259                       
REMARK   3      S21:  -0.6146 S22:   0.1033 S23:  -0.3464                       
REMARK   3      S31:   1.2371 S32:  -0.0684 S33:  -0.1304                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   125        D   258                          
REMARK   3    RESIDUE RANGE :   D     1        D    16                          
REMARK   3    ORIGIN FOR THE GROUP (A):  96.0592  19.1483  10.0893              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1251 T22:   0.3379                                     
REMARK   3      T33:  -0.1204 T12:   0.3278                                     
REMARK   3      T13:   0.1722 T23:   0.3226                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3524 L22:   2.8110                                     
REMARK   3      L33:   6.1937 L12:  -0.7123                                     
REMARK   3      L13:   0.9539 L23:  -1.0271                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3073 S12:   0.8674 S13:   0.2747                       
REMARK   3      S21:  -0.6757 S22:  -0.3329 S23:  -0.2555                       
REMARK   3      S31:   0.6611 S32:   0.6343 S33:   0.0255                       
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 :   D   259        D   437                          
REMARK   3    ORIGIN FOR THE GROUP (A): 102.1580   1.0177  42.7292              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0514 T22:  -0.1706                                     
REMARK   3      T33:  -0.1252 T12:   0.2261                                     
REMARK   3      T13:   0.0307 T23:   0.0714                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1760 L22:   2.1143                                     
REMARK   3      L33:   3.4860 L12:   0.0313                                     
REMARK   3      L13:  -0.6754 L23:  -1.2930                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1002 S12:   0.3179 S13:  -0.0214                       
REMARK   3      S21:  -0.7398 S22:  -0.3123 S23:  -0.1741                       
REMARK   3      S31:   0.7884 S32:   0.4394 S33:   0.2121                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E    12                          
REMARK   3    RESIDUE RANGE :   H    63        H    75                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.1157  34.1053  97.9671              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1624 T22:   0.1508                                     
REMARK   3      T33:   0.0430 T12:  -0.0385                                     
REMARK   3      T13:  -0.0042 T23:   0.1358                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2054 L22:   4.3356                                     
REMARK   3      L33:   7.0187 L12:   0.2252                                     
REMARK   3      L13:   3.2440 L23:  -3.3449                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1149 S12:   0.2741 S13:  -0.6683                       
REMARK   3      S21:  -0.7312 S22:   0.4252 S23:   0.4585                       
REMARK   3      S31:   1.4569 S32:  -0.4038 S33:  -0.5401                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     1        F    12                          
REMARK   3    RESIDUE RANGE :   I    63        I    75                          
REMARK   3    ORIGIN FOR THE GROUP (A):  84.3061  -5.0264  27.9400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4309 T22:   0.1173                                     
REMARK   3      T33:   0.1097 T12:  -0.0672                                     
REMARK   3      T13:  -0.2059 T23:   0.0934                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5837 L22:   8.4797                                     
REMARK   3      L33:  15.3298 L12:   1.6960                                     
REMARK   3      L13:  -1.2973 L23:  -5.8958                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5319 S12:   0.1692 S13:  -0.0475                       
REMARK   3      S21:  -0.3571 S22:   0.4634 S23:   0.9829                       
REMARK   3      S31:   1.2071 S32:  -1.5190 S33:  -0.9953                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     2        G    14                          
REMARK   3    RESIDUE RANGE :   J    61        J    73                          
REMARK   3    ORIGIN FOR THE GROUP (A):  75.5865  29.6286  68.2222              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2350 T22:  -0.1937                                     
REMARK   3      T33:  -0.1416 T12:  -0.0210                                     
REMARK   3      T13:  -0.0319 T23:   0.0362                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2497 L22:   8.8305                                     
REMARK   3      L33:   2.0124 L12:  -2.0323                                     
REMARK   3      L13:   0.3741 L23:  -4.0029                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1493 S12:  -0.1765 S13:   0.0916                       
REMARK   3      S21:  -0.0635 S22:  -0.0912 S23:  -0.4834                       
REMARK   3      S31:   0.1842 S32:   0.3039 S33:   0.2405                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1TFW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000022613.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 122568                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1R89                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       42.38500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, H, G, J, A, B                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, I, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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      A G   6   O5'     A G   6   C5'    -0.063                       
REMARK 500      U G   7   O3'     C G   8   P       0.141                       
REMARK 500    GLU B 387   CG    GLU B 387   CD      0.102                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500      C G   9   C2  -  N3  -  C4  ANGL. DEV. =   4.1 DEGREES          
REMARK 500      C J  61   N1  -  C2  -  O2  ANGL. DEV. =   4.7 DEGREES          
REMARK 500      G J  64   C8  -  N9  -  C4  ANGL. DEV. =  -2.5 DEGREES          
REMARK 500      G J  64   N9  -  C4  -  C5  ANGL. DEV. =   2.4 DEGREES          
REMARK 500      C J  69   O4' -  C1' -  N1  ANGL. DEV. =   4.8 DEGREES          
REMARK 500      G J  70   C3' -  O3' -  P   ANGL. DEV. =   8.9 DEGREES          
REMARK 500    ARG B 343   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG C 299   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG C 299   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ARG C 302   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG C 373   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  94      158.03     61.87                                   
REMARK 500    GLU A  96      -91.98    123.93                                   
REMARK 500    LEU A 117      130.52     70.86                                   
REMARK 500    LEU A 186      -60.16     92.99                                   
REMARK 500    VAL A 203      -63.10    -25.88                                   
REMARK 500    ASP A 221       99.99   -162.34                                   
REMARK 500    ALA A 248       79.50   -157.29                                   
REMARK 500    PRO A 259      154.89    -34.55                                   
REMARK 500    GLU A 261       90.62     59.78                                   
REMARK 500    LYS B   2      119.74    112.30                                   
REMARK 500    VAL B  14      -35.54   -132.16                                   
REMARK 500    SER B  57       46.09   -144.13                                   
REMARK 500    GLU B  69       47.96    -93.19                                   
REMARK 500    SER B  71      159.92     87.47                                   
REMARK 500    GLU B  96      -67.47   -142.38                                   
REMARK 500    LEU B 117      139.14     64.51                                   
REMARK 500    PRO B 120       39.78    -83.55                                   
REMARK 500    ALA B 126      -25.22    139.44                                   
REMARK 500    LEU B 186      -59.79     92.43                                   
REMARK 500    ALA B 248       81.57   -156.22                                   
REMARK 500    PRO B 259      154.95    -48.67                                   
REMARK 500    GLU B 261       93.13     46.43                                   
REMARK 500    LEU B 400       39.26    -93.81                                   
REMARK 500    LYS C   2       70.58     51.01                                   
REMARK 500    TYR C  94       70.72   -111.75                                   
REMARK 500    ALA C  95      -75.21    -69.14                                   
REMARK 500    GLU C  96      -48.73   -136.57                                   
REMARK 500    LEU C 117      128.13     63.84                                   
REMARK 500    LYS C 121      -39.10   -176.62                                   
REMARK 500    LEU C 186      -58.53     95.70                                   
REMARK 500    ALA C 248       73.96   -150.89                                   
REMARK 500    GLU C 261       75.37     45.47                                   
REMARK 500    LYS D   2      123.49     97.75                                   
REMARK 500    GLU D  68       43.01    -87.12                                   
REMARK 500    GLU D  96      -61.83   -138.19                                   
REMARK 500    CYS D 114     -140.53   -152.46                                   
REMARK 500    LYS D 116      -75.84    -72.34                                   
REMARK 500    LEU D 117      134.13     61.55                                   
REMARK 500    LYS D 118      -78.29    -75.61                                   
REMARK 500    LEU D 186      -59.16     93.36                                   
REMARK 500    ALA D 248       74.79   -154.79                                   
REMARK 500    GLU D 261       94.11     63.79                                   
REMARK 500    LEU D 316      -65.96    -92.44                                   
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                              MG B1601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  59   OE2                                                    
REMARK 620 2 ASP B  61   OD2  74.4                                              
REMARK 620 3 ATP B1501   O3G 109.4 165.7                                        
REMARK 620 4 ATP B1501   O2B 164.0  89.6  86.0                                  
REMARK 620 5 ATP B1501   O1A  95.5  70.1  95.7  77.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D1602  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D  59   OE1                                                    
REMARK 620 2 ASP D  61   OD2  80.7                                              
REMARK 620 3 ATP D1502   O1A 104.7  86.4                                        
REMARK 620 4 ATP D1502   O3G 116.8 157.7 101.1                                  
REMARK 620 5 ATP D1502   O2B 157.5  79.5  84.5  80.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 1501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP D 1502                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SZ1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1TFY   RELATED DB: PDB                                   
DBREF  1TFW A    1   437  UNP    O28126   CCA_ARCFU        1    437             
DBREF  1TFW B    1   437  UNP    O28126   CCA_ARCFU        1    437             
DBREF  1TFW C    1   437  UNP    O28126   CCA_ARCFU        1    437             
DBREF  1TFW D    1   437  UNP    O28126   CCA_ARCFU        1    437             
DBREF  1TFW E    1    12  PDB    1TFW     1TFW             1     12             
DBREF  1TFW H   63    75  PDB    1TFW     1TFW            63     75             
DBREF  1TFW F    1    12  PDB    1TFW     1TFW             1     12             
DBREF  1TFW I   63    75  PDB    1TFW     1TFW            63     75             
DBREF  1TFW G    2    14  PDB    1TFW     1TFW             2     14             
DBREF  1TFW J   61    73  PDB    1TFW     1TFW            61     73             
SEQRES   1 E   12    G   C   G   G   A   U   C   C   G   C   A   C              
SEQRES   1 H   13    G   C   G   G   A   U   C   C   G   C   A   C   C          
SEQRES   1 F   12    G   C   G   G   A   C   C   C   G   C   A   C              
SEQRES   1 I   13    G   C   G   G   A   U   C   C   G   C   A   C   C          
SEQRES   1 G   13    G   C   G   G   A   U   C   C   G   C   A   C   C          
SEQRES   1 J   13    C   G   C   G   G   A   U   C   C   G   C   A   C          
SEQRES   1 A  437  MET LYS VAL GLU GLU ILE LEU GLU LYS ALA LEU GLU LEU          
SEQRES   2 A  437  VAL ILE PRO ASP GLU GLU GLU VAL ARG LYS GLY ARG GLU          
SEQRES   3 A  437  ALA GLU GLU GLU LEU ARG ARG ARG LEU ASP GLU LEU GLY          
SEQRES   4 A  437  VAL GLU TYR VAL PHE VAL GLY SER TYR ALA ARG ASN THR          
SEQRES   5 A  437  TRP LEU LYS GLY SER LEU GLU ILE ASP VAL PHE LEU LEU          
SEQRES   6 A  437  PHE PRO GLU GLU PHE SER LYS GLU GLU LEU ARG GLU ARG          
SEQRES   7 A  437  GLY LEU GLU ILE GLY LYS ALA VAL LEU ASP SER TYR GLU          
SEQRES   8 A  437  ILE ARG TYR ALA GLU HIS PRO TYR VAL HIS GLY VAL VAL          
SEQRES   9 A  437  LYS GLY VAL GLU VAL ASP VAL VAL PRO CYS TYR LYS LEU          
SEQRES  10 A  437  LYS GLU PRO LYS ASN ILE LYS SER ALA VAL ASP ARG THR          
SEQRES  11 A  437  PRO PHE HIS HIS LYS TRP LEU GLU GLY ARG ILE LYS GLY          
SEQRES  12 A  437  LYS GLU ASN GLU VAL ARG LEU LEU LYS GLY PHE LEU LYS          
SEQRES  13 A  437  ALA ASN GLY ILE TYR GLY ALA GLU TYR LYS VAL ARG GLY          
SEQRES  14 A  437  PHE SER GLY TYR LEU CYS GLU LEU LEU ILE VAL PHE TYR          
SEQRES  15 A  437  GLY SER PHE LEU GLU THR VAL LYS ASN ALA ARG ARG TRP          
SEQRES  16 A  437  THR ARG ARG THR VAL ILE ASP VAL ALA LYS GLY GLU VAL          
SEQRES  17 A  437  ARG LYS GLY GLU GLU PHE PHE VAL VAL ASP PRO VAL ASP          
SEQRES  18 A  437  GLU LYS ARG ASN VAL ALA ALA ASN LEU SER LEU ASP ASN          
SEQRES  19 A  437  LEU ALA ARG PHE VAL HIS LEU CYS ARG GLU PHE MET GLU          
SEQRES  20 A  437  ALA PRO SER LEU GLY PHE PHE LYS PRO LYS HIS PRO LEU          
SEQRES  21 A  437  GLU ILE GLU PRO GLU ARG LEU ARG LYS ILE VAL GLU GLU          
SEQRES  22 A  437  ARG GLY THR ALA VAL PHE ALA VAL LYS PHE ARG LYS PRO          
SEQRES  23 A  437  ASP ILE VAL ASP ASP ASN LEU TYR PRO GLN LEU GLU ARG          
SEQRES  24 A  437  ALA SER ARG LYS ILE PHE GLU PHE LEU GLU ARG GLU ASN          
SEQRES  25 A  437  PHE MET PRO LEU ARG SER ALA PHE LYS ALA SER GLU GLU          
SEQRES  26 A  437  PHE CYS TYR LEU LEU PHE GLU CYS GLN ILE LYS GLU ILE          
SEQRES  27 A  437  SER ARG VAL PHE ARG ARG MET GLY PRO GLN PHE GLU ASP          
SEQRES  28 A  437  GLU ARG ASN VAL LYS LYS PHE LEU SER ARG ASN ARG ALA          
SEQRES  29 A  437  PHE ARG PRO PHE ILE GLU ASN GLY ARG TRP TRP ALA PHE          
SEQRES  30 A  437  GLU MET ARG LYS PHE THR THR PRO GLU GLU GLY VAL ARG          
SEQRES  31 A  437  SER TYR ALA SER THR HIS TRP HIS THR LEU GLY LYS ASN          
SEQRES  32 A  437  VAL GLY GLU SER ILE ARG GLU TYR PHE GLU ILE ILE SER          
SEQRES  33 A  437  GLY GLU LYS LEU PHE LYS GLU PRO VAL THR ALA GLU LEU          
SEQRES  34 A  437  CYS GLU MET MET GLY VAL LYS ASP                              
SEQRES   1 B  437  MET LYS VAL GLU GLU ILE LEU GLU LYS ALA LEU GLU LEU          
SEQRES   2 B  437  VAL ILE PRO ASP GLU GLU GLU VAL ARG LYS GLY ARG GLU          
SEQRES   3 B  437  ALA GLU GLU GLU LEU ARG ARG ARG LEU ASP GLU LEU GLY          
SEQRES   4 B  437  VAL GLU TYR VAL PHE VAL GLY SER TYR ALA ARG ASN THR          
SEQRES   5 B  437  TRP LEU LYS GLY SER LEU GLU ILE ASP VAL PHE LEU LEU          
SEQRES   6 B  437  PHE PRO GLU GLU PHE SER LYS GLU GLU LEU ARG GLU ARG          
SEQRES   7 B  437  GLY LEU GLU ILE GLY LYS ALA VAL LEU ASP SER TYR GLU          
SEQRES   8 B  437  ILE ARG TYR ALA GLU HIS PRO TYR VAL HIS GLY VAL VAL          
SEQRES   9 B  437  LYS GLY VAL GLU VAL ASP VAL VAL PRO CYS TYR LYS LEU          
SEQRES  10 B  437  LYS GLU PRO LYS ASN ILE LYS SER ALA VAL ASP ARG THR          
SEQRES  11 B  437  PRO PHE HIS HIS LYS TRP LEU GLU GLY ARG ILE LYS GLY          
SEQRES  12 B  437  LYS GLU ASN GLU VAL ARG LEU LEU LYS GLY PHE LEU LYS          
SEQRES  13 B  437  ALA ASN GLY ILE TYR GLY ALA GLU TYR LYS VAL ARG GLY          
SEQRES  14 B  437  PHE SER GLY TYR LEU CYS GLU LEU LEU ILE VAL PHE TYR          
SEQRES  15 B  437  GLY SER PHE LEU GLU THR VAL LYS ASN ALA ARG ARG TRP          
SEQRES  16 B  437  THR ARG ARG THR VAL ILE ASP VAL ALA LYS GLY GLU VAL          
SEQRES  17 B  437  ARG LYS GLY GLU GLU PHE PHE VAL VAL ASP PRO VAL ASP          
SEQRES  18 B  437  GLU LYS ARG ASN VAL ALA ALA ASN LEU SER LEU ASP ASN          
SEQRES  19 B  437  LEU ALA ARG PHE VAL HIS LEU CYS ARG GLU PHE MET GLU          
SEQRES  20 B  437  ALA PRO SER LEU GLY PHE PHE LYS PRO LYS HIS PRO LEU          
SEQRES  21 B  437  GLU ILE GLU PRO GLU ARG LEU ARG LYS ILE VAL GLU GLU          
SEQRES  22 B  437  ARG GLY THR ALA VAL PHE ALA VAL LYS PHE ARG LYS PRO          
SEQRES  23 B  437  ASP ILE VAL ASP ASP ASN LEU TYR PRO GLN LEU GLU ARG          
SEQRES  24 B  437  ALA SER ARG LYS ILE PHE GLU PHE LEU GLU ARG GLU ASN          
SEQRES  25 B  437  PHE MET PRO LEU ARG SER ALA PHE LYS ALA SER GLU GLU          
SEQRES  26 B  437  PHE CYS TYR LEU LEU PHE GLU CYS GLN ILE LYS GLU ILE          
SEQRES  27 B  437  SER ARG VAL PHE ARG ARG MET GLY PRO GLN PHE GLU ASP          
SEQRES  28 B  437  GLU ARG ASN VAL LYS LYS PHE LEU SER ARG ASN ARG ALA          
SEQRES  29 B  437  PHE ARG PRO PHE ILE GLU ASN GLY ARG TRP TRP ALA PHE          
SEQRES  30 B  437  GLU MET ARG LYS PHE THR THR PRO GLU GLU GLY VAL ARG          
SEQRES  31 B  437  SER TYR ALA SER THR HIS TRP HIS THR LEU GLY LYS ASN          
SEQRES  32 B  437  VAL GLY GLU SER ILE ARG GLU TYR PHE GLU ILE ILE SER          
SEQRES  33 B  437  GLY GLU LYS LEU PHE LYS GLU PRO VAL THR ALA GLU LEU          
SEQRES  34 B  437  CYS GLU MET MET GLY VAL LYS ASP                              
SEQRES   1 C  437  MET LYS VAL GLU GLU ILE LEU GLU LYS ALA LEU GLU LEU          
SEQRES   2 C  437  VAL ILE PRO ASP GLU GLU GLU VAL ARG LYS GLY ARG GLU          
SEQRES   3 C  437  ALA GLU GLU GLU LEU ARG ARG ARG LEU ASP GLU LEU GLY          
SEQRES   4 C  437  VAL GLU TYR VAL PHE VAL GLY SER TYR ALA ARG ASN THR          
SEQRES   5 C  437  TRP LEU LYS GLY SER LEU GLU ILE ASP VAL PHE LEU LEU          
SEQRES   6 C  437  PHE PRO GLU GLU PHE SER LYS GLU GLU LEU ARG GLU ARG          
SEQRES   7 C  437  GLY LEU GLU ILE GLY LYS ALA VAL LEU ASP SER TYR GLU          
SEQRES   8 C  437  ILE ARG TYR ALA GLU HIS PRO TYR VAL HIS GLY VAL VAL          
SEQRES   9 C  437  LYS GLY VAL GLU VAL ASP VAL VAL PRO CYS TYR LYS LEU          
SEQRES  10 C  437  LYS GLU PRO LYS ASN ILE LYS SER ALA VAL ASP ARG THR          
SEQRES  11 C  437  PRO PHE HIS HIS LYS TRP LEU GLU GLY ARG ILE LYS GLY          
SEQRES  12 C  437  LYS GLU ASN GLU VAL ARG LEU LEU LYS GLY PHE LEU LYS          
SEQRES  13 C  437  ALA ASN GLY ILE TYR GLY ALA GLU TYR LYS VAL ARG GLY          
SEQRES  14 C  437  PHE SER GLY TYR LEU CYS GLU LEU LEU ILE VAL PHE TYR          
SEQRES  15 C  437  GLY SER PHE LEU GLU THR VAL LYS ASN ALA ARG ARG TRP          
SEQRES  16 C  437  THR ARG ARG THR VAL ILE ASP VAL ALA LYS GLY GLU VAL          
SEQRES  17 C  437  ARG LYS GLY GLU GLU PHE PHE VAL VAL ASP PRO VAL ASP          
SEQRES  18 C  437  GLU LYS ARG ASN VAL ALA ALA ASN LEU SER LEU ASP ASN          
SEQRES  19 C  437  LEU ALA ARG PHE VAL HIS LEU CYS ARG GLU PHE MET GLU          
SEQRES  20 C  437  ALA PRO SER LEU GLY PHE PHE LYS PRO LYS HIS PRO LEU          
SEQRES  21 C  437  GLU ILE GLU PRO GLU ARG LEU ARG LYS ILE VAL GLU GLU          
SEQRES  22 C  437  ARG GLY THR ALA VAL PHE ALA VAL LYS PHE ARG LYS PRO          
SEQRES  23 C  437  ASP ILE VAL ASP ASP ASN LEU TYR PRO GLN LEU GLU ARG          
SEQRES  24 C  437  ALA SER ARG LYS ILE PHE GLU PHE LEU GLU ARG GLU ASN          
SEQRES  25 C  437  PHE MET PRO LEU ARG SER ALA PHE LYS ALA SER GLU GLU          
SEQRES  26 C  437  PHE CYS TYR LEU LEU PHE GLU CYS GLN ILE LYS GLU ILE          
SEQRES  27 C  437  SER ARG VAL PHE ARG ARG MET GLY PRO GLN PHE GLU ASP          
SEQRES  28 C  437  GLU ARG ASN VAL LYS LYS PHE LEU SER ARG ASN ARG ALA          
SEQRES  29 C  437  PHE ARG PRO PHE ILE GLU ASN GLY ARG TRP TRP ALA PHE          
SEQRES  30 C  437  GLU MET ARG LYS PHE THR THR PRO GLU GLU GLY VAL ARG          
SEQRES  31 C  437  SER TYR ALA SER THR HIS TRP HIS THR LEU GLY LYS ASN          
SEQRES  32 C  437  VAL GLY GLU SER ILE ARG GLU TYR PHE GLU ILE ILE SER          
SEQRES  33 C  437  GLY GLU LYS LEU PHE LYS GLU PRO VAL THR ALA GLU LEU          
SEQRES  34 C  437  CYS GLU MET MET GLY VAL LYS ASP                              
SEQRES   1 D  437  MET LYS VAL GLU GLU ILE LEU GLU LYS ALA LEU GLU LEU          
SEQRES   2 D  437  VAL ILE PRO ASP GLU GLU GLU VAL ARG LYS GLY ARG GLU          
SEQRES   3 D  437  ALA GLU GLU GLU LEU ARG ARG ARG LEU ASP GLU LEU GLY          
SEQRES   4 D  437  VAL GLU TYR VAL PHE VAL GLY SER TYR ALA ARG ASN THR          
SEQRES   5 D  437  TRP LEU LYS GLY SER LEU GLU ILE ASP VAL PHE LEU LEU          
SEQRES   6 D  437  PHE PRO GLU GLU PHE SER LYS GLU GLU LEU ARG GLU ARG          
SEQRES   7 D  437  GLY LEU GLU ILE GLY LYS ALA VAL LEU ASP SER TYR GLU          
SEQRES   8 D  437  ILE ARG TYR ALA GLU HIS PRO TYR VAL HIS GLY VAL VAL          
SEQRES   9 D  437  LYS GLY VAL GLU VAL ASP VAL VAL PRO CYS TYR LYS LEU          
SEQRES  10 D  437  LYS GLU PRO LYS ASN ILE LYS SER ALA VAL ASP ARG THR          
SEQRES  11 D  437  PRO PHE HIS HIS LYS TRP LEU GLU GLY ARG ILE LYS GLY          
SEQRES  12 D  437  LYS GLU ASN GLU VAL ARG LEU LEU LYS GLY PHE LEU LYS          
SEQRES  13 D  437  ALA ASN GLY ILE TYR GLY ALA GLU TYR LYS VAL ARG GLY          
SEQRES  14 D  437  PHE SER GLY TYR LEU CYS GLU LEU LEU ILE VAL PHE TYR          
SEQRES  15 D  437  GLY SER PHE LEU GLU THR VAL LYS ASN ALA ARG ARG TRP          
SEQRES  16 D  437  THR ARG ARG THR VAL ILE ASP VAL ALA LYS GLY GLU VAL          
SEQRES  17 D  437  ARG LYS GLY GLU GLU PHE PHE VAL VAL ASP PRO VAL ASP          
SEQRES  18 D  437  GLU LYS ARG ASN VAL ALA ALA ASN LEU SER LEU ASP ASN          
SEQRES  19 D  437  LEU ALA ARG PHE VAL HIS LEU CYS ARG GLU PHE MET GLU          
SEQRES  20 D  437  ALA PRO SER LEU GLY PHE PHE LYS PRO LYS HIS PRO LEU          
SEQRES  21 D  437  GLU ILE GLU PRO GLU ARG LEU ARG LYS ILE VAL GLU GLU          
SEQRES  22 D  437  ARG GLY THR ALA VAL PHE ALA VAL LYS PHE ARG LYS PRO          
SEQRES  23 D  437  ASP ILE VAL ASP ASP ASN LEU TYR PRO GLN LEU GLU ARG          
SEQRES  24 D  437  ALA SER ARG LYS ILE PHE GLU PHE LEU GLU ARG GLU ASN          
SEQRES  25 D  437  PHE MET PRO LEU ARG SER ALA PHE LYS ALA SER GLU GLU          
SEQRES  26 D  437  PHE CYS TYR LEU LEU PHE GLU CYS GLN ILE LYS GLU ILE          
SEQRES  27 D  437  SER ARG VAL PHE ARG ARG MET GLY PRO GLN PHE GLU ASP          
SEQRES  28 D  437  GLU ARG ASN VAL LYS LYS PHE LEU SER ARG ASN ARG ALA          
SEQRES  29 D  437  PHE ARG PRO PHE ILE GLU ASN GLY ARG TRP TRP ALA PHE          
SEQRES  30 D  437  GLU MET ARG LYS PHE THR THR PRO GLU GLU GLY VAL ARG          
SEQRES  31 D  437  SER TYR ALA SER THR HIS TRP HIS THR LEU GLY LYS ASN          
SEQRES  32 D  437  VAL GLY GLU SER ILE ARG GLU TYR PHE GLU ILE ILE SER          
SEQRES  33 D  437  GLY GLU LYS LEU PHE LYS GLU PRO VAL THR ALA GLU LEU          
SEQRES  34 D  437  CYS GLU MET MET GLY VAL LYS ASP                              
HET     MG  B1601       1                                                       
HET    ATP  B1501      31                                                       
HET     MG  D1602       1                                                       
HET    ATP  D1502      31                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL  11   MG    2(MG 2+)                                                     
FORMUL  12  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL  15  HOH   *1059(H2 O)                                                   
HELIX    1   1 LYS A    2  LEU A   13  1                                  12    
HELIX    2   2 ASP A   17  LEU A   38  1                                  22    
HELIX    3   3 GLY A   46  ARG A   50  1                                   5    
HELIX    4   4 SER A   71  LEU A   87  1                                  17    
HELIX    5   5 GLU A  119  ILE A  123  5                                   5    
HELIX    6   6 ARG A  129  GLU A  138  1                                  10    
HELIX    7   7 LYS A  144  ASN A  158  1                                  15    
HELIX    8   8 SER A  171  GLY A  183  1                                  13    
HELIX    9   9 LEU A  186  ARG A  193  1                                   8    
HELIX   10  10 SER A  231  ALA A  248  1                                  18    
HELIX   11  11 SER A  250  LYS A  255  5                                   6    
HELIX   12  12 GLU A  263  GLY A  275  1                                  13    
HELIX   13  13 VAL A  289  GLU A  311  1                                  23    
HELIX   14  14 ASP A  351  ARG A  361  1                                  11    
HELIX   15  15 THR A  384  HIS A  396  1                                  13    
HELIX   16  16 TRP A  397  LEU A  400  5                                   4    
HELIX   17  17 GLY A  401  TYR A  411  1                                  11    
HELIX   18  18 GLY A  417  LYS A  422  1                                   6    
HELIX   19  19 VAL A  425  GLY A  434  1                                  10    
HELIX   20  20 LYS B    2  LEU B   13  1                                  12    
HELIX   21  21 ASP B   17  GLY B   39  1                                  23    
HELIX   22  22 GLY B   46  ARG B   50  1                                   5    
HELIX   23  23 SER B   71  LEU B   87  1                                  17    
HELIX   24  24 ARG B  129  GLU B  138  1                                  10    
HELIX   25  25 LYS B  144  ASN B  158  1                                  15    
HELIX   26  26 SER B  171  GLY B  183  1                                  13    
HELIX   27  27 LEU B  186  ARG B  193  1                                   8    
HELIX   28  28 SER B  231  ALA B  248  1                                  18    
HELIX   29  29 SER B  250  LYS B  255  5                                   6    
HELIX   30  30 GLU B  263  GLY B  275  1                                  13    
HELIX   31  31 VAL B  289  GLU B  311  1                                  23    
HELIX   32  32 ASP B  351  ARG B  361  1                                  11    
HELIX   33  33 THR B  384  HIS B  396  1                                  13    
HELIX   34  34 TRP B  397  LEU B  400  5                                   4    
HELIX   35  35 GLY B  401  TYR B  411  1                                  11    
HELIX   36  36 GLY B  417  PHE B  421  1                                   5    
HELIX   37  37 VAL B  425  GLY B  434  1                                  10    
HELIX   38  38 LYS C    2  LEU C   13  1                                  12    
HELIX   39  39 ASP C   17  LEU C   38  1                                  22    
HELIX   40  40 GLY C   46  ARG C   50  1                                   5    
HELIX   41  41 SER C   71  LEU C   87  1                                  17    
HELIX   42  42 SER C  125  GLU C  138  1                                  14    
HELIX   43  43 LYS C  144  ASN C  158  1                                  15    
HELIX   44  44 SER C  171  GLY C  183  1                                  13    
HELIX   45  45 LEU C  186  ARG C  193  1                                   8    
HELIX   46  46 SER C  231  ALA C  248  1                                  18    
HELIX   47  47 SER C  250  LYS C  255  5                                   6    
HELIX   48  48 GLU C  263  GLY C  275  1                                  13    
HELIX   49  49 VAL C  289  GLU C  311  1                                  23    
HELIX   50  50 ASP C  351  ARG C  361  1                                  11    
HELIX   51  51 THR C  384  HIS C  396  1                                  13    
HELIX   52  52 TRP C  397  LEU C  400  5                                   4    
HELIX   53  53 GLY C  401  TYR C  411  1                                  11    
HELIX   54  54 GLY C  417  LYS C  422  1                                   6    
HELIX   55  55 VAL C  425  GLY C  434  1                                  10    
HELIX   56  56 LYS D    2  LEU D   11  1                                  10    
HELIX   57  57 ASP D   17  GLY D   39  1                                  23    
HELIX   58  58 GLY D   46  ARG D   50  1                                   5    
HELIX   59  59 SER D   71  VAL D   86  1                                  16    
HELIX   60  60 ARG D  129  GLU D  138  1                                  10    
HELIX   61  61 LYS D  144  ASN D  158  1                                  15    
HELIX   62  62 SER D  171  GLY D  183  1                                  13    
HELIX   63  63 LEU D  186  ARG D  193  1                                   8    
HELIX   64  64 SER D  231  ALA D  248  1                                  18    
HELIX   65  65 SER D  250  LYS D  255  5                                   6    
HELIX   66  66 GLU D  263  GLY D  275  1                                  13    
HELIX   67  67 VAL D  289  GLU D  311  1                                  23    
HELIX   68  68 ASP D  351  ARG D  361  1                                  11    
HELIX   69  69 THR D  384  HIS D  396  1                                  13    
HELIX   70  70 TRP D  397  LEU D  400  5                                   4    
HELIX   71  71 GLY D  401  TYR D  411  1                                  11    
HELIX   72  72 GLU D  418  GLU D  423  5                                   6    
HELIX   73  73 VAL D  425  GLY D  434  1                                  10    
SHEET    1   A 5 TYR A  42  VAL A  45  0                                        
SHEET    2   A 5 GLU A  59  PHE A  66 -1  O  PHE A  63   N  VAL A  43           
SHEET    3   A 5 VAL A 107  TYR A 115  1  O  VAL A 112   N  LEU A  64           
SHEET    4   A 5 TYR A  99  VAL A 104 -1  N  GLY A 102   O  VAL A 109           
SHEET    5   A 5 SER A  89  ARG A  93 -1  N  GLU A  91   O  HIS A 101           
SHEET    1   B 4 GLU A 207  LYS A 210  0                                        
SHEET    2   B 4 THR A 199  ASP A 202 -1  N  ASP A 202   O  GLU A 207           
SHEET    3   B 4 PHE A 215  ASP A 218  1  O  PHE A 215   N  ILE A 201           
SHEET    4   B 4 ASP A 221  ASN A 225 -1  O  ARG A 224   N  ASP A 218           
SHEET    1   C 4 PRO A 315  ALA A 322  0                                        
SHEET    2   C 4 PHE A 326  CYS A 333 -1  O  GLU A 332   N  LEU A 316           
SHEET    3   C 4 ALA A 277  ARG A 284 -1  N  PHE A 283   O  CYS A 327           
SHEET    4   C 4 GLU A 413  SER A 416 -1  O  GLU A 413   N  LYS A 282           
SHEET    1   D 3 VAL A 341  GLN A 348  0                                        
SHEET    2   D 3 ARG A 373  MET A 379 -1  O  ALA A 376   N  ARG A 344           
SHEET    3   D 3 PHE A 368  GLU A 370 -1  N  GLU A 370   O  ARG A 373           
SHEET    1   E 5 TYR B  42  VAL B  45  0                                        
SHEET    2   E 5 GLU B  59  PHE B  66 -1  O  PHE B  63   N  VAL B  43           
SHEET    3   E 5 VAL B 107  TYR B 115  1  O  VAL B 112   N  VAL B  62           
SHEET    4   E 5 VAL B 100  VAL B 104 -1  N  VAL B 100   O  VAL B 111           
SHEET    5   E 5 SER B  89  GLU B  91 -1  N  GLU B  91   O  HIS B 101           
SHEET    1   F 4 GLU B 207  LYS B 210  0                                        
SHEET    2   F 4 THR B 199  ASP B 202 -1  N  VAL B 200   O  ARG B 209           
SHEET    3   F 4 PHE B 215  ASP B 218  1  O  PHE B 215   N  ILE B 201           
SHEET    4   F 4 ASP B 221  ASN B 225 -1  O  ARG B 224   N  ASP B 218           
SHEET    1   G 4 PRO B 315  ALA B 322  0                                        
SHEET    2   G 4 PHE B 326  CYS B 333 -1  O  GLU B 332   N  LEU B 316           
SHEET    3   G 4 ALA B 277  ARG B 284 -1  N  PHE B 283   O  CYS B 327           
SHEET    4   G 4 GLU B 413  SER B 416 -1  O  GLU B 413   N  LYS B 282           
SHEET    1   H 3 VAL B 341  GLN B 348  0                                        
SHEET    2   H 3 ARG B 373  MET B 379 -1  O  ALA B 376   N  ARG B 344           
SHEET    3   H 3 PHE B 368  GLU B 370 -1  N  GLU B 370   O  ARG B 373           
SHEET    1   I 5 TYR C  42  VAL C  45  0                                        
SHEET    2   I 5 GLU C  59  PHE C  66 -1  O  PHE C  63   N  VAL C  43           
SHEET    3   I 5 VAL C 107  TYR C 115  1  O  VAL C 112   N  VAL C  62           
SHEET    4   I 5 TYR C  99  VAL C 104 -1  N  VAL C 100   O  VAL C 111           
SHEET    5   I 5 SER C  89  ARG C  93 -1  N  GLU C  91   O  HIS C 101           
SHEET    1   J 4 GLU C 207  LYS C 210  0                                        
SHEET    2   J 4 THR C 199  ASP C 202 -1  N  VAL C 200   O  ARG C 209           
SHEET    3   J 4 PHE C 215  ASP C 218  1  O  PHE C 215   N  ILE C 201           
SHEET    4   J 4 ASP C 221  ASN C 225 -1  O  ARG C 224   N  ASP C 218           
SHEET    1   K 4 PRO C 315  ALA C 322  0                                        
SHEET    2   K 4 PHE C 326  CYS C 333 -1  O  GLU C 332   N  LEU C 316           
SHEET    3   K 4 ALA C 277  ARG C 284 -1  N  PHE C 283   O  CYS C 327           
SHEET    4   K 4 GLU C 413  SER C 416 -1  O  GLU C 413   N  LYS C 282           
SHEET    1   L 3 VAL C 341  GLN C 348  0                                        
SHEET    2   L 3 ARG C 373  MET C 379 -1  O  ALA C 376   N  ARG C 344           
SHEET    3   L 3 PHE C 368  GLU C 370 -1  N  PHE C 368   O  TRP C 375           
SHEET    1   M 5 TYR D  42  VAL D  45  0                                        
SHEET    2   M 5 GLU D  59  LEU D  64 -1  O  PHE D  63   N  VAL D  43           
SHEET    3   M 5 VAL D 107  PRO D 113  1  O  VAL D 112   N  VAL D  62           
SHEET    4   M 5 VAL D 100  VAL D 104 -1  N  GLY D 102   O  VAL D 109           
SHEET    5   M 5 TYR D  90  GLU D  91 -1  N  GLU D  91   O  HIS D 101           
SHEET    1   N 4 GLU D 207  LYS D 210  0                                        
SHEET    2   N 4 THR D 199  ASP D 202 -1  N  VAL D 200   O  ARG D 209           
SHEET    3   N 4 PHE D 215  ASP D 218  1  O  PHE D 215   N  ILE D 201           
SHEET    4   N 4 ASP D 221  ASN D 225 -1  O  ARG D 224   N  ASP D 218           
SHEET    1   O 4 PRO D 315  ALA D 322  0                                        
SHEET    2   O 4 PHE D 326  CYS D 333 -1  O  LEU D 330   N  ALA D 319           
SHEET    3   O 4 ALA D 277  ARG D 284 -1  N  PHE D 283   O  CYS D 327           
SHEET    4   O 4 GLU D 413  SER D 416 -1  O  GLU D 413   N  LYS D 282           
SHEET    1   P 3 VAL D 341  GLN D 348  0                                        
SHEET    2   P 3 ARG D 373  MET D 379 -1  O  ALA D 376   N  ARG D 344           
SHEET    3   P 3 PHE D 368  GLU D 370 -1  N  GLU D 370   O  ARG D 373           
LINK         OE2 GLU B  59                MG    MG B1601     1555   1555  2.22  
LINK         OD2 ASP B  61                MG    MG B1601     1555   1555  2.60  
LINK         O3G ATP B1501                MG    MG B1601     1555   1555  1.89  
LINK         O2B ATP B1501                MG    MG B1601     1555   1555  2.11  
LINK         O1A ATP B1501                MG    MG B1601     1555   1555  2.31  
LINK         OE1 GLU D  59                MG    MG D1602     1555   1555  2.48  
LINK         OD2 ASP D  61                MG    MG D1602     1555   1555  2.52  
LINK         O1A ATP D1502                MG    MG D1602     1555   1555  1.98  
LINK         O3G ATP D1502                MG    MG D1602     1555   1555  2.11  
LINK         O2B ATP D1502                MG    MG D1602     1555   1555  2.18  
SITE     1 AC1  4 SER B  47  GLU B  59  ASP B  61  ATP B1501                    
SITE     1 AC2  3 GLU D  59  ASP D  61  ATP D1502                               
SITE     1 AC3 16 GLY B  46  SER B  47  ARG B  50  GLU B  59                    
SITE     2 AC3 16 ASP B  61  THR B 130  HIS B 133  LYS B 152                    
SITE     3 AC3 16 TYR B 161  ARG B 224   MG B1601  HOH B1647                    
SITE     4 AC3 16 HOH B1685    A H  73    C H  74    C H  75                    
SITE     1 AC4 17 GLY D  46  SER D  47  ARG D  50  GLU D  59                    
SITE     2 AC4 17 ASP D  61  THR D 130  HIS D 133  LYS D 152                    
SITE     3 AC4 17 TYR D 161  ARG D 224   MG D1602  HOH D1675                    
SITE     4 AC4 17 HOH D1753  HOH D1767    A I  73    C I  74                    
SITE     5 AC4 17   C I  75                                                     
CRYST1  116.641   84.770  135.813  90.00 104.66  90.00 P 1 21 1      8          
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      0.008573  0.000000  0.002243        0.00000                         
SCALE2      0.000000  0.011797  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007611        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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