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Database: PDB
Entry: 2FAQ
LinkDB: 2FAQ
Original site: 2FAQ 
HEADER    HYDROLASE/TRANSFERASE                   07-DEC-05   2FAQ              
TITLE     CRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA LIGD POLYMERASE           
TITLE    2 DOMAIN WITH ATP AND MANGANESE                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE ATP-DEPENDENT DNA LIGASE;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: POLYMERASE DOMAIN, RESIDUES 533-840;                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: B834 DE3;                                  
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PSMT3, PET28B DERIVED                     
KEYWDS    POLYMERASE, PRIMASE, LIGASE, NHEJ, ATP,                               
KEYWDS   2 HYDROLASE/TRANSFERASE COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.ZHU,J.NANDAKUMAR,J.ANIUKWU,L.K.WANG,M.S.GLICKMAN,C.D.LIMA,          
AUTHOR   2 S.SHUMAN                                                             
REVDAT   2   24-FEB-09 2FAQ    1       VERSN                                    
REVDAT   1   23-MAY-06 2FAQ    0                                                
JRNL        AUTH   H.ZHU,J.NANDAKUMAR,J.ANIUKWU,L.K.WANG,M.S.GLICKMAN,          
JRNL        AUTH 2 C.D.LIMA,S.SHUMAN                                            
JRNL        TITL   ATOMIC STRUCTURE AND NONHOMOLOGOUS END-JOINING               
JRNL        TITL 2 FUNCTION OF THE POLYMERASE COMPONENT OF BACTERIAL            
JRNL        TITL 3 DNA LIGASE D                                                 
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 103  1711 2006              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   16446439                                                     
JRNL        DOI    10.1073/PNAS.0509083103                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2176385.370                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 97202                          
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 SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4821                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 14607                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1950                       
REMARK   3   BIN FREE R VALUE                    : 0.2400                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 774                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.009                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4642                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 81                                      
REMARK   3   SOLVENT ATOMS            : 462                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 8.20                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.96000                                             
REMARK   3    B22 (A**2) : 0.96000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.21                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.03                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.24                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.13                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.86                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.140 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.680 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.170 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.080 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.39                                                 
REMARK   3   BSOL        : 40.80                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : ATP.PAR                                        
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : ATP.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2FAQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB035659.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK DOUBLE CRYSTAL      
REMARK 200                                   SAGITTAL FOCUSING MONOCHROMETER    
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 97263                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.570                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 33.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.09800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 22.800                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NATIVE MODEL                                          
REMARK 200 STARTING MODEL: PDB ENTRY 2FAO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CACODYLATE, 0.2 M          
REMARK 280  SODIUM ACETATE, 5 MM DTT,26-32% POLYETHYLENE GLYCOL-8000, 10        
REMARK 280  MM MANGANOUS CHLORIDE, 5 MM ATP, PH 6.5, VAPOR DIFFUSION,           
REMARK 280  HANGING DROP, TEMPERATURE 295K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       35.81600            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      102.09850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.81600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      102.09850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   532                                                      
REMARK 465     GLY A   533                                                      
REMARK 465     ALA A   534                                                      
REMARK 465     ARG A   535                                                      
REMARK 465     LYS A   536                                                      
REMARK 465     ALA A   537                                                      
REMARK 465     SER A   538                                                      
REMARK 465     ALA A   539                                                      
REMARK 465     GLY A   540                                                      
REMARK 465     ALA A   541                                                      
REMARK 465     SER A   542                                                      
REMARK 465     GLY A   838                                                      
REMARK 465     ARG A   839                                                      
REMARK 465     GLY A   840                                                      
REMARK 465     MET B   532                                                      
REMARK 465     GLY B   533                                                      
REMARK 465     ALA B   534                                                      
REMARK 465     ARG B   535                                                      
REMARK 465     LYS B   536                                                      
REMARK 465     ALA B   537                                                      
REMARK 465     SER B   538                                                      
REMARK 465     ALA B   539                                                      
REMARK 465     GLY B   540                                                      
REMARK 465     ALA B   541                                                      
REMARK 465     SER B   542                                                      
REMARK 465     GLY B   838                                                      
REMARK 465     ARG B   839                                                      
REMARK 465     GLY B   840                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A 614      107.64    -54.14                                   
REMARK 500    ASP A 624       74.24   -155.96                                   
REMARK 500    ASN A 659       98.43   -165.39                                   
REMARK 500    PRO A 674        0.76    -57.51                                   
REMARK 500    ARG A 752       33.94   -149.64                                   
REMARK 500    HIS B 553       56.86     39.79                                   
REMARK 500    PRO B 614       85.45    -57.85                                   
REMARK 500    ASP B 624       72.33   -160.08                                   
REMARK 500    ASN B 654       33.31    -90.98                                   
REMARK 500    ASN B 659      103.95   -169.01                                   
REMARK 500    ARG B 665      166.49    177.17                                   
REMARK 500    ARG B 752       31.19   -147.10                                   
REMARK 500    ASN B 763       50.81   -105.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 501  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 669   OD1                                                    
REMARK 620 2 ASP A 669   OD2  52.1                                              
REMARK 620 3 HOH A 155   O    62.9 114.5                                        
REMARK 620 4 HOH A 278   O   121.7  70.7 173.9                                  
REMARK 620 5 ASP A 671   OD1 115.6 102.8  97.8  83.9                            
REMARK 620 6 ATP A1304   O1G 148.1 154.3  89.5  84.9  81.8                      
REMARK 620 7 ATP A1304   O1B  83.0  92.9  85.7  90.8 160.7  79.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 502  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 669   OD2                                                    
REMARK 620 2 ASP A 671   OD2  67.3                                              
REMARK 620 3 HOH A 278   O    65.9  81.7                                        
REMARK 620 4 ASP A 759   OD2 119.5  96.6 173.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 503  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP B1302   O1G                                                    
REMARK 620 2 ATP B1302   O1B  78.6                                              
REMARK 620 3 HOH B 415   O    91.8  79.8                                        
REMARK 620 4 ASP B 669   OD1 160.5  97.5  68.7                                  
REMARK 620 5 ASP B 669   OD2 139.8  67.9 103.0  50.7                            
REMARK 620 6 HOH B 431   O    89.9  96.5 175.5 109.5  73.0                      
REMARK 620 7 ASP B 671   OD1  79.1 157.7  99.7 103.1 132.8  84.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 504  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 671   OD2                                                    
REMARK 620 2 ASP B 759   OD2 104.1                                              
REMARK 620 3 HOH B 431   O    75.9 176.5                                        
REMARK 620 4 HOH B 300   O    66.5  64.1 113.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 501                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 502                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 503                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 504                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1301                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1302                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1303                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 1302                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 1304                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2FAO   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA LIGD POLYMERASE          
REMARK 900 DOMAIN                                                               
REMARK 900 RELATED ID: 2FAR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA LIGD POLYMERASE          
REMARK 900 DOMAIN WITH DATP AND MANGANESE                                       
DBREF  2FAQ A  533   840  UNP    Q9I1X7   Q9I1X7_PSEAE   533    840             
DBREF  2FAQ B  533   840  UNP    Q9I1X7   Q9I1X7_PSEAE   533    840             
SEQADV 2FAQ MET A  532  UNP  Q9I1X7              INITIATING METHIONINE          
SEQADV 2FAQ MET B  532  UNP  Q9I1X7              INITIATING METHIONINE          
SEQRES   1 A  309  MET GLY ALA ARG LYS ALA SER ALA GLY ALA SER ARG ALA          
SEQRES   2 A  309  ALA THR ALA GLY VAL ARG ILE SER HIS PRO GLN ARG LEU          
SEQRES   3 A  309  ILE ASP PRO SER ILE GLN ALA SER LYS LEU GLU LEU ALA          
SEQRES   4 A  309  GLU PHE HIS ALA ARG TYR ALA ASP LEU LEU LEU ARG ASP          
SEQRES   5 A  309  LEU ARG GLU ARG PRO VAL SER LEU VAL ARG GLY PRO ASP          
SEQRES   6 A  309  GLY ILE GLY GLY GLU LEU PHE PHE GLN LYS HIS ALA ALA          
SEQRES   7 A  309  ARG LEU LYS ILE PRO GLY ILE VAL GLN LEU ASP PRO ALA          
SEQRES   8 A  309  LEU ASP PRO GLY HIS PRO PRO LEU LEU GLN ILE ARG SER          
SEQRES   9 A  309  ALA GLU ALA LEU VAL GLY ALA VAL GLN MET GLY SER ILE          
SEQRES  10 A  309  GLU PHE HIS THR TRP ASN ALA SER LEU ALA ASN LEU GLU          
SEQRES  11 A  309  ARG PRO ASP ARG PHE VAL LEU ASP LEU ASP PRO ASP PRO          
SEQRES  12 A  309  ALA LEU PRO TRP LYS ARG MET LEU GLU ALA THR GLN LEU          
SEQRES  13 A  309  SER LEU THR LEU LEU ASP GLU LEU GLY LEU ARG ALA PHE          
SEQRES  14 A  309  LEU LYS THR SER GLY GLY LYS GLY MET HIS LEU LEU VAL          
SEQRES  15 A  309  PRO LEU GLU ARG ARG HIS GLY TRP ASP GLU VAL LYS ASP          
SEQRES  16 A  309  PHE ALA GLN ALA ILE SER GLN HIS LEU ALA ARG LEU MET          
SEQRES  17 A  309  PRO GLU ARG PHE SER ALA VAL SER GLY PRO ARG ASN ARG          
SEQRES  18 A  309  VAL GLY LYS ILE PHE VAL ASP TYR LEU ARG ASN SER ARG          
SEQRES  19 A  309  GLY ALA SER THR VAL ALA ALA TYR SER VAL ARG ALA ARG          
SEQRES  20 A  309  GLU GLY LEU PRO VAL SER VAL PRO VAL PHE ARG GLU GLU          
SEQRES  21 A  309  LEU ASP SER LEU GLN GLY ALA ASN GLN TRP ASN LEU ARG          
SEQRES  22 A  309  SER LEU PRO GLN ARG LEU ASP GLU LEU ALA GLY ASP ASP          
SEQRES  23 A  309  PRO TRP ALA ASP TYR ALA GLY THR ARG GLN ARG ILE SER          
SEQRES  24 A  309  ALA ALA MET ARG ARG GLN LEU GLY ARG GLY                      
SEQRES   1 B  309  MET GLY ALA ARG LYS ALA SER ALA GLY ALA SER ARG ALA          
SEQRES   2 B  309  ALA THR ALA GLY VAL ARG ILE SER HIS PRO GLN ARG LEU          
SEQRES   3 B  309  ILE ASP PRO SER ILE GLN ALA SER LYS LEU GLU LEU ALA          
SEQRES   4 B  309  GLU PHE HIS ALA ARG TYR ALA ASP LEU LEU LEU ARG ASP          
SEQRES   5 B  309  LEU ARG GLU ARG PRO VAL SER LEU VAL ARG GLY PRO ASP          
SEQRES   6 B  309  GLY ILE GLY GLY GLU LEU PHE PHE GLN LYS HIS ALA ALA          
SEQRES   7 B  309  ARG LEU LYS ILE PRO GLY ILE VAL GLN LEU ASP PRO ALA          
SEQRES   8 B  309  LEU ASP PRO GLY HIS PRO PRO LEU LEU GLN ILE ARG SER          
SEQRES   9 B  309  ALA GLU ALA LEU VAL GLY ALA VAL GLN MET GLY SER ILE          
SEQRES  10 B  309  GLU PHE HIS THR TRP ASN ALA SER LEU ALA ASN LEU GLU          
SEQRES  11 B  309  ARG PRO ASP ARG PHE VAL LEU ASP LEU ASP PRO ASP PRO          
SEQRES  12 B  309  ALA LEU PRO TRP LYS ARG MET LEU GLU ALA THR GLN LEU          
SEQRES  13 B  309  SER LEU THR LEU LEU ASP GLU LEU GLY LEU ARG ALA PHE          
SEQRES  14 B  309  LEU LYS THR SER GLY GLY LYS GLY MET HIS LEU LEU VAL          
SEQRES  15 B  309  PRO LEU GLU ARG ARG HIS GLY TRP ASP GLU VAL LYS ASP          
SEQRES  16 B  309  PHE ALA GLN ALA ILE SER GLN HIS LEU ALA ARG LEU MET          
SEQRES  17 B  309  PRO GLU ARG PHE SER ALA VAL SER GLY PRO ARG ASN ARG          
SEQRES  18 B  309  VAL GLY LYS ILE PHE VAL ASP TYR LEU ARG ASN SER ARG          
SEQRES  19 B  309  GLY ALA SER THR VAL ALA ALA TYR SER VAL ARG ALA ARG          
SEQRES  20 B  309  GLU GLY LEU PRO VAL SER VAL PRO VAL PHE ARG GLU GLU          
SEQRES  21 B  309  LEU ASP SER LEU GLN GLY ALA ASN GLN TRP ASN LEU ARG          
SEQRES  22 B  309  SER LEU PRO GLN ARG LEU ASP GLU LEU ALA GLY ASP ASP          
SEQRES  23 B  309  PRO TRP ALA ASP TYR ALA GLY THR ARG GLN ARG ILE SER          
SEQRES  24 B  309  ALA ALA MET ARG ARG GLN LEU GLY ARG GLY                      
HET     MN  A 501       1                                                       
HET     MN  A 502       1                                                       
HET     MN  B 503       1                                                       
HET     MN  B 504       1                                                       
HET    SO4  B1301       5                                                       
HET    SO4  A1302       5                                                       
HET    SO4  A1303       5                                                       
HET    ATP  B1302      31                                                       
HET    ATP  A1304      31                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   3   MN    4(MN 2+)                                                     
FORMUL   7  SO4    3(O4 S 2-)                                                   
FORMUL  10  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL  12  HOH   *462(H2 O)                                                    
HELIX    1   1 LYS A  566  TYR A  576  1                                  11    
HELIX    2   2 TYR A  576  ARG A  585  1                                  10    
HELIX    3   3 ASP A  620  ASP A  624  5                                   5    
HELIX    4   4 SER A  635  MET A  645  1                                  11    
HELIX    5   5 PRO A  677  GLY A  696  1                                  20    
HELIX    6   6 GLY A  720  MET A  739  1                                  20    
HELIX    7   7 GLY A  748  ARG A  752  5                                   5    
HELIX    8   8 TYR A  760  SER A  764  5                                   5    
HELIX    9   9 PHE A  788  LEU A  795  5                                   8    
HELIX   10  10 SER A  805  ALA A  814  1                                  10    
HELIX   11  11 SER A  830  LEU A  837  1                                   8    
HELIX   12  12 ARG B  543  ALA B  547  5                                   5    
HELIX   13  13 PRO B  560  GLN B  563  5                                   4    
HELIX   14  14 LYS B  566  TYR B  576  1                                  11    
HELIX   15  15 TYR B  576  ARG B  585  1                                  10    
HELIX   16  16 ASP B  620  ASP B  624  5                                   5    
HELIX   17  17 SER B  635  MET B  645  1                                  11    
HELIX   18  18 PRO B  677  GLY B  696  1                                  20    
HELIX   19  19 GLY B  720  MET B  739  1                                  20    
HELIX   20  20 GLY B  748  ARG B  752  5                                   5    
HELIX   21  21 PHE B  788  LEU B  795  5                                   8    
HELIX   22  22 SER B  805  ALA B  814  1                                  10    
HELIX   23  23 SER B  830  LEU B  837  1                                   8    
SHEET    1   A 2 LEU A 557  ASP A 559  0                                        
SHEET    2   A 2 ALA A 564  SER A 565 -1  O  ALA A 564   N  ILE A 558           
SHEET    1   B 4 PHE A 603  GLN A 605  0                                        
SHEET    2   B 4 VAL A 589  ARG A 593 -1  N  ARG A 593   O  PHE A 603           
SHEET    3   B 4 SER A 647  THR A 652 -1  O  HIS A 651   N  SER A 590           
SHEET    4   B 4 THR A 769  VAL A 770 -1  O  THR A 769   N  THR A 652           
SHEET    1   C 2 VAL A 617  GLN A 618  0                                        
SHEET    2   C 2 LEU A 631  GLN A 632 -1  O  GLN A 632   N  VAL A 617           
SHEET    1   D 6 PHE A 743  SER A 744  0                                        
SHEET    2   D 6 ILE A 756  ASP A 759  1  O  VAL A 758   N  SER A 744           
SHEET    3   D 6 ARG A 665  PRO A 672 -1  N  ASP A 671   O  PHE A 757           
SHEET    4   D 6 MET A 709  PRO A 714 -1  O  LEU A 711   N  LEU A 668           
SHEET    5   D 6 PHE A 700  THR A 703 -1  N  PHE A 700   O  LEU A 712           
SHEET    6   D 6 PRO A 786  VAL A 787 -1  O  VAL A 787   N  LEU A 701           
SHEET    1   E 2 LEU B 557  ASP B 559  0                                        
SHEET    2   E 2 ALA B 564  SER B 565 -1  O  ALA B 564   N  ILE B 558           
SHEET    1   F 4 PHE B 603  GLN B 605  0                                        
SHEET    2   F 4 VAL B 589  ARG B 593 -1  N  ARG B 593   O  PHE B 603           
SHEET    3   F 4 SER B 647  THR B 652 -1  O  HIS B 651   N  SER B 590           
SHEET    4   F 4 THR B 769  VAL B 770 -1  O  THR B 769   N  THR B 652           
SHEET    1   G 2 VAL B 617  GLN B 618  0                                        
SHEET    2   G 2 LEU B 631  GLN B 632 -1  O  GLN B 632   N  VAL B 617           
SHEET    1   H 6 PHE B 743  SER B 744  0                                        
SHEET    2   H 6 ILE B 756  ASP B 759  1  O  ILE B 756   N  SER B 744           
SHEET    3   H 6 ARG B 665  PRO B 672 -1  N  ASP B 669   O  ASP B 759           
SHEET    4   H 6 MET B 709  PRO B 714 -1  O  LEU B 711   N  LEU B 668           
SHEET    5   H 6 PHE B 700  THR B 703 -1  N  LYS B 702   O  HIS B 710           
SHEET    6   H 6 PRO B 786  VAL B 787 -1  O  VAL B 787   N  LEU B 701           
LINK        MN    MN A 501                 OD1 ASP A 669     1555   1555  2.59  
LINK        MN    MN A 501                 OD2 ASP A 669     1555   1555  2.37  
LINK        MN    MN A 501                 O   HOH A 155     1555   1555  2.32  
LINK        MN    MN A 501                 O   HOH A 278     1555   1555  2.40  
LINK        MN    MN A 501                 OD1 ASP A 671     1555   1555  2.35  
LINK        MN    MN A 501                 O1G ATP A1304     1555   1555  2.27  
LINK        MN    MN A 501                 O1B ATP A1304     1555   1555  2.32  
LINK        MN    MN A 502                 OD2 ASP A 669     1555   1555  2.67  
LINK        MN    MN A 502                 OD2 ASP A 671     1555   1555  2.51  
LINK        MN    MN A 502                 O   HOH A 278     1555   1555  2.39  
LINK        MN    MN A 502                 OD2 ASP A 759     1555   1555  2.35  
LINK        MN    MN B 503                 O1G ATP B1302     1555   1555  2.31  
LINK        MN    MN B 503                 O1B ATP B1302     1555   1555  2.26  
LINK        MN    MN B 503                 O   HOH B 415     1555   1555  2.35  
LINK        MN    MN B 503                 OD1 ASP B 669     1555   1555  2.38  
LINK        MN    MN B 503                 OD2 ASP B 669     1555   1555  2.69  
LINK        MN    MN B 503                 O   HOH B 431     1555   1555  2.19  
LINK        MN    MN B 503                 OD1 ASP B 671     1555   1555  2.28  
LINK        MN    MN B 504                 OD2 ASP B 671     1555   1555  2.54  
LINK        MN    MN B 504                 OD2 ASP B 759     1555   1555  2.45  
LINK        MN    MN B 504                 O   HOH B 431     1555   1555  2.28  
LINK        MN    MN B 504                 O   HOH B 300     1555   1555  2.61  
SITE     1 AC1  5 HOH A 155  HOH A 278  ASP A 669  ASP A 671                    
SITE     2 AC1  5 ATP A1304                                                     
SITE     1 AC2  5 HOH A 278  ASP A 669  ASP A 671  ASP A 759                    
SITE     2 AC2  5 ARG A 762                                                     
SITE     1 AC3  5 HOH B 415  HOH B 431  ASP B 669  ASP B 671                    
SITE     2 AC3  5 ATP B1302                                                     
SITE     1 AC4  6 HOH B 300  HOH B 431  ASP B 669  ASP B 671                    
SITE     2 AC4  6 ASP B 759  ARG B 762                                          
SITE     1 AC5  7 HOH A 162  HOH B 175  HOH B 330  SER B 552                    
SITE     2 AC5  7 HIS B 553  ARG B 556  LYS B 566                               
SITE     1 AC6  5 HOH A  84  SER A 552  HIS A 553  ARG A 556                    
SITE     2 AC6  5 LYS A 566                                                     
SITE     1 AC7  6 HOH A 212  HOH A 245  ARG A 750  ASN A 751                    
SITE     2 AC7  6 ARG B 750  ASN B 751                                          
SITE     1 AC8 24 HOH B  71  HOH B  77  HOH B  94  HOH B 157                    
SITE     2 AC8 24 HOH B 231  HOH B 273  HOH B 370  HOH B 404                    
SITE     3 AC8 24 HOH B 415  HOH B 431   MN B 503  PHE B 604                    
SITE     4 AC8 24 HIS B 651  ASP B 669  ASP B 671  SER B 704                    
SITE     5 AC8 24 LYS B 707  GLY B 708  HIS B 710  ARG B 762                    
SITE     6 AC8 24 SER B 768  THR B 769  ARG B 776  ARG B 778                    
SITE     1 AC9 21 HOH A  32  HOH A  47  HOH A 130  HOH A 145                    
SITE     2 AC9 21 HOH A 155  HOH A 204  HOH A 278  HOH A 395                    
SITE     3 AC9 21  MN A 501  PHE A 604  HIS A 651  ASP A 669                    
SITE     4 AC9 21 ASP A 671  SER A 704  LYS A 707  GLY A 708                    
SITE     5 AC9 21 HIS A 710  ARG A 762  SER A 768  ARG A 776                    
SITE     6 AC9 21 ARG A 778                                                     
CRYST1   71.632  204.197   44.152  90.00  90.00  90.00 P 21 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      0.013960  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004897  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022649        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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