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Database: PDB
Entry: 2HIX
LinkDB: 2HIX
Original site: 2HIX 
HEADER    LIGASE                                  29-JUN-06   2HIX              
TITLE     ATP DEPENDENT DNA LIGASE FROM S. SOLFATARICUS BOUND TO ATP            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THERMOSTABLE DNA LIGASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: POLYDEOXYRIBONUCLEOTIDE SYNTHASE;                           
COMPND   5 EC: 6.5.1.1;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;                        
SOURCE   3 ORGANISM_TAXID: 2287;                                                
SOURCE   4 GENE: LIG;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ATP-DEPENDENT DNA LIGASE, DNA REPLICATION, LIGASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.PASCAL,T.ELLENBERGER                                              
REVDAT   3   13-JUL-11 2HIX    1       VERSN                                    
REVDAT   2   24-FEB-09 2HIX    1       VERSN                                    
REVDAT   1   07-NOV-06 2HIX    0                                                
JRNL        AUTH   J.M.PASCAL,O.V.TSODIKOV,G.L.HURA,W.SONG,E.A.COTNER,          
JRNL        AUTH 2 S.CLASSEN,A.E.TOMKINSON,J.A.TAINER,T.ELLENBERGER             
JRNL        TITL   A FLEXIBLE INTERFACE BETWEEN DNA LIGASE AND PCNA SUPPORTS    
JRNL        TITL 2 CONFORMATIONAL SWITCHING AND EFFICIENT LIGATION OF DNA.      
JRNL        REF    MOL.CELL                      V.  24   279 2006              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   17052461                                                     
JRNL        DOI    10.1016/J.MOLCEL.2006.08.015                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.87 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.87                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 17962                          
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) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 916                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.87                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.94                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 835                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 64.99                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3160                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 41                           
REMARK   3   BIN FREE R VALUE                    : 0.3620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4562                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 4                                       
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) : 49.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.99000                                             
REMARK   3    B22 (A**2) : -2.33000                                             
REMARK   3    B33 (A**2) : 4.32000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.431         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.316         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 35.431        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.892                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4684 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6322 ; 1.338 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   577 ; 5.638 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   204 ;36.939 ;24.461       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   881 ;19.690 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;21.789 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   708 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3442 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2062 ; 0.219 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3217 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   152 ; 0.159 ; 0.200       
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):    55 ; 0.196 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.210 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2943 ; 0.414 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4628 ; 0.747 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1970 ; 1.054 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1693 ; 1.769 ; 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  : 3                                          
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     1        A   230                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.3737  19.4623  48.7420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1063 T22:   0.0127                                     
REMARK   3      T33:  -0.0039 T12:  -0.0512                                     
REMARK   3      T13:  -0.0200 T23:  -0.0474                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3328 L22:   2.7368                                     
REMARK   3      L33:   3.9916 L12:   0.1000                                     
REMARK   3      L13:   0.3673 L23:  -0.5742                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1520 S12:  -0.2376 S13:  -0.1138                       
REMARK   3      S21:   0.6948 S22:   0.0770 S23:  -0.0069                       
REMARK   3      S31:   0.3478 S32:   0.1798 S33:  -0.2290                       
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   231        A   440                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.5223  23.6784  15.3762              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2124 T22:  -0.1479                                     
REMARK   3      T33:  -0.2980 T12:  -0.0603                                     
REMARK   3      T13:   0.0341 T23:  -0.0644                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1062 L22:   5.6917                                     
REMARK   3      L33:   3.2959 L12:   0.6062                                     
REMARK   3      L13:   0.9798 L23:  -2.0013                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0839 S12:   0.1512 S13:  -0.1540                       
REMARK   3      S21:  -0.1202 S22:   0.1251 S23:   0.4203                       
REMARK   3      S31:   0.1618 S32:  -0.0260 S33:  -0.2090                       
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   441        A   590                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1627  38.9458  -2.3184              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0345 T22:   0.0696                                     
REMARK   3      T33:   0.2528 T12:  -0.0260                                     
REMARK   3      T13:  -0.0285 T23:  -0.0024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2011 L22:   4.1849                                     
REMARK   3      L33:   5.4613 L12:   1.4852                                     
REMARK   3      L13:   1.6592 L23:  -0.6053                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2049 S12:   0.1882 S13:   0.5526                       
REMARK   3      S21:   0.3609 S22:  -0.1305 S23:  -0.9290                       
REMARK   3      S31:  -0.3822 S32:   0.7502 S33:   0.3354                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2HIX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB038393.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 12.3.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18026                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.860                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.86                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6-8% PEG 3350, 50 MM SODIUM ACETATE PH   
REMARK 280  4.5, 30-80 MM SODIUM/POTASSIUM TARTRATE, VAPOR DIFFUSION, SITTING   
REMARK 280  DROP, TEMPERATURE 298K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
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   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.34300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.34300            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       59.66200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       85.82500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       59.66200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       85.82500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       39.34300            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       59.66200            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       85.82500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       39.34300            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       59.66200            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       85.82500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     GLN A   103                                                      
REMARK 465     SER A   104                                                      
REMARK 465     THR A   105                                                      
REMARK 465     GLY A   106                                                      
REMARK 465     ILE A   107                                                      
REMARK 465     LEU A   108                                                      
REMARK 465     GLY A   109                                                      
REMARK 465     PHE A   110                                                      
REMARK 465     LEU A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     THR A   113                                                      
REMARK 465     THR A   114                                                      
REMARK 465     SER A   115                                                      
REMARK 465     LYS A   591                                                      
REMARK 465     ILE A   592                                                      
REMARK 465     GLU A   593                                                      
REMARK 465     SER A   594                                                      
REMARK 465     PRO A   595                                                      
REMARK 465     ALA A   596                                                      
REMARK 465     VAL A   597                                                      
REMARK 465     ASP A   598                                                      
REMARK 465     GLU A   599                                                      
REMARK 465     SER A   600                                                      
REMARK 465     VAL A   601                                                      
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     LYS A  35    CG   CD   CE   NZ                                   
REMARK 470     LYS A 116    CG   CD   CE   NZ                                   
REMARK 470     GLU A 409    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 436    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A 438    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET A 442    CG   SD   CE                                        
REMARK 470     LYS A 457    CG   CD   CE   NZ                                   
REMARK 470     LYS A 590    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    GLY A 462   C     GLY A 462   O       0.109                       
REMARK 500    LYS A 586   CD    LYS A 586   CE      0.398                       
REMARK 500    LYS A 586   CE    LYS A 586   NZ      0.185                       
REMARK 500    LYS A 589   CD    LYS A 589   CE      0.184                       
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    LEU A 352   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    LYS A 586   CG  -  CD  -  CE  ANGL. DEV. = -19.3 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    ASN A  75       73.09     55.07                                   
REMARK 500    GLU A 137      112.95    -15.90                                   
REMARK 500    ARG A 169       39.00    -64.79                                   
REMARK 500    ARG A 171      -78.13     -8.41                                   
REMARK 500    VAL A 172      -61.49     46.81                                   
REMARK 500    GLU A 272      -64.42     57.48                                   
REMARK 500    GLU A 317     -121.50    -65.08                                   
REMARK 500    SER A 318      -34.43    -16.73                                   
REMARK 500    PHE A 350       -4.68   -141.62                                   
REMARK 500    ARG A 436      -28.24    -37.98                                   
REMARK 500    ASP A 437      -24.82    -33.25                                   
REMARK 500    TYR A 438      -13.48    -43.62                                   
REMARK 500    GLU A 441     -174.41   -173.57                                   
REMARK 500    VAL A 526      -45.39   -141.46                                   
REMARK 500    ASP A 547       -3.60     66.70                                   
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 ATP A 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2HII   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2HIK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2HIV   RELATED DB: PDB                                   
DBREF  2HIX A    1   601  UNP    Q980T8   DNLI_SULSO       1    601             
SEQADV 2HIX MET A  -19  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIX GLY A  -18  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIX SER A  -17  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIX SER A  -16  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIX HIS A  -15  UNP  Q980T8              EXPRESSION TAG                 
SEQADV 2HIX HIS A  -14  UNP  Q980T8              EXPRESSION TAG                 
SEQADV 2HIX HIS A  -13  UNP  Q980T8              EXPRESSION TAG                 
SEQADV 2HIX HIS A  -12  UNP  Q980T8              EXPRESSION TAG                 
SEQADV 2HIX HIS A  -11  UNP  Q980T8              EXPRESSION TAG                 
SEQADV 2HIX HIS A  -10  UNP  Q980T8              EXPRESSION TAG                 
SEQADV 2HIX SER A   -9  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIX SER A   -8  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIX GLY A   -7  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIX LEU A   -6  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIX VAL A   -5  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIX PRO A   -4  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIX ARG A   -3  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIX GLY A   -2  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIX SER A   -1  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIX HIS A    0  UNP  Q980T8              CLONING ARTIFACT               
SEQRES   1 A  621  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  621  LEU VAL PRO ARG GLY SER HIS MET GLU PHE LYS VAL ILE          
SEQRES   3 A  621  ALA GLU TYR PHE ASP LYS LEU GLU LYS ILE SER SER ARG          
SEQRES   4 A  621  LEU GLN LEU THR ALA LEU LEU ALA ASP LEU LEU SER LYS          
SEQRES   5 A  621  SER ASP LYS THR ILE ILE ASP LYS VAL VAL TYR ILE ILE          
SEQRES   6 A  621  GLN GLY LYS LEU TRP PRO ASP PHE LEU GLY TYR PRO GLU          
SEQRES   7 A  621  LEU GLY ILE GLY GLU LYS PHE LEU ILE LYS ALA ILE SER          
SEQRES   8 A  621  ILE ALA THR ASN THR ASP GLU ASN SER VAL GLU ASN LEU          
SEQRES   9 A  621  TYR LYS THR ILE GLY ASP LEU GLY GLU VAL ALA ARG ARG          
SEQRES  10 A  621  LEU LYS SER LYS GLN GLN SER THR GLY ILE LEU GLY PHE          
SEQRES  11 A  621  LEU GLY THR THR SER LYS GLU SER LEU THR VAL ASP GLU          
SEQRES  12 A  621  VAL TYR SER THR LEU SER LYS VAL ALA LEU THR THR GLY          
SEQRES  13 A  621  GLU GLY SER ARG ASP LEU LYS ILE ARG LEU LEU ALA GLY          
SEQRES  14 A  621  LEU LEU LYS LYS ALA ASP PRO LEU GLU ALA LYS PHE LEU          
SEQRES  15 A  621  VAL ARG PHE VAL GLU GLY ARG LEU ARG VAL GLY ILE GLY          
SEQRES  16 A  621  ASP ALA THR VAL LEU ASP ALA MET ALA ILE ALA PHE GLY          
SEQRES  17 A  621  GLY GLY GLN SER ALA SER GLU ILE ILE GLU ARG ALA TYR          
SEQRES  18 A  621  ASN LEU ARG ALA ASP LEU GLY ASN ILE ALA LYS ILE ILE          
SEQRES  19 A  621  VAL GLU LYS GLY ILE GLU ALA LEU LYS THR LEU LYS PRO          
SEQRES  20 A  621  GLN VAL GLY ILE PRO ILE ARG PRO MET LEU ALA GLU ARG          
SEQRES  21 A  621  LEU SER ASN PRO GLU GLU ILE LEU LYS LYS MET GLY GLY          
SEQRES  22 A  621  ASN ALA ILE VAL ASP TYR LYS TYR ASP GLY GLU ARG ALA          
SEQRES  23 A  621  GLN ILE HIS LYS LYS GLU ASP LYS ILE PHE ILE PHE SER          
SEQRES  24 A  621  ARG ARG LEU GLU ASN ILE THR SER GLN TYR PRO ASP VAL          
SEQRES  25 A  621  VAL ASP TYR VAL SER LYS TYR ILE GLU GLY LYS GLU PHE          
SEQRES  26 A  621  ILE ILE GLU GLY GLU ILE VAL ALA ILE ASP PRO GLU SER          
SEQRES  27 A  621  GLY GLU MET ARG PRO PHE GLN GLU LEU MET HIS ARG LYS          
SEQRES  28 A  621  ARG LYS SER ASP ILE TYR GLU ALA ILE LYS GLU TYR PRO          
SEQRES  29 A  621  VAL ASN VAL PHE LEU PHE ASP LEU MET TYR TYR GLU ASP          
SEQRES  30 A  621  VAL ASP TYR THR THR LYS PRO LEU GLU ALA ARG ARG LYS          
SEQRES  31 A  621  LEU LEU GLU SER ILE VAL LYS PRO ASN ASP TYR VAL LYS          
SEQRES  32 A  621  ILE ALA HIS HIS ILE GLN ALA ASN ASN VAL GLU ASP LEU          
SEQRES  33 A  621  LYS SER PHE PHE TYR ARG ALA ILE SER GLU GLY GLY GLU          
SEQRES  34 A  621  GLY VAL MET VAL LYS ALA ILE GLY LYS ASP ALA ILE TYR          
SEQRES  35 A  621  GLN ALA GLY ALA ARG GLY TRP LEU TRP ILE LYS LEU LYS          
SEQRES  36 A  621  ARG ASP TYR GLN SER GLU MET ALA ASP THR VAL ASP LEU          
SEQRES  37 A  621  VAL VAL VAL GLY GLY PHE TYR GLY LYS GLY LYS ARG GLY          
SEQRES  38 A  621  GLY LYS ILE SER SER LEU LEU MET ALA ALA TYR ASN PRO          
SEQRES  39 A  621  LYS THR ASP SER PHE GLU SER VAL CYS LYS VAL ALA SER          
SEQRES  40 A  621  GLY PHE SER ASP GLU GLN LEU ASP GLU LEU GLN LYS LYS          
SEQRES  41 A  621  LEU MET GLU ILE LYS ARG ASP VAL LYS HIS PRO ARG VAL          
SEQRES  42 A  621  ASN SER LYS MET GLU PRO ASP ILE TRP VAL GLU PRO VAL          
SEQRES  43 A  621  TYR VAL ALA GLU ILE ILE GLY SER GLU ILE THR ILE SER          
SEQRES  44 A  621  PRO LEU HIS THR CYS CYS GLN ASP VAL VAL GLU LYS ASP          
SEQRES  45 A  621  ALA GLY LEU SER ILE ARG PHE PRO ARG PHE ILE ARG TRP          
SEQRES  46 A  621  ARG ASP ASP LYS SER PRO GLU ASP ALA THR THR THR ASP          
SEQRES  47 A  621  GLU ILE LEU GLU MET TYR ASN LYS GLN PRO LYS LYS LYS          
SEQRES  48 A  621  ILE GLU SER PRO ALA VAL ASP GLU SER VAL                      
HET    ATP  A 602      31                                                       
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   2  ATP    C10 H16 N5 O13 P3                                            
FORMUL   3  HOH   *4(H2 O)                                                      
HELIX    1   1 PHE A    3  GLU A   14  1                                  12    
HELIX    2   2 SER A   18  LYS A   32  1                                  15    
HELIX    3   3 ASP A   34  THR A   36  5                                   3    
HELIX    4   4 ILE A   37  ILE A   45  1                                   9    
HELIX    5   5 PRO A   51  GLY A   55  5                                   5    
HELIX    6   6 GLY A   62  ASN A   75  1                                  14    
HELIX    7   7 ASP A   77  GLY A   89  1                                  13    
HELIX    8   8 ASP A   90  SER A  100  1                                  11    
HELIX    9   9 THR A  120  THR A  134  1                                  15    
HELIX   10  10 GLY A  138  ALA A  154  1                                  17    
HELIX   11  11 ASP A  155  GLY A  168  1                                  14    
HELIX   12  12 GLY A  175  PHE A  187  1                                  13    
HELIX   13  13 GLY A  190  SER A  192  5                                   3    
HELIX   14  14 ALA A  193  ARG A  204  1                                  12    
HELIX   15  15 ASP A  206  LYS A  217  1                                  12    
HELIX   16  16 GLU A  220  LEU A  225  5                                   6    
HELIX   17  17 ASN A  243  MET A  251  1                                   9    
HELIX   18  18 ILE A  285  GLN A  288  5                                   4    
HELIX   19  19 TYR A  289  ILE A  300  1                                  12    
HELIX   20  20 PRO A  323  LYS A  331  1                                   9    
HELIX   21  21 ASP A  335  TYR A  343  1                                   9    
HELIX   22  22 PRO A  364  ILE A  375  1                                  12    
HELIX   23  23 ASN A  392  GLU A  406  1                                  15    
HELIX   24  24 ASP A  437  SER A  440  5                                   4    
HELIX   25  25 LYS A  457  GLY A  461  5                                   5    
HELIX   26  26 SER A  490  GLU A  503  1                                  14    
HELIX   27  27 SER A  570  ALA A  574  5                                   5    
HELIX   28  28 THR A  576  ASN A  585  1                                  10    
SHEET    1   A 5 LEU A 237  ARG A 240  0                                        
SHEET    2   A 5 ARG A 427  LYS A 435  1  O  LYS A 433   N  GLU A 239           
SHEET    3   A 5 GLY A 410  LYS A 414 -1  N  VAL A 413   O  ILE A 432           
SHEET    4   A 5 ALA A 255  TYR A 259 -1  N  ILE A 256   O  LYS A 414           
SHEET    5   A 5 HIS A 387  ALA A 390 -1  O  ILE A 388   N  VAL A 257           
SHEET    1   B 5 LYS A 274  PHE A 278  0                                        
SHEET    2   B 5 GLU A 264  LYS A 271 -1  N  HIS A 269   O  PHE A 276           
SHEET    3   B 5 GLU A 304  ALA A 313 -1  O  ILE A 311   N  GLU A 264           
SHEET    4   B 5 VAL A 345  TYR A 355 -1  O  PHE A 348   N  GLU A 310           
SHEET    5   B 5 VAL A 358  ASP A 359 -1  O  VAL A 358   N  TYR A 355           
SHEET    1   C 5 LYS A 274  PHE A 278  0                                        
SHEET    2   C 5 GLU A 264  LYS A 271 -1  N  HIS A 269   O  PHE A 276           
SHEET    3   C 5 GLU A 304  ALA A 313 -1  O  ILE A 311   N  GLU A 264           
SHEET    4   C 5 VAL A 345  TYR A 355 -1  O  PHE A 348   N  GLU A 310           
SHEET    5   C 5 VAL A 382  ILE A 384  1  O  LYS A 383   N  VAL A 347           
SHEET    1   D 6 LYS A 505  ARG A 506  0                                        
SHEET    2   D 6 ILE A 521  VAL A 523 -1  O  TRP A 522   N  ARG A 506           
SHEET    3   D 6 ASP A 444  TYR A 455 -1  N  GLY A 453   O  ILE A 521           
SHEET    4   D 6 ILE A 464  ASN A 473 -1  O  SER A 466   N  PHE A 454           
SHEET    5   D 6 SER A 478  VAL A 485 -1  O  VAL A 485   N  LEU A 467           
SHEET    6   D 6 VAL A 513  ASN A 514  1  O  ASN A 514   N  PHE A 479           
SHEET    1   E 5 LYS A 505  ARG A 506  0                                        
SHEET    2   E 5 ILE A 521  VAL A 523 -1  O  TRP A 522   N  ARG A 506           
SHEET    3   E 5 ASP A 444  TYR A 455 -1  N  GLY A 453   O  ILE A 521           
SHEET    4   E 5 VAL A 528  GLY A 533 -1  O  ILE A 531   N  VAL A 446           
SHEET    5   E 5 ARG A 561  PHE A 562 -1  O  ARG A 561   N  ILE A 532           
SHEET    1   F 2 ILE A 536  SER A 539  0                                        
SHEET    2   F 2 GLY A 554  ILE A 557 -1  O  GLY A 554   N  SER A 539           
SITE     1 AC1 13 ASP A 258  TYR A 259  LYS A 260  TYR A 261                    
SITE     2 AC1 13 ARG A 265  ARG A 280  GLU A 310  PHE A 350                    
SITE     3 AC1 13 MET A 412  LYS A 414  ARG A 427  LYS A 433                    
SITE     4 AC1 13 LYS A 435                                                     
CRYST1  119.324  171.650   78.686  90.00  90.00  90.00 C 2 2 21      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      0.008381  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005826  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012709        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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