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Database: PDB
Entry: 2FAO
LinkDB: 2FAO
Original site: 2FAO 
HEADER    HYDROLASE/TRANSFERASE                   07-DEC-05   2FAO              
TITLE     CRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA LIGD POLYMERASE           
TITLE    2 DOMAIN                                                               
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, HYDROLASE/TRANSFERASE              
KEYWDS   2 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 2FAO    1       VERSN                                    
REVDAT   1   23-MAY-06 2FAO    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.    1.50 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) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1614942.980                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 100611                         
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) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5073                            
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) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.59                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 14293                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2020                       
REMARK   3   BIN FREE R VALUE                    : 0.2310                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 755                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.008                        
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          : 25                                      
REMARK   3   SOLVENT ATOMS            : 498                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.27000                                              
REMARK   3    B22 (A**2) : -0.08000                                             
REMARK   3    B33 (A**2) : -0.19000                                             
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) : 0.17                            
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) : 0.18                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.08                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.91                            
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) : 0.990 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.530 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.960 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.740 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 44.31                                                
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  : 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   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2FAO 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 RCSB035658.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-APR-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   : 199285                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.540                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.85                                     
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, PH       
REMARK 280  6.5, VAPOR DIFFUSION, 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       35.87250            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      101.78850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.87250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      101.78850            
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    ASP A 624       73.71   -157.01                                   
REMARK 500    ASN A 659       95.47   -164.07                                   
REMARK 500    PRO A 674        2.90    -58.47                                   
REMARK 500    ARG A 752       30.33   -144.11                                   
REMARK 500    TYR A 773       -0.75     75.94                                   
REMARK 500    LYS B 612       23.41   -161.68                                   
REMARK 500    ILE B 613       67.83   -111.72                                   
REMARK 500    PRO B 614       91.80    -31.89                                   
REMARK 500    ASP B 624       72.27   -160.07                                   
REMARK 500    ASN B 659      103.08   -170.20                                   
REMARK 500    ARG B 665      169.12    177.33                                   
REMARK 500    PRO B 674       -1.99    -55.77                                   
REMARK 500    ARG B 752       30.86   -145.24                                   
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 SO4 B 1301                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1302                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1303                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1305                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1306                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2FAQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA LIGD POLYMERASE          
REMARK 900 DOMAIN WITH ATP AND MANGANESE                                        
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  2FAO A  533   840  UNP    Q9I1X7   Q9I1X7_PSEAE   533    840             
DBREF  2FAO B  533   840  UNP    Q9I1X7   Q9I1X7_PSEAE   533    840             
SEQADV 2FAO MET A  532  UNP  Q9I1X7              INITIATING METHIONINE          
SEQADV 2FAO 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    SO4  B1301       5                                                       
HET    SO4  A1302       5                                                       
HET    SO4  A1303       5                                                       
HET    SO4  A1305       5                                                       
HET    SO4  B1306       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   8  HOH   *498(H2 O)                                                    
HELIX    1   1 PRO A  560  GLN A  563  5                                   4    
HELIX    2   2 LYS A  566  TYR A  576  1                                  11    
HELIX    3   3 TYR A  576  ARG A  585  1                                  10    
HELIX    4   4 ASP A  620  ASP A  624  5                                   5    
HELIX    5   5 SER A  635  MET A  645  1                                  11    
HELIX    6   6 PRO A  677  GLY A  696  1                                  20    
HELIX    7   7 GLY A  720  MET A  739  1                                  20    
HELIX    8   8 GLY A  748  ARG A  752  5                                   5    
HELIX    9   9 TYR A  760  SER A  764  5                                   5    
HELIX   10  10 PHE A  788  LEU A  795  5                                   8    
HELIX   11  11 SER A  805  ALA A  814  1                                  10    
HELIX   12  12 SER A  830  LEU A  837  1                                   8    
HELIX   13  13 ARG B  543  ALA B  547  5                                   5    
HELIX   14  14 PRO B  560  GLN B  563  5                                   4    
HELIX   15  15 LYS B  566  TYR B  576  1                                  11    
HELIX   16  16 TYR B  576  ARG B  585  1                                  10    
HELIX   17  17 ASP B  620  ASP B  624  5                                   5    
HELIX   18  18 SER B  635  MET B  645  1                                  11    
HELIX   19  19 PRO B  677  GLY B  696  1                                  20    
HELIX   20  20 GLY B  720  MET B  739  1                                  20    
HELIX   21  21 GLY B  748  ARG B  752  5                                   5    
HELIX   22  22 PHE B  788  LEU B  795  5                                   8    
HELIX   23  23 SER B  805  ALA B  814  1                                  10    
HELIX   24  24 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  LEU A 591   O  GLN A 605           
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  VAL A 713   N  PHE A 666           
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  VAL B 758   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  MET B 709   N  LEU B 670           
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           
SITE     1 AC1  7 HOH B 162  HOH B 175  HOH B 330  SER B 552                    
SITE     2 AC1  7 HIS B 553  ARG B 556  LYS B 566                               
SITE     1 AC2  7 HOH A  84  HOH A 325  HOH A 488  SER A 552                    
SITE     2 AC2  7 HIS A 553  ARG A 556  LYS A 566                               
SITE     1 AC3  7 HOH A 212  HOH A 245  HOH A 480  ARG A 750                    
SITE     2 AC3  7 ASN A 751  ARG B 750  ASN B 751                               
SITE     1 AC4  6 HOH A 492  SER A 704  GLY A 706  LYS A 707                    
SITE     2 AC4  6 ARG A 776  ARG A 778                                          
SITE     1 AC5  8 HOH B 370  HOH B 503  SER B 704  GLY B 706                    
SITE     2 AC5  8 LYS B 707  GLY B 708  ARG B 776  ARG B 778                    
CRYST1   71.745  203.577   44.200  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      0.013938  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004912  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022624        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system