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Database: PDB
Entry: 3L2P
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Original site: 3L2P 
HEADER    LIGASE/DNA                              15-DEC-09   3L2P              
TITLE     HUMAN DNA LIGASE III RECOGNIZES DNA ENDS BY DYNAMIC SWITCHING BETWEEN 
TITLE    2 TWO DNA BOUND STATES                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA LIGASE 3;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 257-833;                                      
COMPND   5 SYNONYM: DNA LIGASE III, POLYDEOXYRIBONUCLEOTIDE SYNTHASE [ATP] 3;   
COMPND   6 EC: 6.5.1.1;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: 5'-D(P*CP*GP*GP*GP*AP*TP*GP*CP*GP*TP*C)-3';                
COMPND  10 CHAIN: B;                                                            
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: 5'-D(*GP*TP*CP*GP*GP*AP*CP*TP*G)-3';                       
COMPND  14 CHAIN: C;                                                            
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: 5'-D(*GP*CP*CP*AP*GP*TP*CP*CP*GP*AP*CP*GP*AP*CP*GP*CP*AP*TP
COMPND  18 *CP*CP*CP*G)-3';                                                     
COMPND  19 CHAIN: D;                                                            
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LIG3;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET-28;                               
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 OTHER_DETAILS: SYNTHETIC CONSTRUCT;                                  
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 SYNTHETIC: YES;                                                      
SOURCE  15 OTHER_DETAILS: SYNTHETIC CONSTRUCT;                                  
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 SYNTHETIC: YES;                                                      
SOURCE  18 OTHER_DETAILS: SYNTHETIC CONSTRUCT                                   
KEYWDS    DNA LIGASE, DNA REPAIR, ATP-BINDING, CELL CYCLE, CELL DIVISION, DNA   
KEYWDS   2 DAMAGE, DNA RECOMBINATION, DNA REPLICATION, LIGASE, MAGNESIUM,       
KEYWDS   3 METAL-BINDING, NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN, ZINC-    
KEYWDS   4 FINGER, LIGASE-DNA COMPLEX                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.A.COTNER-GOHARA,I.K.KIM,M.HAMMEL,J.A.TAINER,A.TOMKINSON,            
AUTHOR   2 T.ELLENBERGER                                                        
REVDAT   2   11-AUG-10 3L2P    1       JRNL                                     
REVDAT   1   14-JUL-10 3L2P    0                                                
JRNL        AUTH   E.COTNER-GOHARA,I.K.KIM,M.HAMMEL,J.A.TAINER,A.E.TOMKINSON,   
JRNL        AUTH 2 T.ELLENBERGER                                                
JRNL        TITL   HUMAN DNA LIGASE III RECOGNIZES DNA ENDS BY DYNAMIC          
JRNL        TITL 2 SWITCHING BETWEEN TWO DNA-BOUND STATES.                      
JRNL        REF    BIOCHEMISTRY                  V.  49  6165 2010              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   20518483                                                     
JRNL        DOI    10.1021/BI100503W                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 49.21                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 24119                          
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) : 0.235                           
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1287                            
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) : 1331                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.10                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 77                           
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4145                                    
REMARK   3   NUCLEIC ACID ATOMS       : 855                                     
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 144.10                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.07000                                             
REMARK   3    B22 (A**2) : -0.07000                                             
REMARK   3    B33 (A**2) : 0.14000                                              
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): 0.806         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.383         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.303         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.042        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.919                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.890                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5200 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7206 ; 1.840 ; 2.182       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   530 ; 7.059 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   185 ;38.570 ;24.595       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   747 ;20.966 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;22.962 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   816 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3598 ; 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):  2664 ; 0.516 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4268 ; 1.014 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2536 ; 1.673 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2938 ; 2.682 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : NULL                            
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
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   159        A   390                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.9180   7.6830  54.4880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2551 T22:   0.2582                                     
REMARK   3      T33:   0.3132 T12:   0.0718                                     
REMARK   3      T13:   0.0064 T23:   0.0111                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1114 L22:   2.4193                                     
REMARK   3      L33:   2.2843 L12:  -0.3772                                     
REMARK   3      L13:  -0.1493 L23:   0.0156                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1377 S12:   0.2796 S13:  -0.5908                       
REMARK   3      S21:  -0.3668 S22:  -0.0013 S23:  -0.2880                       
REMARK   3      S31:   0.5068 S32:   0.4252 S33:   0.1390                       
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   391        A   590                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3070  33.6310  60.5010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1643 T22:   0.1828                                     
REMARK   3      T33:   0.3068 T12:   0.0938                                     
REMARK   3      T13:  -0.1133 T23:   0.0428                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4009 L22:   2.1615                                     
REMARK   3      L33:   3.2157 L12:  -0.1284                                     
REMARK   3      L13:  -0.4678 L23:  -0.1198                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0287 S12:   0.1461 S13:   0.4297                       
REMARK   3      S21:  -0.2559 S22:   0.0276 S23:   0.2916                       
REMARK   3      S31:  -0.5717 S32:  -0.4608 S33:   0.0010                       
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   591        A   745                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.3560  33.5060  29.6090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1147 T22:   0.8414                                     
REMARK   3      T33:   0.3931 T12:   0.0283                                     
REMARK   3      T13:  -0.0676 T23:   0.2340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4553 L22:   0.2373                                     
REMARK   3      L33:   3.7540 L12:  -0.1082                                     
REMARK   3      L13:   0.9631 L23:  -0.4616                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0700 S12:   0.8995 S13:   0.2828                       
REMARK   3      S21:  -0.3937 S22:  -0.0225 S23:   0.0494                       
REMARK   3      S31:  -0.3553 S32:   0.2024 S33:   0.0926                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B    11                          
REMARK   3    RESIDUE RANGE :   C    12        C    20                          
REMARK   3    RESIDUE RANGE :   D    23        D    42                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.4670  23.8050  45.6750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2686 T22:   0.3835                                     
REMARK   3      T33:   0.3612 T12:  -0.0536                                     
REMARK   3      T13:  -0.0836 T23:   0.0565                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3831 L22:   1.7507                                     
REMARK   3      L33:   1.6315 L12:  -0.0835                                     
REMARK   3      L13:  -0.0862 L23:  -0.1269                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0846 S12:   0.6376 S13:   0.2084                       
REMARK   3      S21:  -0.6722 S22:  -0.0058 S23:   0.1906                       
REMARK   3      S31:   0.0802 S32:   0.0956 S33:   0.0905                       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3L2P COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB056757.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
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-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : CRYO-COOLED SI(111) DOUBLE         
REMARK 200                                   CRYSTAL.                           
REMARK 200  OPTICS                         : CRYOGENICALLY-COOLED DOUBLE        
REMARK 200                                   CRYSTAL SI(111) MONOCHROMATOR.     
REMARK 200                                   TRIPLE STRIPED VERTICAL AND        
REMARK 200                                   HORIZANTAL FOCUSSING MIRRORS IN    
REMARK 200                                   KIRKPATRICK-BAEZ GEOMETRY          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25407                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.210                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 12.900                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.0000                            
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) : 3.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.60200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.250                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM SULFATE, 0.1M SODIUM      
REMARK 280  ACETATE PH 5.6, VAPOR DIFFUSION, TEMPERATURE 295K                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.21550            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       65.07450            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       65.07450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       37.60775            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       65.07450            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       65.07450            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      112.82325            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       65.07450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       65.07450            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       37.60775            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       65.07450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       65.07450            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      112.82325            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       75.21550            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, B, C                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   207                                                      
REMARK 465     ALA A   208                                                      
REMARK 465     GLY A   209                                                      
REMARK 465     ASP A   210                                                      
REMARK 465     GLY A   211                                                      
REMARK 465     PHE A   212                                                      
REMARK 465     HIS A   213                                                      
REMARK 465     LYS A   376                                                      
REMARK 465     GLU A   377                                                      
REMARK 465     PRO A   378                                                      
REMARK 465     GLY A   379                                                      
REMARK 465     GLN A   380                                                      
REMARK 465     ARG A   381                                                      
REMARK 465     ARG A   382                                                      
REMARK 465     ALA A   383                                                      
REMARK 465     GLU A   596                                                      
REMARK 465     GLY A   597                                                      
REMARK 465     ALA A   598                                                      
REMARK 465     ASP A   666                                                      
REMARK 465     PRO A   667                                                      
REMARK 465     SER A   668                                                      
REMARK 465     LYS A   669                                                      
REMARK 465     ILE A   670                                                      
REMARK 465     PRO A   671                                                      
REMARK 465     SER A   672                                                      
REMARK 465     TRP A   673                                                      
REMARK 465     LEU A   674                                                      
REMARK 465     LYS A   675                                                      
REMARK 465     VAL A   676                                                      
REMARK 465     ASN A   677                                                      
REMARK 465     LYS A   678                                                      
REMARK 465     ILE A   679                                                      
REMARK 465     TYR A   680                                                      
REMARK 465     TYR A   681                                                      
REMARK 465     PRO A   682                                                      
REMARK 465     ASP A   683                                                      
REMARK 465     PHE A   684                                                      
REMARK 465     ILE A   685                                                      
REMARK 465     VAL A   686                                                      
REMARK 465     PRO A   687                                                      
REMARK 465     ASP A   688                                                      
REMARK 465     PRO A   689                                                      
REMARK 465     LYS A   690                                                      
REMARK 465     LYS A   691                                                      
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     HIS A 168    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A 170    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS A 171    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 172    CG   CD   CE   NZ                                   
REMARK 470     THR A 230    OG1  CG2                                            
REMARK 470     LYS A 237    CG   CD   CE   NZ                                   
REMARK 470     ASN A 248    CG   OD1  ND2                                       
REMARK 470     ARG A 268    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 275    CG   CD   CE   NZ                                   
REMARK 470     PHE A 277    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 282    CG   CD   CE   NZ                                   
REMARK 470     LYS A 480    CG   CD   CE   NZ                                   
REMARK 470     LYS A 483    CG   CD   CE   NZ                                   
REMARK 470     GLN A 499    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 500    CG   OD1  OD2                                       
REMARK 470     LYS A 635    CG   CD   CE   NZ                                   
REMARK 470     LYS A 662    CG   CD   CE   NZ                                   
REMARK 470     LYS A 665    CG   CD   CE   NZ                                   
REMARK 470     PHE A 702    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 704    CG   CD   CE   NZ                                   
REMARK 470     GLU A 706    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 711    CG   OD1  OD2                                       
REMARK 470     ARG A 722    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 727    CG   CD   CE   NZ                                   
REMARK 470     LYS A 730    CG   CD   CE   NZ                                   
REMARK 470      DC B  11    O3'                                                 
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASN A 502   CB    ASN A 502   CG      0.172                       
REMARK 500     DC B   8   O3'    DC B   8   C3'    -0.039                       
REMARK 500     DG C  12   P      DG C  12   O5'     0.123                       
REMARK 500     DG C  12   O5'    DG C  12   C5'     0.179                       
REMARK 500     DG C  12   C5'    DG C  12   C4'     0.070                       
REMARK 500     DC D  24   O3'    DC D  24   C3'    -0.040                       
REMARK 500     DC D  25   C1'    DC D  25   N1      0.085                       
REMARK 500     DT D  28   O3'    DT D  28   C3'    -0.063                       
REMARK 500     DA D  35   O3'    DA D  35   C3'    -0.048                       
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    PRO A 538   C   -  N   -  CA  ANGL. DEV. =  11.0 DEGREES          
REMARK 500     DC B   1   O4' -  C1' -  N1  ANGL. DEV. =   7.1 DEGREES          
REMARK 500     DG B   2   C5' -  C4' -  O4' ANGL. DEV. =   7.1 DEGREES          
REMARK 500     DG B   2   C3' -  C2' -  C1' ANGL. DEV. =  -6.0 DEGREES          
REMARK 500     DG B   2   O4' -  C1' -  C2' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DG B   2   O4' -  C1' -  N9  ANGL. DEV. =   4.3 DEGREES          
REMARK 500     DG B   3   O4' -  C1' -  N9  ANGL. DEV. =  -5.4 DEGREES          
REMARK 500     DT B   6   C4  -  C5  -  C7  ANGL. DEV. =   3.7 DEGREES          
REMARK 500     DT B   6   C6  -  C5  -  C7  ANGL. DEV. =  -4.0 DEGREES          
REMARK 500     DG B   7   C4  -  C5  -  N7  ANGL. DEV. =   3.0 DEGREES          
REMARK 500     DG B   7   C5  -  N7  -  C8  ANGL. DEV. =  -3.8 DEGREES          
REMARK 500     DG B   7   N7  -  C8  -  N9  ANGL. DEV. =   3.2 DEGREES          
REMARK 500     DT B  10   O4' -  C4' -  C3' ANGL. DEV. =  -9.0 DEGREES          
REMARK 500     DT B  10   N3  -  C4  -  O4  ANGL. DEV. =   4.1 DEGREES          
REMARK 500     DT B  10   C5  -  C4  -  O4  ANGL. DEV. =  -4.5 DEGREES          
REMARK 500     DG C  12   O4' -  C4' -  C3' ANGL. DEV. =  -5.8 DEGREES          
REMARK 500     DG C  12   C5' -  C4' -  C3' ANGL. DEV. =   9.2 DEGREES          
REMARK 500     DG C  12   C4' -  C3' -  C2' ANGL. DEV. =   7.4 DEGREES          
REMARK 500     DG C  12   O4' -  C1' -  N9  ANGL. DEV. =   8.0 DEGREES          
REMARK 500     DG C  12   C8  -  N9  -  C4  ANGL. DEV. =  -3.3 DEGREES          
REMARK 500     DT C  13   C5  -  C4  -  O4  ANGL. DEV. =  -4.3 DEGREES          
REMARK 500     DC C  14   O5' -  P   -  OP2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500     DG C  15   O5' -  C5' -  C4' ANGL. DEV. =  -5.3 DEGREES          
REMARK 500     DA C  17   O4' -  C1' -  C2' ANGL. DEV. =   3.0 DEGREES          
REMARK 500     DA C  17   O4' -  C1' -  N9  ANGL. DEV. =   4.7 DEGREES          
REMARK 500     DT C  19   O4' -  C1' -  N1  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500     DG C  20   N3  -  C4  -  C5  ANGL. DEV. =  -3.5 DEGREES          
REMARK 500     DG C  20   N3  -  C4  -  N9  ANGL. DEV. =   3.7 DEGREES          
REMARK 500     DG D  23   C3' -  C2' -  C1' ANGL. DEV. =  -4.8 DEGREES          
REMARK 500     DG D  23   O4' -  C1' -  N9  ANGL. DEV. =   3.6 DEGREES          
REMARK 500     DC D  24   O4' -  C4' -  C3' ANGL. DEV. =  -3.7 DEGREES          
REMARK 500     DC D  25   O4' -  C4' -  C3' ANGL. DEV. =  -2.6 DEGREES          
REMARK 500     DC D  25   C3' -  C2' -  C1' ANGL. DEV. =  -5.5 DEGREES          
REMARK 500     DC D  25   O4' -  C1' -  N1  ANGL. DEV. =   6.0 DEGREES          
REMARK 500     DA D  32   O4' -  C1' -  N9  ANGL. DEV. =   3.7 DEGREES          
REMARK 500     DC D  33   O4' -  C1' -  N1  ANGL. DEV. =   4.8 DEGREES          
REMARK 500     DG D  34   O4' -  C1' -  N9  ANGL. DEV. =   4.6 DEGREES          
REMARK 500     DA D  35   O4' -  C1' -  N9  ANGL. DEV. =   2.7 DEGREES          
REMARK 500     DC D  36   O5' -  C5' -  C4' ANGL. DEV. =  -5.0 DEGREES          
REMARK 500     DC D  38   O4' -  C4' -  C3' ANGL. DEV. =  -2.4 DEGREES          
REMARK 500     DC D  38   C1' -  O4' -  C4' ANGL. DEV. =  -7.8 DEGREES          
REMARK 500     DC D  38   O4' -  C1' -  N1  ANGL. DEV. =   2.8 DEGREES          
REMARK 500     DC D  43   O4' -  C4' -  C3' ANGL. DEV. =  -2.7 DEGREES          
REMARK 500     DC D  43   C3' -  C2' -  C1' ANGL. DEV. =  -7.0 DEGREES          
REMARK 500     DC D  43   O4' -  C1' -  C2' ANGL. DEV. =  -7.3 DEGREES          
REMARK 500     DC D  42   C3' -  O3' -  P   ANGL. DEV. =  -7.8 DEGREES          
REMARK 500     DG D  44   O4' -  C1' -  C2' ANGL. DEV. =  -4.9 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    LYS A 205      -69.85   -101.40                                   
REMARK 500    ASP A 236      -59.62    -27.41                                   
REMARK 500    ASP A 262      103.40   -166.67                                   
REMARK 500    PHE A 270       21.93    -77.44                                   
REMARK 500    LYS A 275       22.32    -65.17                                   
REMARK 500    SER A 276      -44.21   -136.05                                   
REMARK 500    THR A 301      -27.47   -149.75                                   
REMARK 500    SER A 315       22.44    -77.06                                   
REMARK 500    ARG A 316       31.11   -140.24                                   
REMARK 500    THR A 318       11.95    -69.10                                   
REMARK 500    ALA A 319      -65.09     72.05                                   
REMARK 500    LYS A 334       56.94     36.82                                   
REMARK 500    ASP A 347      138.57    169.12                                   
REMARK 500    PRO A 348      -32.01    -34.35                                   
REMARK 500    VAL A 374      -85.85   -123.43                                   
REMARK 500    MET A 391      -10.07     86.81                                   
REMARK 500    CYS A 412       77.45   -115.83                                   
REMARK 500    LEU A 443       18.29     58.84                                   
REMARK 500    VAL A 451       -8.62   -162.78                                   
REMARK 500    THR A 489       -8.35    -51.84                                   
REMARK 500    ASN A 514       62.81     28.38                                   
REMARK 500    PRO A 538      110.32    -25.24                                   
REMARK 500    ARG A 540      -65.39   -132.32                                   
REMARK 500    THR A 550      -20.72   -155.26                                   
REMARK 500    GLU A 565       50.60   -100.13                                   
REMARK 500    ALA A 643      -53.95   -128.21                                   
REMARK 500    GLU A 657       10.14    -65.37                                   
REMARK 500    MET A 660       71.54   -108.92                                   
REMARK 500    ALA A 707      -34.03   -139.91                                   
REMARK 500    THR A 709      -34.77    -37.20                                   
REMARK 500    ALA A 710       93.61    -66.87                                   
REMARK 500    ASP A 711      -32.72     43.08                                   
REMARK 500    PHE A 717       61.17     39.32                                   
REMARK 500    THR A 721      -75.93   -107.97                                   
REMARK 500    LYS A 727       51.93   -105.41                                   
REMARK 500    ASP A 728       85.65    -52.41                                   
REMARK 500    TRP A 729     -173.57     67.89                                   
REMARK 500    LYS A 730      -43.73     60.38                                   
REMARK 500    ALA A 732      176.79    -59.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     AMP A  901                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP A 901                 
DBREF  3L2P A  170   746  UNP    P49916   DNLI3_HUMAN    257    833             
DBREF  3L2P B    1    11  PDB    3L2P     3L2P             1     11             
DBREF  3L2P C   12    20  PDB    3L2P     3L2P            12     20             
DBREF  3L2P D   23    44  PDB    3L2P     3L2P            23     44             
SEQADV 3L2P HIS A  168  UNP  P49916              EXPRESSION TAG                 
SEQADV 3L2P MET A  169  UNP  P49916              EXPRESSION TAG                 
SEQRES   1 A  579  HIS MET ARG HIS LYS ASP CYS LEU LEU ARG GLU PHE ARG          
SEQRES   2 A  579  LYS LEU CYS ALA MET VAL ALA ASP ASN PRO SER TYR ASN          
SEQRES   3 A  579  THR LYS THR GLN ILE ILE GLN ASP PHE LEU ARG LYS GLY          
SEQRES   4 A  579  SER ALA GLY ASP GLY PHE HIS GLY ASP VAL TYR LEU THR          
SEQRES   5 A  579  VAL LYS LEU LEU LEU PRO GLY VAL ILE LYS THR VAL TYR          
SEQRES   6 A  579  ASN LEU ASN ASP LYS GLN ILE VAL LYS LEU PHE SER ARG          
SEQRES   7 A  579  ILE PHE ASN CYS ASN PRO ASP ASP MET ALA ARG ASP LEU          
SEQRES   8 A  579  GLU GLN GLY ASP VAL SER GLU THR ILE ARG VAL PHE PHE          
SEQRES   9 A  579  GLU GLN SER LYS SER PHE PRO PRO ALA ALA LYS SER LEU          
SEQRES  10 A  579  LEU THR ILE GLN GLU VAL ASP GLU PHE LEU LEU ARG LEU          
SEQRES  11 A  579  SER LYS LEU THR LYS GLU ASP GLU GLN GLN GLN ALA LEU          
SEQRES  12 A  579  GLN ASP ILE ALA SER ARG CYS THR ALA ASN ASP LEU LYS          
SEQRES  13 A  579  CYS ILE ILE ARG LEU ILE LYS HIS ASP LEU LYS MET ASN          
SEQRES  14 A  579  SER GLY ALA LYS HIS VAL LEU ASP ALA LEU ASP PRO ASN          
SEQRES  15 A  579  ALA TYR GLU ALA PHE LYS ALA SER ARG ASN LEU GLN ASP          
SEQRES  16 A  579  VAL VAL GLU ARG VAL LEU HIS ASN ALA GLN GLU VAL GLU          
SEQRES  17 A  579  LYS GLU PRO GLY GLN ARG ARG ALA LEU SER VAL GLN ALA          
SEQRES  18 A  579  SER LEU MET THR PRO VAL GLN PRO MET LEU ALA GLU ALA          
SEQRES  19 A  579  CYS LYS SER VAL GLU TYR ALA MET LYS LYS CYS PRO ASN          
SEQRES  20 A  579  GLY MET PHE SER GLU ILE LYS TYR ASP GLY GLU ARG VAL          
SEQRES  21 A  579  GLN VAL HIS LYS ASN GLY ASP HIS PHE SER TYR PHE SER          
SEQRES  22 A  579  ARG SER LEU LYS PRO VAL LEU PRO HIS LYS VAL ALA HIS          
SEQRES  23 A  579  PHE LYS ASP TYR ILE PRO GLN ALA PHE PRO GLY GLY HIS          
SEQRES  24 A  579  SER MET ILE LEU ASP SER GLU VAL LEU LEU ILE ASP ASN          
SEQRES  25 A  579  LYS THR GLY LYS PRO LEU PRO PHE GLY THR LEU GLY VAL          
SEQRES  26 A  579  HIS LYS LYS ALA ALA PHE GLN ASP ALA ASN VAL CYS LEU          
SEQRES  27 A  579  PHE VAL PHE ASP CYS ILE TYR PHE ASN ASP VAL SER LEU          
SEQRES  28 A  579  MET ASP ARG PRO LEU CYS GLU ARG ARG LYS PHE LEU HIS          
SEQRES  29 A  579  ASP ASN MET VAL GLU ILE PRO ASN ARG ILE MET PHE SER          
SEQRES  30 A  579  GLU MET LYS ARG VAL THR LYS ALA LEU ASP LEU ALA ASP          
SEQRES  31 A  579  MET ILE THR ARG VAL ILE GLN GLU GLY LEU GLU GLY LEU          
SEQRES  32 A  579  VAL LEU LYS ASP VAL LYS GLY THR TYR GLU PRO GLY LYS          
SEQRES  33 A  579  ARG HIS TRP LEU LYS VAL LYS LYS ASP TYR LEU ASN GLU          
SEQRES  34 A  579  GLY ALA MET ALA ASP THR ALA ASP LEU VAL VAL LEU GLY          
SEQRES  35 A  579  ALA PHE TYR GLY GLN GLY SER LYS GLY GLY MET MET SER          
SEQRES  36 A  579  ILE PHE LEU MET GLY CYS TYR ASP PRO GLY SER GLN LYS          
SEQRES  37 A  579  TRP CYS THR VAL THR LYS CYS ALA GLY GLY HIS ASP ASP          
SEQRES  38 A  579  ALA THR LEU ALA ARG LEU GLN ASN GLU LEU ASP MET VAL          
SEQRES  39 A  579  LYS ILE SER LYS ASP PRO SER LYS ILE PRO SER TRP LEU          
SEQRES  40 A  579  LYS VAL ASN LYS ILE TYR TYR PRO ASP PHE ILE VAL PRO          
SEQRES  41 A  579  ASP PRO LYS LYS ALA ALA VAL TRP GLU ILE THR GLY ALA          
SEQRES  42 A  579  GLU PHE SER LYS SER GLU ALA HIS THR ALA ASP GLY ILE          
SEQRES  43 A  579  SER ILE ARG PHE PRO ARG CYS THR ARG ILE ARG ASP ASP          
SEQRES  44 A  579  LYS ASP TRP LYS SER ALA THR ASN LEU PRO GLN LEU LYS          
SEQRES  45 A  579  GLU LEU TYR GLN LEU SER LYS                                  
SEQRES   1 B   11   DC  DG  DG  DG  DA  DT  DG  DC  DG  DT  DC                  
SEQRES   1 C    9   DG  DT  DC  DG  DG  DA  DC  DT  DG                          
SEQRES   1 D   22   DG  DC  DC  DA  DG  DT  DC  DC  DG  DA  DC  DG  DA          
SEQRES   2 D   22   DC  DG  DC  DA  DT  DC  DC  DC  DG                          
HET    AMP  A 901      22                                                       
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
FORMUL   5  AMP    C10 H14 N5 O7 P                                              
HELIX    1   1 HIS A  171  CYS A  174  5                                   4    
HELIX    2   2 LEU A  175  ASP A  188  1                                  14    
HELIX    3   3 SER A  191  LYS A  205  1                                  15    
HELIX    4   4 ASP A  215  LEU A  224  1                                  10    
HELIX    5   5 ASN A  235  ASN A  248  1                                  14    
HELIX    6   6 ASN A  250  LEU A  258  1                                   9    
HELIX    7   7 GLU A  259  GLY A  261  5                                   3    
HELIX    8   8 ASP A  262  GLN A  273  1                                  12    
HELIX    9   9 THR A  286  LYS A  299  1                                  14    
HELIX   10  10 LYS A  302  SER A  315  1                                  14    
HELIX   11  11 ALA A  319  LYS A  330  1                                  12    
HELIX   12  12 GLY A  338  ALA A  345  1                                   8    
HELIX   13  13 ASN A  349  SER A  357  1                                   9    
HELIX   14  14 ASN A  359  GLU A  373  1                                  15    
HELIX   15  15 SER A  404  CYS A  412  1                                   9    
HELIX   16  16 LEU A  447  VAL A  451  5                                   5    
HELIX   17  17 HIS A  453  ASP A  456  5                                   4    
HELIX   18  18 TYR A  457  PHE A  462  1                                   6    
HELIX   19  19 PRO A  486  LEU A  490  5                                   5    
HELIX   20  20 GLY A  491  PHE A  498  1                                   8    
HELIX   21  21 PRO A  522  MET A  534  1                                  13    
HELIX   22  22 LYS A  551  GLU A  565  1                                  15    
HELIX   23  23 ASP A  647  LEU A  654  1                                   8    
HELIX   24  24 ASN A  734  LEU A  744  1                                  11    
SHEET    1   A 5 LEU A 398  ALA A 401  0                                        
SHEET    2   A 5 ARG A 584  VAL A 589  1  O  TRP A 586   N  GLU A 400           
SHEET    3   A 5 LEU A 570  ASP A 574 -1  N  LEU A 572   O  LEU A 587           
SHEET    4   A 5 MET A 416  ILE A 420 -1  N  PHE A 417   O  LYS A 573           
SHEET    5   A 5 MET A 546  VAL A 549 -1  O  VAL A 549   N  MET A 416           
SHEET    1   B 5 HIS A 435  PHE A 439  0                                        
SHEET    2   B 5 GLU A 425  ASN A 432 -1  N  ASN A 432   O  HIS A 435           
SHEET    3   B 5 SER A 467  LEU A 476 -1  O  SER A 472   N  VAL A 427           
SHEET    4   B 5 VAL A 503  PHE A 513 -1  O  CYS A 504   N  LEU A 475           
SHEET    5   B 5 VAL A 516  SER A 517 -1  O  VAL A 516   N  PHE A 513           
SHEET    1   C 5 HIS A 435  PHE A 439  0                                        
SHEET    2   C 5 GLU A 425  ASN A 432 -1  N  ASN A 432   O  HIS A 435           
SHEET    3   C 5 SER A 467  LEU A 476 -1  O  SER A 472   N  VAL A 427           
SHEET    4   C 5 VAL A 503  PHE A 513 -1  O  CYS A 504   N  LEU A 475           
SHEET    5   C 5 ILE A 541  PHE A 543  1  O  MET A 542   N  VAL A 507           
SHEET    1   D 5 TRP A 636  CYS A 642  0                                        
SHEET    2   D 5 ILE A 623  TYR A 629 -1  N  CYS A 628   O  CYS A 637           
SHEET    3   D 5 ASP A 601  PHE A 611 -1  N  VAL A 606   O  GLY A 627           
SHEET    4   D 5 ALA A 693  GLY A 699 -1  O  ILE A 697   N  ALA A 603           
SHEET    5   D 5 ARG A 719  CYS A 720 -1  O  ARG A 719   N  THR A 698           
SHEET    1   E 2 PHE A 702  LYS A 704  0                                        
SHEET    2   E 2 ILE A 713  ILE A 715 -1  O  SER A 714   N  SER A 703           
LINK         NZ  LYS A 421                 P   AMP A 901     1555   1555  2.23  
SITE     1 AC1 11 GLU A 419  ILE A 420  LYS A 421  TYR A 422                    
SITE     2 AC1 11 ARG A 426  PHE A 508  LYS A 573  TRP A 586                    
SITE     3 AC1 11 LYS A 588  LYS A 590   DG C  12                               
CRYST1  130.149  130.149  150.431  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007684  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007684  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006648        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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