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Database: PDB
Entry: 1X9N
LinkDB: 1X9N
Original site: 1X9N 
HEADER    LIGASE/DNA                              23-AUG-04   1X9N              
TITLE     CRYSTAL STRUCTURE OF HUMAN DNA LIGASE I BOUND TO 5'-ADENYLATED, NICKED
TITLE    2 DNA                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIDEOXY TERMINATED DNA;                                    
COMPND   3 CHAIN: B;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: 5'-PHOSPHORYLATED DNA;                                     
COMPND   7 CHAIN: C;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: TEMPLATE DNA;                                              
COMPND  11 CHAIN: D;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: DNA LIGASE I;                                              
COMPND  15 CHAIN: A;                                                            
COMPND  16 SYNONYM: POLYDEOXYRIBONUCLEOTIDE SYNTHASE [ATP];                     
COMPND  17 EC: 6.5.1.1;                                                         
COMPND  18 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 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 GENE: LIG1;                                                          
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RP;                               
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PET24A                                    
KEYWDS    DNA LIGASE, 5'-ADENYLATED NICKED DNA, PROTEIN-DNA COMPLEX, LIGASE-DNA 
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.PASCAL,P.J.O'BRIEN,A.E.TOMKINSON,T.ELLENBERGER                    
REVDAT   3   13-JUL-11 1X9N    1       VERSN                                    
REVDAT   2   24-FEB-09 1X9N    1       VERSN                                    
REVDAT   1   30-NOV-04 1X9N    0                                                
JRNL        AUTH   J.M.PASCAL,P.J.O'BRIEN,A.E.TOMKINSON,T.ELLENBERGER           
JRNL        TITL   HUMAN DNA LIGASE I COMPLETELY ENCIRCLES AND PARTIALLY        
JRNL        TITL 2 UNWINDS NICKED DNA.                                          
JRNL        REF    NATURE                        V. 432   473 2004              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   15565146                                                     
JRNL        DOI    10.1038/NATURE03082                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.80                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 50.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 24943                          
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) : 0.236                           
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1301                            
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) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1811                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 103                          
REMARK   3   BIN FREE R VALUE                    : 0.4130                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4894                                    
REMARK   3   NUCLEIC ACID ATOMS       : 813                                     
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
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) : 41.59                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.65000                                             
REMARK   3    B22 (A**2) : -3.65000                                             
REMARK   3    B33 (A**2) : 5.47000                                              
REMARK   3    B12 (A**2) : -1.82000                                             
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): 1.209         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.394         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.311         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.766        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.909                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5929 ; 0.012 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8207 ; 1.524 ; 2.158       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   630 ; 6.603 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   890 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4186 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2408 ; 0.254 ; 0.200       
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):    26 ; 0.316 ; 0.200       
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):  3155 ; 0.458 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5078 ; 0.938 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2773 ; 1.587 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3126 ; 2.597 ; 4.500       
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  : 4                                          
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   262        A   535                          
REMARK   3    ORIGIN FOR THE GROUP (A):  53.8081  32.5779  64.4371              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3602 T22:   0.2820                                     
REMARK   3      T33:   0.5749 T12:   0.0338                                     
REMARK   3      T13:  -0.1933 T23:   0.3443                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9895 L22:   2.0743                                     
REMARK   3      L33:   2.2156 L12:   1.4420                                     
REMARK   3      L13:   0.0323 L23:   1.0091                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0941 S12:  -0.1954 S13:  -0.1516                       
REMARK   3      S21:   0.0904 S22:   0.1135 S23:   0.4208                       
REMARK   3      S31:   0.1322 S32:  -0.0302 S33:  -0.2076                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   536        A   747                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.2927  40.7568  30.3652              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6517 T22:   0.7693                                     
REMARK   3      T33:   0.4864 T12:   0.0041                                     
REMARK   3      T13:  -0.2627 T23:   0.0649                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5908 L22:   2.2446                                     
REMARK   3      L33:   0.9556 L12:   0.1867                                     
REMARK   3      L13:   0.0622 L23:  -0.6667                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1689 S12:   0.6150 S13:  -0.0202                       
REMARK   3      S21:  -0.3274 S22:   0.0148 S23:   0.3758                       
REMARK   3      S31:  -0.1052 S32:  -0.2482 S33:  -0.1837                       
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   748        A   901                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.3422  43.8775  40.3222              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4315 T22:   0.4872                                     
REMARK   3      T33:   0.8080 T12:   0.0622                                     
REMARK   3      T13:  -0.3477 T23:   0.2832                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6181 L22:   3.7920                                     
REMARK   3      L33:   4.3194 L12:   0.1438                                     
REMARK   3      L13:   0.4227 L23:   0.4706                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0178 S12:   0.2943 S13:  -0.0817                       
REMARK   3      S21:  -0.2877 S22:   0.0655 S23:   0.3420                       
REMARK   3      S31:  -0.3951 S32:  -0.3272 S33:  -0.0833                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     3        B    13                          
REMARK   3    RESIDUE RANGE :   C     1        C     9                          
REMARK   3    RESIDUE RANGE :   D     7        D    26                          
REMARK   3    RESIDUE RANGE :   C   100        C   100                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.7841  35.3336  45.9060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4026 T22:   0.2969                                     
REMARK   3      T33:   0.7884 T12:  -0.0538                                     
REMARK   3      T13:  -0.3157 T23:   0.1994                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5830 L22:   0.8286                                     
REMARK   3      L33:   3.5126 L12:  -0.5190                                     
REMARK   3      L13:  -0.7111 L23:  -0.1536                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0363 S12:   0.2699 S13:  -0.2147                       
REMARK   3      S21:  -0.3180 S22:   0.1497 S23:   0.1582                       
REMARK   3      S31:  -0.0001 S32:  -0.1064 S33:  -0.1135                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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: NULL                                      
REMARK   4                                                                      
REMARK   4 1X9N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-AUG-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030113.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-OCT-03; NULL; NULL              
REMARK 200  TEMPERATURE           (KELVIN) : 100; NULL; NULL                    
REMARK 200  PH                             : 4.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y; Y                            
REMARK 200  RADIATION SOURCE               : NSLS; NSLS; NSLS                   
REMARK 200  BEAMLINE                       : X25; X25; X12C                     
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL; NULL                   
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL; NULL                      
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97880; 0.9787, 0.9791, 0.9635,   
REMARK 200                                   1.1; 1.006, 1.011, 0.969, 1.1      
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200                                   SI(111) OR (220); NULL; NULL       
REMARK 200  OPTICS                         : NULL; NULL; NULL                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; NULL; NULL                    
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4; NULL; NULL         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : ACE                                
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26365                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 10.000                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.48000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD; NULL; NULL                                
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM ACETATE, PH 4.8,        
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298.0K                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       44.22750            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       44.22750            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       44.22750            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D, A                            
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      DG B     1                                                      
REMARK 465      DT B     2                                                      
REMARK 465      DA C    10                                                      
REMARK 465      DT C    11                                                      
REMARK 465      DT C    12                                                      
REMARK 465      DC C    13                                                      
REMARK 465      DG C    14                                                      
REMARK 465      DG C    15                                                      
REMARK 465      DC D     1                                                      
REMARK 465      DC D     2                                                      
REMARK 465      DG D     3                                                      
REMARK 465      DA D     4                                                      
REMARK 465      DA D     5                                                      
REMARK 465      DT D     6                                                      
REMARK 465      DA D    27                                                      
REMARK 465      DC D    28                                                      
REMARK 465     MET A   232                                                      
REMARK 465     THR A   233                                                      
REMARK 465     PRO A   234                                                      
REMARK 465     ARG A   235                                                      
REMARK 465     LYS A   236                                                      
REMARK 465     PRO A   237                                                      
REMARK 465     ALA A   238                                                      
REMARK 465     VAL A   239                                                      
REMARK 465     LYS A   240                                                      
REMARK 465     LYS A   241                                                      
REMARK 465     GLU A   242                                                      
REMARK 465     VAL A   243                                                      
REMARK 465     LYS A   244                                                      
REMARK 465     GLU A   245                                                      
REMARK 465     GLU A   246                                                      
REMARK 465     GLU A   247                                                      
REMARK 465     PRO A   248                                                      
REMARK 465     GLY A   249                                                      
REMARK 465     ALA A   250                                                      
REMARK 465     PRO A   251                                                      
REMARK 465     GLY A   252                                                      
REMARK 465     LYS A   253                                                      
REMARK 465     GLU A   254                                                      
REMARK 465     GLY A   255                                                      
REMARK 465     ALA A   256                                                      
REMARK 465     ALA A   257                                                      
REMARK 465     GLU A   258                                                      
REMARK 465     GLY A   259                                                      
REMARK 465     PRO A   260                                                      
REMARK 465     LEU A   261                                                      
REMARK 465     ASN A   385                                                      
REMARK 465     SER A   386                                                      
REMARK 465     ARG A   387                                                      
REMARK 465     SER A   388                                                      
REMARK 465     THR A   389                                                      
REMARK 465     GLN A   390                                                      
REMARK 465     ARG A   391                                                      
REMARK 465     LEU A   392                                                      
REMARK 465     GLN A   902                                                      
REMARK 465     ILE A   903                                                      
REMARK 465     GLN A   904                                                      
REMARK 465     ASN A   905                                                      
REMARK 465     GLN A   906                                                      
REMARK 465     GLN A   907                                                      
REMARK 465     GLY A   908                                                      
REMARK 465     GLU A   909                                                      
REMARK 465     ASP A   910                                                      
REMARK 465     SER A   911                                                      
REMARK 465     GLY A   912                                                      
REMARK 465     SER A   913                                                      
REMARK 465     ASP A   914                                                      
REMARK 465     PRO A   915                                                      
REMARK 465     GLU A   916                                                      
REMARK 465     ASP A   917                                                      
REMARK 465     THR A   918                                                      
REMARK 465     TYR A   919                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470      DG B   3    P    OP1  OP2                                       
REMARK 470      DC D   7    P    OP1  OP2                                       
REMARK 470     ARG A 627    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 628    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 643    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 644    CG   CD   CE   NZ                                   
REMARK 470     GLU A 645    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 646    CG1  CG2                                            
REMARK 470     GLU A 709    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 712    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 807    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 859    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 899    CG   CD   CE   NZ                                   
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     DG B  11   O3'    DG B  11   C3'    -0.037                       
REMARK 500     DG C   1   O3'    DG C   1   C3'    -0.075                       
REMARK 500     DT C   2   O3'    DT C   2   C3'    -0.042                       
REMARK 500     DC C   3   O3'    DC C   3   C3'    -0.056                       
REMARK 500     DG C   4   O3'    DG C   4   C3'    -0.052                       
REMARK 500     DC C   7   O3'    DC C   7   C3'    -0.037                       
REMARK 500     DG D  16   O3'    DG D  16   C3'    -0.049                       
REMARK 500     DA D  17   O3'    DA D  17   C3'    -0.036                       
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     DG B   6   O4' -  C1' -  N9  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DT B   8   C5' -  C4' -  O4' ANGL. DEV. =  10.2 DEGREES          
REMARK 500     DT B   8   O4' -  C1' -  N1  ANGL. DEV. =  12.9 DEGREES          
REMARK 500     DC B  10   C3' -  C2' -  C1' ANGL. DEV. =  -4.8 DEGREES          
REMARK 500     DC B  10   O4' -  C1' -  N1  ANGL. DEV. =   4.0 DEGREES          
REMARK 500     DG B   9   C3' -  O3' -  P   ANGL. DEV. =   8.0 DEGREES          
REMARK 500     DT B  12   O4' -  C4' -  C3' ANGL. DEV. =  -3.1 DEGREES          
REMARK 500     DT B  12   O4' -  C1' -  N1  ANGL. DEV. =   2.6 DEGREES          
REMARK 500     DT C   2   O4' -  C1' -  C2' ANGL. DEV. =   3.2 DEGREES          
REMARK 500     DT C   2   C4  -  C5  -  C7  ANGL. DEV. =   3.7 DEGREES          
REMARK 500     DT C   2   C6  -  C5  -  C7  ANGL. DEV. =  -4.3 DEGREES          
REMARK 500     DA C   6   O5' -  C5' -  C4' ANGL. DEV. =  -5.3 DEGREES          
REMARK 500     DT C   8   O4' -  C4' -  C3' ANGL. DEV. =  -2.5 DEGREES          
REMARK 500     DG C   9   O4' -  C4' -  C3' ANGL. DEV. =  -2.4 DEGREES          
REMARK 500     DC D   7   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DT D  10   C4' -  C3' -  C2' ANGL. DEV. =  -4.3 DEGREES          
REMARK 500     DC D  11   O4' -  C1' -  N1  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500     DC D  12   N1  -  C2  -  O2  ANGL. DEV. =   4.1 DEGREES          
REMARK 500     DC D  11   C3' -  O3' -  P   ANGL. DEV. =   8.4 DEGREES          
REMARK 500     DG D  13   C3' -  C2' -  C1' ANGL. DEV. =  -5.4 DEGREES          
REMARK 500     DG D  13   O4' -  C1' -  N9  ANGL. DEV. =   4.8 DEGREES          
REMARK 500     DA D  14   O4' -  C1' -  N9  ANGL. DEV. =   3.4 DEGREES          
REMARK 500     DC D  15   O4' -  C4' -  C3' ANGL. DEV. =  -3.8 DEGREES          
REMARK 500     DC D  15   N1  -  C2  -  O2  ANGL. DEV. =   3.7 DEGREES          
REMARK 500     DG D  16   O4' -  C4' -  C3' ANGL. DEV. =  -4.0 DEGREES          
REMARK 500     DA D  17   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DC D  18   P   -  O5' -  C5' ANGL. DEV. = -12.4 DEGREES          
REMARK 500     DC D  18   O4' -  C4' -  C3' ANGL. DEV. =   4.3 DEGREES          
REMARK 500     DA D  21   O4' -  C1' -  N9  ANGL. DEV. =  -5.4 DEGREES          
REMARK 500     DT D  22   C3' -  C2' -  C1' ANGL. DEV. =  -6.3 DEGREES          
REMARK 500     DT D  22   O4' -  C1' -  N1  ANGL. DEV. =   3.5 DEGREES          
REMARK 500     DC D  23   C3' -  C2' -  C1' ANGL. DEV. =  -6.8 DEGREES          
REMARK 500     DA D  24   O4' -  C1' -  N9  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500     DC D  26   O4' -  C1' -  N1  ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ASP A 278   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A 326   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 748   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A 784   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A 802   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A 881   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 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    PRO A 268        8.85    -68.59                                   
REMARK 500    SER A 323       55.71   -159.04                                   
REMARK 500    LEU A 366      -39.12    -39.69                                   
REMARK 500    PRO A 396      173.35    -54.31                                   
REMARK 500    LEU A 414       92.59    -65.03                                   
REMARK 500    HIS A 436     -109.84   -129.90                                   
REMARK 500    SER A 447       -6.96    -55.72                                   
REMARK 500    ALA A 455     -149.83   -126.09                                   
REMARK 500    ALA A 461      -58.55    -26.85                                   
REMARK 500    ASP A 512       99.16   -160.86                                   
REMARK 500    PHE A 558       32.86    -97.69                                   
REMARK 500    SER A 615      146.48   -171.85                                   
REMARK 500    GLU A 628      -72.06    -81.52                                   
REMARK 500    LYS A 630       72.84     63.31                                   
REMARK 500    LYS A 644      -81.62    -68.21                                   
REMARK 500    VAL A 646       55.21   -102.08                                   
REMARK 500    PHE A 660       -4.79   -156.39                                   
REMARK 500    GLU A 692      -73.79   -110.36                                   
REMARK 500    SER A 718       74.69     57.01                                   
REMARK 500    ARG A 738      100.98   -168.30                                   
REMARK 500    LYS A 747      -57.67    -25.96                                   
REMARK 500    ASP A 748      -86.89     -8.00                                   
REMARK 500    ASP A 751      -71.36    -60.92                                   
REMARK 500    VAL A 753      107.82   -176.37                                   
REMARK 500    ARG A 774     -159.73   -124.38                                   
REMARK 500    SER A 839      -41.28   -158.38                                   
REMARK 500    ASP A 848     -168.96   -163.36                                   
REMARK 500    ALA A 857      125.90    -38.42                                   
REMARK 500    ILE A 876      -55.05   -125.71                                   
REMARK 500    GLN A 886       33.17    -94.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP C 100                 
DBREF  1X9N A  233   919  UNP    P18858   DNL1_HUMAN     233    919             
DBREF  1X9N B    1    13  PDB    1X9N     1X9N             1     13             
DBREF  1X9N C    1    15  PDB    1X9N     1X9N             1     15             
DBREF  1X9N D    1    28  PDB    1X9N     1X9N             1     28             
SEQADV 1X9N MET A  232  UNP  P18858              INITIATING METHIONINE          
SEQADV 1X9N MSE A  308  UNP  P18858    MET   308 MODIFIED RESIDUE               
SEQADV 1X9N MSE A  393  UNP  P18858    MET   393 MODIFIED RESIDUE               
SEQADV 1X9N MSE A  480  UNP  P18858    MET   480 MODIFIED RESIDUE               
SEQADV 1X9N MSE A  501  UNP  P18858    MET   501 MODIFIED RESIDUE               
SEQADV 1X9N MSE A  543  UNP  P18858    MET   543 MODIFIED RESIDUE               
SEQADV 1X9N MSE A  723  UNP  P18858    MET   723 MODIFIED RESIDUE               
SEQRES   1 B   13   DG  DT  DG  DC  DT  DG  DA  DT  DG  DC  DG  DT DOC          
SEQRES   1 C   15   DG  DT  DC  DG  DG  DA  DC  DT  DG  DA  DT  DT  DC          
SEQRES   2 C   15   DG  DG                                                      
SEQRES   1 D   28   DC  DC  DG  DA  DA  DT  DC  DA  DG  DT  DC  DC  DG          
SEQRES   2 D   28   DA  DC  DG  DA  DC  DG  DC  DA  DT  DC  DA  DG  DC          
SEQRES   3 D   28   DA  DC                                                      
SEQRES   1 A  688  MET THR PRO ARG LYS PRO ALA VAL LYS LYS GLU VAL LYS          
SEQRES   2 A  688  GLU GLU GLU PRO GLY ALA PRO GLY LYS GLU GLY ALA ALA          
SEQRES   3 A  688  GLU GLY PRO LEU ASP PRO SER GLY TYR ASN PRO ALA LYS          
SEQRES   4 A  688  ASN ASN TYR HIS PRO VAL GLU ASP ALA CYS TRP LYS PRO          
SEQRES   5 A  688  GLY GLN LYS VAL PRO TYR LEU ALA VAL ALA ARG THR PHE          
SEQRES   6 A  688  GLU LYS ILE GLU GLU VAL SER ALA ARG LEU ARG MSE VAL          
SEQRES   7 A  688  GLU THR LEU SER ASN LEU LEU ARG SER VAL VAL ALA LEU          
SEQRES   8 A  688  SER PRO PRO ASP LEU LEU PRO VAL LEU TYR LEU SER LEU          
SEQRES   9 A  688  ASN HIS LEU GLY PRO PRO GLN GLN GLY LEU GLU LEU GLY          
SEQRES  10 A  688  VAL GLY ASP GLY VAL LEU LEU LYS ALA VAL ALA GLN ALA          
SEQRES  11 A  688  THR GLY ARG GLN LEU GLU SER VAL ARG ALA GLU ALA ALA          
SEQRES  12 A  688  GLU LYS GLY ASP VAL GLY LEU VAL ALA GLU ASN SER ARG          
SEQRES  13 A  688  SER THR GLN ARG LEU MSE LEU PRO PRO PRO PRO LEU THR          
SEQRES  14 A  688  ALA SER GLY VAL PHE SER LYS PHE ARG ASP ILE ALA ARG          
SEQRES  15 A  688  LEU THR GLY SER ALA SER THR ALA LYS LYS ILE ASP ILE          
SEQRES  16 A  688  ILE LYS GLY LEU PHE VAL ALA CYS ARG HIS SER GLU ALA          
SEQRES  17 A  688  ARG PHE ILE ALA ARG SER LEU SER GLY ARG LEU ARG LEU          
SEQRES  18 A  688  GLY LEU ALA GLU GLN SER VAL LEU ALA ALA LEU SER GLN          
SEQRES  19 A  688  ALA VAL SER LEU THR PRO PRO GLY GLN GLU PHE PRO PRO          
SEQRES  20 A  688  ALA MSE VAL ASP ALA GLY LYS GLY LYS THR ALA GLU ALA          
SEQRES  21 A  688  ARG LYS THR TRP LEU GLU GLU GLN GLY MSE ILE LEU LYS          
SEQRES  22 A  688  GLN THR PHE CYS GLU VAL PRO ASP LEU ASP ARG ILE ILE          
SEQRES  23 A  688  PRO VAL LEU LEU GLU HIS GLY LEU GLU ARG LEU PRO GLU          
SEQRES  24 A  688  HIS CYS LYS LEU SER PRO GLY ILE PRO LEU LYS PRO MSE          
SEQRES  25 A  688  LEU ALA HIS PRO THR ARG GLY ILE SER GLU VAL LEU LYS          
SEQRES  26 A  688  ARG PHE GLU GLU ALA ALA PHE THR CYS GLU TYR LYS TYR          
SEQRES  27 A  688  ASP GLY GLN ARG ALA GLN ILE HIS ALA LEU GLU GLY GLY          
SEQRES  28 A  688  GLU VAL LYS ILE PHE SER ARG ASN GLN GLU ASP ASN THR          
SEQRES  29 A  688  GLY LYS TYR PRO ASP ILE ILE SER ARG ILE PRO LYS ILE          
SEQRES  30 A  688  LYS LEU PRO SER VAL THR SER PHE ILE LEU ASP THR GLU          
SEQRES  31 A  688  ALA VAL ALA TRP ASP ARG GLU LYS LYS GLN ILE GLN PRO          
SEQRES  32 A  688  PHE GLN VAL LEU THR THR ARG LYS ARG LYS GLU VAL ASP          
SEQRES  33 A  688  ALA SER GLU ILE GLN VAL GLN VAL CYS LEU TYR ALA PHE          
SEQRES  34 A  688  ASP LEU ILE TYR LEU ASN GLY GLU SER LEU VAL ARG GLU          
SEQRES  35 A  688  PRO LEU SER ARG ARG ARG GLN LEU LEU ARG GLU ASN PHE          
SEQRES  36 A  688  VAL GLU THR GLU GLY GLU PHE VAL PHE ALA THR SER LEU          
SEQRES  37 A  688  ASP THR LYS ASP ILE GLU GLN ILE ALA GLU PHE LEU GLU          
SEQRES  38 A  688  GLN SER VAL LYS ASP SER CYS GLU GLY LEU MSE VAL LYS          
SEQRES  39 A  688  THR LEU ASP VAL ASP ALA THR TYR GLU ILE ALA LYS ARG          
SEQRES  40 A  688  SER HIS ASN TRP LEU LYS LEU LYS LYS ASP TYR LEU ASP          
SEQRES  41 A  688  GLY VAL GLY ASP THR LEU ASP LEU VAL VAL ILE GLY ALA          
SEQRES  42 A  688  TYR LEU GLY ARG GLY LYS ARG ALA GLY ARG TYR GLY GLY          
SEQRES  43 A  688  PHE LEU LEU ALA SER TYR ASP GLU ASP SER GLU GLU LEU          
SEQRES  44 A  688  GLN ALA ILE CYS LYS LEU GLY THR GLY PHE SER ASP GLU          
SEQRES  45 A  688  GLU LEU GLU GLU HIS HIS GLN SER LEU LYS ALA LEU VAL          
SEQRES  46 A  688  LEU PRO SER PRO ARG PRO TYR VAL ARG ILE ASP GLY ALA          
SEQRES  47 A  688  VAL ILE PRO ASP HIS TRP LEU ASP PRO SER ALA VAL TRP          
SEQRES  48 A  688  GLU VAL LYS CYS ALA ASP LEU SER LEU SER PRO ILE TYR          
SEQRES  49 A  688  PRO ALA ALA ARG GLY LEU VAL ASP SER ASP LYS GLY ILE          
SEQRES  50 A  688  SER LEU ARG PHE PRO ARG PHE ILE ARG VAL ARG GLU ASP          
SEQRES  51 A  688  LYS GLN PRO GLU GLN ALA THR THR SER ALA GLN VAL ALA          
SEQRES  52 A  688  CYS LEU TYR ARG LYS GLN SER GLN ILE GLN ASN GLN GLN          
SEQRES  53 A  688  GLY GLU ASP SER GLY SER ASP PRO GLU ASP THR TYR              
MODRES 1X9N DOC B   13   DC  2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE             
MODRES 1X9N MSE A  308  MET  SELENOMETHIONINE                                   
MODRES 1X9N MSE A  393  MET  SELENOMETHIONINE                                   
MODRES 1X9N MSE A  480  MET  SELENOMETHIONINE                                   
MODRES 1X9N MSE A  501  MET  SELENOMETHIONINE                                   
MODRES 1X9N MSE A  543  MET  SELENOMETHIONINE                                   
MODRES 1X9N MSE A  723  MET  SELENOMETHIONINE                                   
HET    DOC  B  13      18                                                       
HET    MSE  A 308       8                                                       
HET    MSE  A 393       8                                                       
HET    MSE  A 480       8                                                       
HET    MSE  A 501       8                                                       
HET    MSE  A 543       8                                                       
HET    MSE  A 723       8                                                       
HET    AMP  C 100      23                                                       
HETNAM     DOC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE                           
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
FORMUL   1  DOC    C9 H14 N3 O6 P                                               
FORMUL   4  MSE    6(C5 H11 N O2 SE)                                            
FORMUL   5  AMP    C10 H14 N5 O7 P                                              
HELIX    1   1 ASP A  262  TYR A  266  5                                   5    
HELIX    2   2 HIS A  274  ALA A  279  1                                   6    
HELIX    3   3 PRO A  288  GLU A  301  1                                  14    
HELIX    4   4 ALA A  304  SER A  323  1                                  20    
HELIX    5   5 ASP A  326  ASN A  336  1                                  11    
HELIX    6   6 PRO A  340  GLY A  344  5                                   5    
HELIX    7   7 GLY A  350  GLY A  363  1                                  14    
HELIX    8   8 GLN A  365  GLY A  377  1                                  13    
HELIX    9   9 ASP A  378  ALA A  383  1                                   6    
HELIX   10  10 THR A  400  LEU A  414  1                                  15    
HELIX   11  11 ALA A  418  CYS A  434  1                                  17    
HELIX   12  12 SER A  437  SER A  447  1                                  11    
HELIX   13  13 ALA A  455  THR A  470  1                                  16    
HELIX   14  14 THR A  488  VAL A  510  1                                  23    
HELIX   15  15 ASP A  512  LEU A  528  1                                  17    
HELIX   16  16 PRO A  529  CYS A  532  5                                   4    
HELIX   17  17 GLY A  550  PHE A  558  1                                   9    
HELIX   18  18 TYR A  598  ARG A  604  1                                   7    
HELIX   19  19 ILE A  605  LYS A  609  5                                   5    
HELIX   20  20 PRO A  634  THR A  639  1                                   6    
HELIX   21  21 ASP A  647  ILE A  651  5                                   5    
HELIX   22  22 PRO A  674  PHE A  686  1                                  13    
HELIX   23  23 ASP A  703  ASP A  717  1                                  15    
HELIX   24  24 LYS A  747  GLY A  752  1                                   6    
HELIX   25  25 SER A  801  LEU A  815  1                                  15    
HELIX   26  26 GLN A  883  ALA A  887  5                                   5    
HELIX   27  27 THR A  889  SER A  901  1                                  13    
SHEET    1   A 5 LEU A 544  THR A 548  0                                        
SHEET    2   A 5 HIS A 740  LYS A 746  1  O  TRP A 742   N  HIS A 546           
SHEET    3   A 5 CYS A 719  THR A 726 -1  N  LEU A 722   O  LEU A 745           
SHEET    4   A 5 PHE A 563  TYR A 569 -1  N  LYS A 568   O  GLY A 721           
SHEET    5   A 5 SER A 698  LEU A 699 -1  O  LEU A 699   N  CYS A 565           
SHEET    1   B 5 VAL A 584  PHE A 587  0                                        
SHEET    2   B 5 GLN A 572  ALA A 578 -1  N  GLN A 575   O  PHE A 587           
SHEET    3   B 5 PHE A 616  TRP A 625 -1  O  THR A 620   N  ALA A 574           
SHEET    4   B 5 GLN A 654  LEU A 665 -1  O  CYS A 656   N  VAL A 623           
SHEET    5   B 5 GLU A 668  SER A 669 -1  O  GLU A 668   N  LEU A 665           
SHEET    1   C 5 VAL A 584  PHE A 587  0                                        
SHEET    2   C 5 GLN A 572  ALA A 578 -1  N  GLN A 575   O  PHE A 587           
SHEET    3   C 5 PHE A 616  TRP A 625 -1  O  THR A 620   N  ALA A 574           
SHEET    4   C 5 GLN A 654  LEU A 665 -1  O  CYS A 656   N  VAL A 623           
SHEET    5   C 5 PHE A 693  PHE A 695  1  O  VAL A 694   N  LEU A 657           
SHEET    1   D 6 VAL A 816  LEU A 817  0                                        
SHEET    2   D 6 HIS A 834  LEU A 836 -1  O  TRP A 835   N  LEU A 817           
SHEET    3   D 6 ASP A 755  LEU A 766 -1  N  ILE A 762   O  LEU A 836           
SHEET    4   D 6 TYR A 775  ASP A 784 -1  O  LEU A 779   N  ILE A 762           
SHEET    5   D 6 GLU A 789  LEU A 796 -1  O  ILE A 793   N  LEU A 780           
SHEET    6   D 6 VAL A 824  ARG A 825  1  O  ARG A 825   N  ALA A 792           
SHEET    1   E 5 VAL A 816  LEU A 817  0                                        
SHEET    2   E 5 HIS A 834  LEU A 836 -1  O  TRP A 835   N  LEU A 817           
SHEET    3   E 5 ASP A 755  LEU A 766 -1  N  ILE A 762   O  LEU A 836           
SHEET    4   E 5 VAL A 841  CYS A 846 -1  O  VAL A 844   N  LEU A 757           
SHEET    5   E 5 ARG A 874  VAL A 878 -1  O  ARG A 877   N  GLU A 843           
SHEET    1   F 2 ASP A 848  SER A 852  0                                        
SHEET    2   F 2 GLY A 867  ARG A 871 -1  O  SER A 869   N  SER A 850           
LINK         P    DG C   1                 O3P AMP C 100     1555   1555  1.59  
LINK         C   ARG A 307                 N   MSE A 308     1555   1555  1.33  
LINK         C   MSE A 308                 N   VAL A 309     1555   1555  1.33  
LINK         C   MSE A 393                 N   LEU A 394     1555   1555  1.34  
LINK         C   ALA A 479                 N   MSE A 480     1555   1555  1.33  
LINK         C   MSE A 480                 N   VAL A 481     1555   1555  1.32  
LINK         C   GLY A 500                 N   MSE A 501     1555   1555  1.33  
LINK         C   MSE A 501                 N   ILE A 502     1555   1555  1.32  
LINK         C   PRO A 542                 N   MSE A 543     1555   1555  1.33  
LINK         C   MSE A 543                 N   LEU A 544     1555   1555  1.32  
LINK         C   LEU A 722                 N   MSE A 723     1555   1555  1.33  
LINK         C   MSE A 723                 N   VAL A 724     1555   1555  1.33  
LINK         O3'  DT B  12                 P   DOC B  13     1555   1555  1.59  
CISPEP   1 PHE A  476    PRO A  477          0        -2.09                     
SITE     1 AC1 13 GLU A 566  TYR A 567  LYS A 568  TYR A 569                    
SITE     2 AC1 13 ARG A 573  ARG A 589  GLU A 621  PHE A 660                    
SITE     3 AC1 13 MSE A 723  LYS A 725  TRP A 742  LYS A 744                    
SITE     4 AC1 13  DG C   1                                                     
CRYST1  161.889  161.889   88.455  90.00  90.00 120.00 P 63          6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006177  0.003566  0.000000        0.00000                         
SCALE2      0.000000  0.007133  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011305        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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