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Database: PDB
Entry: 4FK0
LinkDB: 4FK0
Original site: 4FK0 
HEADER    TRANSFERASE/DNA                         12-JUN-12   4FK0              
TITLE     RB69 DNA POLYMERASE TERNARY COMPLEX WITH DCTP/DG                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA POLYMERASE;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: GP43;                                                       
COMPND   5 EC: 2.7.7.7;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: DNA TEMPLATE;                                              
COMPND  10 CHAIN: T;                                                            
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: DNA PRIMER;                                                
COMPND  14 CHAIN: P;                                                            
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE RB69;                      
SOURCE   3 ORGANISM_TAXID: 12353;                                               
SOURCE   4 GENE: 43;                                                            
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 SYNTHETIC: YES;                                                      
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 SYNTHETIC: YES                                                       
KEYWDS    DCTP/DG, RB69, RB69 POL, QUADRUPLE, TRANSFERASE-DNA COMPLEX           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.XIA,J.WANG,W.H.KONIGSBERG                                           
REVDAT   3   28-FEB-24 4FK0    1       REMARK SEQADV LINK                       
REVDAT   2   30-JAN-13 4FK0    1       JRNL                                     
REVDAT   1   19-DEC-12 4FK0    0                                                
JRNL        AUTH   S.XIA,J.WANG,W.H.KONIGSBERG                                  
JRNL        TITL   DNA MISMATCH SYNTHESIS COMPLEXES PROVIDE INSIGHTS INTO BASE  
JRNL        TITL 2 SELECTIVITY OF A B FAMILY DNA POLYMERASE.                    
JRNL        REF    J.AM.CHEM.SOC.                V. 135   193 2013              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   23214497                                                     
JRNL        DOI    10.1021/JA3079048                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.18 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.18                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.21                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 58032                          
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3105                            
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) : 2.18                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.23                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3793                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.31                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3180                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 198                          
REMARK   3   BIN FREE R VALUE                    : 0.3870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7329                                    
REMARK   3   NUCLEIC ACID ATOMS       : 614                                     
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 364                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.65000                                              
REMARK   3    B33 (A**2) : -0.66000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.256         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.213         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.155         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.271        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8224 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11247 ; 1.255 ; 1.905       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   899 ; 5.650 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   371 ;35.404 ;24.178       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1339 ;15.117 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;14.655 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1162 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6071 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  4490 ; 1.719 ; 4.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7275 ; 2.837 ; 6.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3733 ; 3.359 ; 6.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3968 ; 4.799 ; 9.000       
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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   T     2        T    18                          
REMARK   3    RESIDUE RANGE :   P   103        P   114                          
REMARK   3    RESIDUE RANGE :   A  1001        A  1001                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.3670  -2.7460 -35.7090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1290 T22:   0.1893                                     
REMARK   3      T33:   0.2926 T12:   0.0415                                     
REMARK   3      T13:  -0.0357 T23:  -0.0115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2207 L22:   0.1048                                     
REMARK   3      L33:   0.0278 L12:   0.1287                                     
REMARK   3      L13:   0.0221 L23:   0.0255                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1290 S12:  -0.0267 S13:   0.1966                       
REMARK   3      S21:  -0.0621 S22:   0.0581 S23:   0.1232                       
REMARK   3      S31:   0.0240 S32:   0.0251 S33:   0.0709                       
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     1        A   105                          
REMARK   3    RESIDUE RANGE :   A   340        A   389                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.8240   2.1840 -33.6490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0402 T22:   0.0407                                     
REMARK   3      T33:   0.1148 T12:  -0.0133                                     
REMARK   3      T13:  -0.0173 T23:   0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1055 L22:   1.2146                                     
REMARK   3      L33:   0.2476 L12:   0.1077                                     
REMARK   3      L13:  -0.1315 L23:  -0.4184                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0020 S12:  -0.0008 S13:   0.0136                       
REMARK   3      S21:   0.0454 S22:  -0.0355 S23:  -0.1036                       
REMARK   3      S31:  -0.0234 S32:   0.0283 S33:   0.0336                       
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   106        A   339                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.3560 -22.0170 -14.9650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0283 T22:   0.0388                                     
REMARK   3      T33:   0.0638 T12:  -0.0093                                     
REMARK   3      T13:  -0.0109 T23:  -0.0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2533 L22:   0.6372                                     
REMARK   3      L33:   0.9535 L12:   0.2285                                     
REMARK   3      L13:   0.1302 L23:   0.1465                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0175 S12:  -0.0232 S13:   0.0435                       
REMARK   3      S21:   0.0771 S22:  -0.0511 S23:  -0.0363                       
REMARK   3      S31:   0.0442 S32:  -0.0832 S33:   0.0336                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   390        A   468                          
REMARK   3    RESIDUE RANGE :   A   576        A   706                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5890  -6.6780 -60.2830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0568 T22:   0.1083                                     
REMARK   3      T33:   0.0274 T12:  -0.0350                                     
REMARK   3      T13:  -0.0131 T23:   0.0192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6647 L22:   0.6481                                     
REMARK   3      L33:   0.1866 L12:   0.4053                                     
REMARK   3      L13:  -0.2202 L23:   0.0383                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0490 S12:   0.2245 S13:   0.0349                       
REMARK   3      S21:  -0.0815 S22:   0.0973 S23:  -0.0034                       
REMARK   3      S31:  -0.0015 S32:  -0.1030 S33:  -0.0483                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   469        A   575                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.4330 -26.3640 -47.2050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0449 T22:   0.0581                                     
REMARK   3      T33:   0.0872 T12:   0.0006                                     
REMARK   3      T13:   0.0179 T23:  -0.0112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4072 L22:   2.2997                                     
REMARK   3      L33:   0.2841 L12:   0.0572                                     
REMARK   3      L13:  -0.0286 L23:   0.4831                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0245 S12:   0.0854 S13:  -0.1037                       
REMARK   3      S21:   0.1330 S22:  -0.0563 S23:  -0.0389                       
REMARK   3      S31:   0.0497 S32:   0.0443 S33:   0.0809                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   707        A   737                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.4660 -22.7760 -47.9540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0396 T22:   0.1081                                     
REMARK   3      T33:   0.0974 T12:  -0.0379                                     
REMARK   3      T13:  -0.0003 T23:  -0.0413                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7520 L22:   0.7092                                     
REMARK   3      L33:   1.1519 L12:  -0.5068                                     
REMARK   3      L13:  -0.8785 L23:   0.3916                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0445 S12:  -0.0368 S13:  -0.0178                       
REMARK   3      S21:   0.0311 S22:   0.0760 S23:   0.0555                       
REMARK   3      S31:   0.0488 S32:   0.0526 S33:  -0.0315                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   738        A   900                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.1990 -20.7170 -27.6800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0079 T22:   0.1243                                     
REMARK   3      T33:   0.0740 T12:   0.0231                                     
REMARK   3      T13:   0.0145 T23:   0.0545                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5794 L22:   0.3985                                     
REMARK   3      L33:   1.5662 L12:   0.0403                                     
REMARK   3      L13:   0.3174 L23:   0.5792                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1034 S12:  -0.2877 S13:  -0.1311                       
REMARK   3      S21:   0.0080 S22:   0.0852 S23:   0.0651                       
REMARK   3      S31:  -0.0104 S32:  -0.1198 S33:   0.0183                       
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 USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4FK0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000072994.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : APEX II CCD                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58032                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.180                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.800                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : 2.18                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 150 MM CACL2, 10% (W/V) PEG 350          
REMARK 280  MONOMETHYL ETHER (MME), AND 100 MM SODIUM CACODYLATE PH 6.5,        
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 298K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       37.42300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.30950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.07450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.30950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.42300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.07450            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 42980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, T, P                               
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     PHE A   901                                                      
REMARK 465     ASP A   902                                                      
REMARK 465     PHE A   903                                                      
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    LEU A 871   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500     DG P 110   C3' -  O3' -  P   ANGL. DEV. =   7.3 DEGREES          
REMARK 500     DT P 113   C3' -  O3' -  P   ANGL. DEV. =  -8.2 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    SER A  44       46.21    -77.05                                   
REMARK 500    ASP A 121       40.64   -100.78                                   
REMARK 500    PHE A 221      -70.02   -126.49                                   
REMARK 500    ASN A 316       69.06   -154.07                                   
REMARK 500    ASN A 402      164.70    178.59                                   
REMARK 500    PRO A 458        1.03    -63.97                                   
REMARK 500    ASP A 579      113.36   -161.55                                   
REMARK 500    THR A 622      -70.27     70.57                                   
REMARK 500    ASP A 623       16.84   -143.25                                   
REMARK 500    GLU A 686      -70.36    -95.99                                   
REMARK 500    LYS A 800       19.49     59.52                                   
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                              CA A1006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 116   OE2                                                    
REMARK 620 2 GLU A 116   OE1  46.6                                              
REMARK 620 3 HOH A1114   O    64.2  79.6                                        
REMARK 620 4 HOH A1347   O    71.3 117.8  69.9                                  
REMARK 620 5 HOH A1368   O   141.3 158.3  88.5  73.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 411   OD1                                                    
REMARK 620 2 ASP A 411   OD2  49.4                                              
REMARK 620 3 LEU A 412   O    83.3 109.2                                        
REMARK 620 4 ASP A 623   OD1 116.4  75.3  89.0                                  
REMARK 620 5 DCP A1001   O1G  79.9 117.6  95.6 163.5                            
REMARK 620 6 DCP A1001   O2B 154.6 154.0  89.7  87.7  76.5                      
REMARK 620 7 DCP A1001   O2A 111.4  82.6 165.3  85.5  86.1  76.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 411   OD2                                                    
REMARK 620 2 ASP A 623   OD2  76.3                                              
REMARK 620 3 DCP A1001   O2A  86.4  81.6                                        
REMARK 620 4 HOH P 211   O    97.2 138.8 139.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 505   O                                                      
REMARK 620 2 ASN A 507   OD1  94.3                                              
REMARK 620 3 LYS A 531   O   166.6  84.0                                        
REMARK 620 4 HOH A1193   O    76.3 141.6  96.8                                  
REMARK 620 5 HOH A1273   O    89.0  74.5  77.8  68.2                            
REMARK 620 6 HOH A1281   O   103.6 140.5  85.7  77.5 139.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1102   O                                                      
REMARK 620 2 HOH A1144   O   107.1                                              
REMARK 620 3 HOH A1150   O   136.6  91.1                                        
REMARK 620 4 HOH A1267   O    80.1  76.1  66.2                                  
REMARK 620 5 HOH A1353   O   157.3  63.5  65.9 114.9                            
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 DCP A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1006                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4FJ5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FJ7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FJ8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FJ9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FJG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FJH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FJI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FJJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FJK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FJL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FJM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FJN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FJX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FK2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FK4   RELATED DB: PDB                                   
DBREF  4FK0 A    1   903  UNP    Q38087   DPOL_BPR69       1    903             
DBREF  4FK0 T    2    18  PDB    4FK0     4FK0             2     18             
DBREF  4FK0 P  103   115  PDB    4FK0     4FK0           103    115             
SEQADV 4FK0 ALA A  222  UNP  Q38087    ASP   222 ENGINEERED MUTATION            
SEQADV 4FK0 ALA A  327  UNP  Q38087    ASP   327 ENGINEERED MUTATION            
SEQADV 4FK0 ALA A  415  UNP  Q38087    LEU   415 ENGINEERED MUTATION            
SEQADV 4FK0 ALA A  561  UNP  Q38087    LEU   561 ENGINEERED MUTATION            
SEQADV 4FK0 GLY A  565  UNP  Q38087    SER   565 ENGINEERED MUTATION            
SEQADV 4FK0 ALA A  567  UNP  Q38087    TYR   567 ENGINEERED MUTATION            
SEQRES   1 A  903  MET LYS GLU PHE TYR LEU THR VAL GLU GLN ILE GLY ASP          
SEQRES   2 A  903  SER ILE PHE GLU ARG TYR ILE ASP SER ASN GLY ARG GLU          
SEQRES   3 A  903  ARG THR ARG GLU VAL GLU TYR LYS PRO SER LEU PHE ALA          
SEQRES   4 A  903  HIS CYS PRO GLU SER GLN ALA THR LYS TYR PHE ASP ILE          
SEQRES   5 A  903  TYR GLY LYS PRO CYS THR ARG LYS LEU PHE ALA ASN MET          
SEQRES   6 A  903  ARG ASP ALA SER GLN TRP ILE LYS ARG MET GLU ASP ILE          
SEQRES   7 A  903  GLY LEU GLU ALA LEU GLY MET ASP ASP PHE LYS LEU ALA          
SEQRES   8 A  903  TYR LEU SER ASP THR TYR ASN TYR GLU ILE LYS TYR ASP          
SEQRES   9 A  903  HIS THR LYS ILE ARG VAL ALA ASN PHE ASP ILE GLU VAL          
SEQRES  10 A  903  THR SER PRO ASP GLY PHE PRO GLU PRO SER GLN ALA LYS          
SEQRES  11 A  903  HIS PRO ILE ASP ALA ILE THR HIS TYR ASP SER ILE ASP          
SEQRES  12 A  903  ASP ARG PHE TYR VAL PHE ASP LEU LEU ASN SER PRO TYR          
SEQRES  13 A  903  GLY ASN VAL GLU GLU TRP SER ILE GLU ILE ALA ALA LYS          
SEQRES  14 A  903  LEU GLN GLU GLN GLY GLY ASP GLU VAL PRO SER GLU ILE          
SEQRES  15 A  903  ILE ASP LYS ILE ILE TYR MET PRO PHE ASP ASN GLU LYS          
SEQRES  16 A  903  GLU LEU LEU MET GLU TYR LEU ASN PHE TRP GLN GLN LYS          
SEQRES  17 A  903  THR PRO VAL ILE LEU THR GLY TRP ASN VAL GLU SER PHE          
SEQRES  18 A  903  ALA ILE PRO TYR VAL TYR ASN ARG ILE LYS ASN ILE PHE          
SEQRES  19 A  903  GLY GLU SER THR ALA LYS ARG LEU SER PRO HIS ARG LYS          
SEQRES  20 A  903  THR ARG VAL LYS VAL ILE GLU ASN MET TYR GLY SER ARG          
SEQRES  21 A  903  GLU ILE ILE THR LEU PHE GLY ILE SER VAL LEU ASP TYR          
SEQRES  22 A  903  ILE ASP LEU TYR LYS LYS PHE SER PHE THR ASN GLN PRO          
SEQRES  23 A  903  SER TYR SER LEU ASP TYR ILE SER GLU PHE GLU LEU ASN          
SEQRES  24 A  903  VAL GLY LYS LEU LYS TYR ASP GLY PRO ILE SER LYS LEU          
SEQRES  25 A  903  ARG GLU SER ASN HIS GLN ARG TYR ILE SER TYR ASN ILE          
SEQRES  26 A  903  ILE ALA VAL TYR ARG VAL LEU GLN ILE ASP ALA LYS ARG          
SEQRES  27 A  903  GLN PHE ILE ASN LEU SER LEU ASP MET GLY TYR TYR ALA          
SEQRES  28 A  903  LYS ILE GLN ILE GLN SER VAL PHE SER PRO ILE LYS THR          
SEQRES  29 A  903  TRP ASP ALA ILE ILE PHE ASN SER LEU LYS GLU GLN ASN          
SEQRES  30 A  903  LYS VAL ILE PRO GLN GLY ARG SER HIS PRO VAL GLN PRO          
SEQRES  31 A  903  TYR PRO GLY ALA PHE VAL LYS GLU PRO ILE PRO ASN ARG          
SEQRES  32 A  903  TYR LYS TYR VAL MET SER PHE ASP LEU THR SER ALA TYR          
SEQRES  33 A  903  PRO SER ILE ILE ARG GLN VAL ASN ILE SER PRO GLU THR          
SEQRES  34 A  903  ILE ALA GLY THR PHE LYS VAL ALA PRO LEU HIS ASP TYR          
SEQRES  35 A  903  ILE ASN ALA VAL ALA GLU ARG PRO SER ASP VAL TYR SER          
SEQRES  36 A  903  CYS SER PRO ASN GLY MET MET TYR TYR LYS ASP ARG ASP          
SEQRES  37 A  903  GLY VAL VAL PRO THR GLU ILE THR LYS VAL PHE ASN GLN          
SEQRES  38 A  903  ARG LYS GLU HIS LYS GLY TYR MET LEU ALA ALA GLN ARG          
SEQRES  39 A  903  ASN GLY GLU ILE ILE LYS GLU ALA LEU HIS ASN PRO ASN          
SEQRES  40 A  903  LEU SER VAL ASP GLU PRO LEU ASP VAL ASP TYR ARG PHE          
SEQRES  41 A  903  ASP PHE SER ASP GLU ILE LYS GLU LYS ILE LYS LYS LEU          
SEQRES  42 A  903  SER ALA LYS SER LEU ASN GLU MET LEU PHE ARG ALA GLN          
SEQRES  43 A  903  ARG THR GLU VAL ALA GLY MET THR ALA GLN ILE ASN ARG          
SEQRES  44 A  903  LYS ALA LEU ILE ASN GLY LEU ALA GLY ALA LEU GLY ASN          
SEQRES  45 A  903  VAL TRP PHE ARG TYR TYR ASP LEU ARG ASN ALA THR ALA          
SEQRES  46 A  903  ILE THR THR PHE GLY GLN MET ALA LEU GLN TRP ILE GLU          
SEQRES  47 A  903  ARG LYS VAL ASN GLU TYR LEU ASN GLU VAL CYS GLY THR          
SEQRES  48 A  903  GLU GLY GLU ALA PHE VAL LEU TYR GLY ASP THR ASP SER          
SEQRES  49 A  903  ILE TYR VAL SER ALA ASP LYS ILE ILE ASP LYS VAL GLY          
SEQRES  50 A  903  GLU SER LYS PHE ARG ASP THR ASN HIS TRP VAL ASP PHE          
SEQRES  51 A  903  LEU ASP LYS PHE ALA ARG GLU ARG MET GLU PRO ALA ILE          
SEQRES  52 A  903  ASP ARG GLY PHE ARG GLU MET CYS GLU TYR MET ASN ASN          
SEQRES  53 A  903  LYS GLN HIS LEU MET PHE MET ASP ARG GLU ALA ILE ALA          
SEQRES  54 A  903  GLY PRO PRO LEU GLY SER LYS GLY ILE GLY GLY PHE TRP          
SEQRES  55 A  903  THR GLY LYS LYS ARG TYR ALA LEU ASN VAL TRP ASP MET          
SEQRES  56 A  903  GLU GLY THR ARG TYR ALA GLU PRO LYS LEU LYS ILE MET          
SEQRES  57 A  903  GLY LEU GLU THR GLN LYS SER SER THR PRO LYS ALA VAL          
SEQRES  58 A  903  GLN LYS ALA LEU LYS GLU CYS ILE ARG ARG MET LEU GLN          
SEQRES  59 A  903  GLU GLY GLU GLU SER LEU GLN GLU TYR PHE LYS GLU PHE          
SEQRES  60 A  903  GLU LYS GLU PHE ARG GLN LEU ASN TYR ILE SER ILE ALA          
SEQRES  61 A  903  SER VAL SER SER ALA ASN ASN ILE ALA LYS TYR ASP VAL          
SEQRES  62 A  903  GLY GLY PHE PRO GLY PRO LYS CYS PRO PHE HIS ILE ARG          
SEQRES  63 A  903  GLY ILE LEU THR TYR ASN ARG ALA ILE LYS GLY ASN ILE          
SEQRES  64 A  903  ASP ALA PRO GLN VAL VAL GLU GLY GLU LYS VAL TYR VAL          
SEQRES  65 A  903  LEU PRO LEU ARG GLU GLY ASN PRO PHE GLY ASP LYS CYS          
SEQRES  66 A  903  ILE ALA TRP PRO SER GLY THR GLU ILE THR ASP LEU ILE          
SEQRES  67 A  903  LYS ASP ASP VAL LEU HIS TRP MET ASP TYR THR VAL LEU          
SEQRES  68 A  903  LEU GLU LYS THR PHE ILE LYS PRO LEU GLU GLY PHE THR          
SEQRES  69 A  903  SER ALA ALA LYS LEU ASP TYR GLU LYS LYS ALA SER LEU          
SEQRES  70 A  903  PHE ASP MET PHE ASP PHE                                      
SEQRES   1 T   17   DC  DG  DG  DG  DT  DA  DA  DG  DC  DA  DG  DT  DC          
SEQRES   2 T   17   DC  DG  DC  DG                                              
SEQRES   1 P   13   DG  DC  DG  DG  DA  DC  DT  DG  DC  DT  DT  DA DOC          
MODRES 4FK0 DOC P  115   DC  2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE             
HET    DOC  P 115      18                                                       
HET    DCP  A1001      28                                                       
HET     CA  A1002       1                                                       
HET     CA  A1003       1                                                       
HET     CA  A1004       1                                                       
HET     CA  A1005       1                                                       
HET     CA  A1006       1                                                       
HET     CA  T 101       1                                                       
HETNAM     DOC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE                           
HETNAM     DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE                                 
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  DOC    C9 H14 N3 O6 P                                               
FORMUL   4  DCP    C9 H16 N3 O13 P3                                             
FORMUL   5   CA    6(CA 2+)                                                     
FORMUL  11  HOH   *364(H2 O)                                                    
HELIX    1   1 ASN A   64  GLY A   79  1                                  16    
HELIX    2   2 ASP A   87  TYR A   97  1                                  11    
HELIX    3   3 ASP A  104  ILE A  108  5                                   5    
HELIX    4   4 SER A  163  LYS A  169  1                                   7    
HELIX    5   5 LEU A  170  GLY A  174  5                                   5    
HELIX    6   6 PRO A  179  ASP A  184  1                                   6    
HELIX    7   7 ASN A  193  LYS A  208  1                                  16    
HELIX    8   8 PHE A  221  GLY A  235  1                                  15    
HELIX    9   9 GLY A  235  LYS A  240  1                                   6    
HELIX   10  10 ARG A  241  SER A  243  5                                   3    
HELIX   11  11 ASP A  272  SER A  281  1                                  10    
HELIX   12  12 SER A  289  ASN A  299  1                                  11    
HELIX   13  13 PRO A  308  GLN A  339  1                                  32    
HELIX   14  14 GLN A  339  LYS A  352  1                                  14    
HELIX   15  15 GLN A  354  PHE A  359  5                                   6    
HELIX   16  16 SER A  360  GLU A  375  1                                  16    
HELIX   17  17 SER A  414  ASN A  424  1                                  11    
HELIX   18  18 PRO A  438  ASN A  444  1                                   7    
HELIX   19  19 GLY A  469  LEU A  503  1                                  35    
HELIX   20  20 SER A  523  LYS A  531  1                                   9    
HELIX   21  21 SER A  534  LEU A  570  1                                  37    
HELIX   22  22 ASP A  579  CYS A  609  1                                  31    
HELIX   23  23 ALA A  629  GLY A  637  1                                   9    
HELIX   24  24 GLU A  638  PHE A  641  5                                   4    
HELIX   25  25 ASP A  643  ARG A  658  1                                  16    
HELIX   26  26 ARG A  658  ASN A  675  1                                  18    
HELIX   27  27 LEU A  730  LYS A  734  5                                   5    
HELIX   28  28 PRO A  738  GLU A  755  1                                  18    
HELIX   29  29 GLY A  756  PHE A  771  1                                  16    
HELIX   30  30 ARG A  772  LEU A  774  5                                   3    
HELIX   31  31 ASN A  775  ALA A  780  1                                   6    
HELIX   32  32 PRO A  802  LYS A  816  1                                  15    
HELIX   33  33 THR A  855  MET A  866  1                                  12    
HELIX   34  34 ASP A  867  PHE A  876  1                                  10    
HELIX   35  35 PHE A  876  ALA A  887  1                                  12    
HELIX   36  36 SER A  896  MET A  900  5                                   5    
SHEET    1   A 3 PHE A   4  ILE A  11  0                                        
SHEET    2   A 3 SER A  14  ILE A  20 -1  O  ARG A  18   N  LEU A   6           
SHEET    3   A 3 GLU A  26  VAL A  31 -1  O  VAL A  31   N  ILE A  15           
SHEET    1   B 4 SER A  36  HIS A  40  0                                        
SHEET    2   B 4 PRO A  56  LEU A  61 -1  O  LYS A  60   N  LEU A  37           
SHEET    3   B 4 TYR A  49  ASP A  51 -1  N  TYR A  49   O  CYS A  57           
SHEET    4   B 4 LYS A 378  VAL A 379  1  O  VAL A 379   N  PHE A  50           
SHEET    1   C 6 ILE A 186  PHE A 191  0                                        
SHEET    2   C 6 ARG A 145  LEU A 151  1  N  ASP A 150   O  PHE A 191           
SHEET    3   C 6 ILE A 133  ASP A 140 -1  N  ILE A 136   O  PHE A 149           
SHEET    4   C 6 VAL A 110  VAL A 117 -1  N  ASN A 112   O  TYR A 139           
SHEET    5   C 6 ILE A 212  THR A 214  1  O  ILE A 212   N  ALA A 111           
SHEET    6   C 6 SER A 269  VAL A 270  1  O  SER A 269   N  LEU A 213           
SHEET    1   D 2 ASN A 153  SER A 154  0                                        
SHEET    2   D 2 GLY A 157  ASN A 158 -1  O  GLY A 157   N  SER A 154           
SHEET    1   E 2 THR A 248  GLU A 254  0                                        
SHEET    2   E 2 SER A 259  LEU A 265 -1  O  ILE A 262   N  LYS A 251           
SHEET    1   F 7 ASN A 402  ARG A 403  0                                        
SHEET    2   F 7 GLY A 700  GLY A 704 -1  O  TRP A 702   N  ASN A 402           
SHEET    3   F 7 ARG A 707  MET A 715 -1  O  ALA A 709   N  PHE A 701           
SHEET    4   F 7 MET A 683  ALA A 689 -1  N  ILE A 688   O  TRP A 713           
SHEET    5   F 7 VAL A 407  LEU A 412 -1  N  SER A 409   O  GLU A 686           
SHEET    6   F 7 SER A 624  SER A 628 -1  O  VAL A 627   N  MET A 408           
SHEET    7   F 7 VAL A 617  TYR A 619 -1  N  LEU A 618   O  TYR A 626           
SHEET    1   G 4 ASN A 402  ARG A 403  0                                        
SHEET    2   G 4 GLY A 700  GLY A 704 -1  O  TRP A 702   N  ASN A 402           
SHEET    3   G 4 ARG A 707  MET A 715 -1  O  ALA A 709   N  PHE A 701           
SHEET    4   G 4 THR A 718  MET A 728 -1  O  MET A 728   N  TYR A 708           
SHEET    1   H 3 ILE A 430  THR A 433  0                                        
SHEET    2   H 3 MET A 461  TYR A 463 -1  O  MET A 462   N  ALA A 431           
SHEET    3   H 3 SER A 455  SER A 457 -1  N  SER A 455   O  TYR A 463           
SHEET    1   I 3 SER A 781  SER A 784  0                                        
SHEET    2   I 3 LYS A 829  PRO A 834 -1  O  VAL A 830   N  SER A 783           
SHEET    3   I 3 CYS A 845  PRO A 849 -1  O  TRP A 848   N  TYR A 831           
SHEET    1   J 2 ASP A 792  VAL A 793  0                                        
SHEET    2   J 2 PHE A 796  PRO A 797 -1  O  PHE A 796   N  VAL A 793           
LINK         O3'  DA P 114                 P   DOC P 115     1555   1555  1.59  
LINK         OE2 GLU A 116                CA    CA A1006     1555   1555  2.70  
LINK         OE1 GLU A 116                CA    CA A1006     1555   1555  2.80  
LINK         OD1 ASP A 411                CA    CA A1002     1555   1555  2.32  
LINK         OD2 ASP A 411                CA    CA A1002     1555   1555  2.80  
LINK         OD2 ASP A 411                CA    CA A1003     1555   1555  2.18  
LINK         O   LEU A 412                CA    CA A1002     1555   1555  2.24  
LINK         O   ASN A 505                CA    CA A1004     1555   1555  2.35  
LINK         OD1 ASN A 507                CA    CA A1004     1555   1555  2.27  
LINK         O   LYS A 531                CA    CA A1004     1555   1555  2.17  
LINK         OD1 ASP A 623                CA    CA A1002     1555   1555  2.31  
LINK         OD2 ASP A 623                CA    CA A1003     1555   1555  2.81  
LINK         O1G DCP A1001                CA    CA A1002     1555   1555  2.19  
LINK         O2B DCP A1001                CA    CA A1002     1555   1555  2.26  
LINK         O2A DCP A1001                CA    CA A1002     1555   1555  2.35  
LINK         O2A DCP A1001                CA    CA A1003     1555   1555  2.77  
LINK        CA    CA A1003                 O   HOH P 211     1555   1555  2.50  
LINK        CA    CA A1004                 O   HOH A1193     1555   1555  2.48  
LINK        CA    CA A1004                 O   HOH A1273     1555   1555  2.65  
LINK        CA    CA A1004                 O   HOH A1281     1555   1555  1.97  
LINK        CA    CA A1005                 O   HOH A1102     1555   1555  2.84  
LINK        CA    CA A1005                 O   HOH A1144     1555   1555  2.99  
LINK        CA    CA A1005                 O   HOH A1150     1555   1555  2.97  
LINK        CA    CA A1005                 O   HOH A1267     1555   1555  2.62  
LINK        CA    CA A1005                 O   HOH A1353     1555   1555  2.32  
LINK        CA    CA A1006                 O   HOH A1114     1555   1555  2.63  
LINK        CA    CA A1006                 O   HOH A1347     1555   1555  2.31  
LINK        CA    CA A1006                 O   HOH A1368     1555   1555  2.39  
SITE     1 AC1 19 ASP A 411  LEU A 412  THR A 413  SER A 414                    
SITE     2 AC1 19 ALA A 415  TYR A 416  ARG A 482  LYS A 560                    
SITE     3 AC1 19 ASN A 564  THR A 622  ASP A 623   CA A1002                    
SITE     4 AC1 19  CA A1003  HOH A1102  HOH A1115  HOH A1165                    
SITE     5 AC1 19 DOC P 115   DG T   4   DG T   5                               
SITE     1 AC2  4 ASP A 411  LEU A 412  ASP A 623  DCP A1001                    
SITE     1 AC3  4 ASP A 411  ASP A 623  DCP A1001  HOH P 211                    
SITE     1 AC4  6 ASN A 505  ASN A 507  LYS A 531  HOH A1193                    
SITE     2 AC4  6 HOH A1273  HOH A1281                                          
SITE     1 AC5  6 GLU A 716  HOH A1102  HOH A1144  HOH A1150                    
SITE     2 AC5  6 HOH A1267  HOH A1353                                          
SITE     1 AC6  4 GLU A 116  HOH A1114  HOH A1347  HOH A1368                    
CRYST1   74.846  120.149  130.619  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013361  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008323  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007656        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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