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Database: PDB
Entry: 1KJQ
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Original site: 1KJQ 
HEADER    TRANSFERASE                             05-DEC-01   1KJQ              
TITLE     CRYSTAL STRUCTURE OF GLYCINAMIDE RIBONUCLEOTIDE                       
TITLE    2 TRANSFORMYLASE IN COMPLEX WITH MG-ADP                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE 2;             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GART 2; GAR TRANSFORMYLASE 2; 5'-                           
COMPND   5 PHOSPHORIBOSYLGLYCINAMIDE;                                           
COMPND   6 EC: 2.1.2.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: PURT;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-22B                                   
KEYWDS    ATP-GRASP, PURINE BIOSYNTHESIS, NUCLEOTIDE, TRANSFERASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.B.THODEN,S.M.FIRESTINE,S.J.BENKOVIC,H.M.HOLDEN                      
REVDAT   3   24-FEB-09 1KJQ    1       VERSN                                    
REVDAT   2   01-APR-03 1KJQ    1       JRNL                                     
REVDAT   1   28-JUN-02 1KJQ    0                                                
JRNL        AUTH   J.B.THODEN,S.M.FIRESTINE,S.J.BENKOVIC,H.M.HOLDEN             
JRNL        TITL   PURT-ENCODED GLYCINAMIDE RIBONUCLEOTIDE                      
JRNL        TITL 2 TRANSFORMYLASE. ACCOMMODATION OF ADENOSINE                   
JRNL        TITL 3 NUCLEOTIDE ANALOGS WITHIN THE ACTIVE SITE.                   
JRNL        REF    J.BIOL.CHEM.                  V. 277 23898 2002              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   11953435                                                     
JRNL        DOI    10.1074/JBC.M202251200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 365075                         
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 36505                           
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.1900                 
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 365075                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6029                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 135                                     
REMARK   3   SOLVENT ATOMS            : 1040                                    
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.014 ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : 2.320 ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : ENGH & HUBER                                     
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1KJQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB015023.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.7009                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SBC-2                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 365075                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: TNT                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1EYZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 5000, NACL, MGCL2, MOPS, ADP,        
REMARK 280  GAR, PH 6.7, BATCH AT 277K                                          
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       31.17500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       89.67000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.17500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       89.67000            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     SER A   160                                                      
REMARK 465     SER A   161                                                      
REMARK 465     GLY A   162                                                      
REMARK 465     SER B   160                                                      
REMARK 465     SER B   161                                                      
REMARK 465     GLY B   162                                                      
REMARK 465     LYS B   163                                                      
REMARK 465     GLY B   185                                                      
REMARK 465     ARG B   186                                                      
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 163    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   728     O    HOH A   845              2.09            
REMARK 500   NH2  ARG A    43     O    HOH A   809              2.11            
REMARK 500   NH1  ARG A    14     O    HOH A   553              2.18            
REMARK 500   O2   EDO A   402     O    HOH A   700              2.18            
REMARK 500   O1   EDO B   399     O    HOH B   714              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500  CL    CL  A   395     O    HOH A   699     4455     1.72            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    GLU A  30   CD    GLU A  30   OE2     0.078                       
REMARK 500    GLU A  95   CD    GLU A  95   OE2     0.072                       
REMARK 500    GLU A 115   CD    GLU A 115   OE2     0.069                       
REMARK 500    GLU A 123   CD    GLU A 123   OE2     0.067                       
REMARK 500    GLU A 138   CD    GLU A 138   OE2     0.067                       
REMARK 500    GLU A 172   CD    GLU A 172   OE2     0.067                       
REMARK 500    GLU A 267   CD    GLU A 267   OE2     0.087                       
REMARK 500    GLU A 372   CD    GLU A 372   OE2     0.068                       
REMARK 500    GLU A 379   CD    GLU A 379   OE2     0.068                       
REMARK 500    GLU B  26   CD    GLU B  26   OE2     0.073                       
REMARK 500    GLU B  95   CD    GLU B  95   OE2     0.070                       
REMARK 500    GLU B  96   CD    GLU B  96   OE2     0.070                       
REMARK 500    GLU B 123   CD    GLU B 123   OE2     0.067                       
REMARK 500    GLU B 138   CD    GLU B 138   OE2     0.073                       
REMARK 500    GLU B 245   CD    GLU B 245   OE2     0.086                       
REMARK 500    GLU B 267   CD    GLU B 267   OE2     0.077                       
REMARK 500    GLU B 274   CD    GLU B 274   OE2     0.071                       
REMARK 500    GLU B 372   CD    GLU B 372   OE2     0.069                       
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    ASP A  63   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A  65   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG A  68   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A  68   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG A  68   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A  68   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG A 133   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP A 136   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    PHE A 167   CB  -  CG  -  CD2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ARG A 169   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    TYR A 180   CB  -  CG  -  CD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    TYR A 180   CB  -  CG  -  CD1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A 191   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ASP A 227   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG A 231   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A 252   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG A 283   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP A 286   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A 316   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 316   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ASP A 338   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG A 363   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ASP A 376   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP A 376   CB  -  CG  -  OD2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ASP B  42   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG B  43   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG B  43   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG B  55   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP B  65   CB  -  CG  -  OD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG B 118   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ASP B 136   CB  -  CG  -  OD2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    ASP B 147   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP B 201   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ASP B 227   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP B 227   CB  -  CG  -  OD2 ANGL. DEV. =  -8.1 DEGREES          
REMARK 500    ASP B 286   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP B 286   CB  -  CG  -  OD2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    ASP B 296   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP B 296   CB  -  CG  -  OD2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ARG B 305   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ASP B 347   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG B 363   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG B 363   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG B 380   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A   8       -6.52     78.14                                   
REMARK 500    ALA A  87       92.89    -68.09                                   
REMARK 500    GLU A 123      -61.32    -94.21                                   
REMARK 500    ALA A 187        6.90     58.34                                   
REMARK 500    ARG A 283      174.73    177.48                                   
REMARK 500    ASN A 334       59.79   -156.87                                   
REMARK 500    ASP A 359       69.80   -152.36                                   
REMARK 500    LEU B   8       -1.17     77.35                                   
REMARK 500    GLU B 123      -66.63    -90.73                                   
REMARK 500    SER B 278      -61.42   -107.85                                   
REMARK 500    PRO B 282       51.48    -92.24                                   
REMARK 500    ARG B 283      172.45    178.12                                   
REMARK 500    TYR B 318       35.96    -98.35                                   
REMARK 500    ASN B 334       59.81   -153.74                                   
REMARK 500    ASP B 359       73.57   -153.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 806        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH A 946        DISTANCE =  7.45 ANGSTROMS                       
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                              MG A 393  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A   1   O3B                                                    
REMARK 620 2 ADP A   1   O2A  90.6                                              
REMARK 620 3 HOH A 841   O    88.3 178.9                                        
REMARK 620 4 HOH A 485   O    93.3  86.1  93.8                                  
REMARK 620 5 GLU A 279   OE1  92.1  87.3  93.0 171.5                            
REMARK 620 6 GLU A 267   OE2 174.7  94.7  86.4  86.9  88.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 394  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL A 101   O                                                      
REMARK 620 2 ASN A 100   ND2  89.8                                              
REMARK 620 3 PRO A 103   O    77.0 141.4                                        
REMARK 620 4 HOH A 821   O   158.6 110.7  89.6                                  
REMARK 620 5 HOH A 445   O    77.7  90.1 121.2  95.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 393  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 279   OE1                                                    
REMARK 620 2 GLU B 267   OE1  83.8                                              
REMARK 620 3 HOH B 767   O    93.7  86.9                                        
REMARK 620 4 ADP B 397   O2A  87.6  94.3 178.4                                  
REMARK 620 5 ADP B 397   O3B  97.8 175.1  88.4  90.4                            
REMARK 620 6 HOH B 470   O   166.5  84.5  92.3  86.7  94.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 394  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 811   O                                                      
REMARK 620 2 HOH A 920   O    80.5                                              
REMARK 620 3 HIS B  51   O   121.2 156.8                                        
REMARK 620 4 HOH A 505   O   132.4  55.0 101.8                                  
REMARK 620 5 HOH B 555   O    50.5  71.6 127.4 117.9                            
REMARK 620 6 HOH A 586   O    58.8 138.1  65.0 166.4  74.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 393                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 393                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 394                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 394                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 395                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 396                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 395                  
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 396                  
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 1                   
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 397                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPO A 397                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 398                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 398                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 399                 
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 399                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 400                 
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 401                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 402                 
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 400                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 403                 
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 404                 
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 405                 
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 401                 
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 402                 
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 406                 
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 407                 
DBREF  1KJQ A    2   392  UNP    P33221   PURT_ECOLI       1    391             
DBREF  1KJQ B    2   392  UNP    P33221   PURT_ECOLI       1    391             
SEQRES   1 A  391  THR LEU LEU GLY THR ALA LEU ARG PRO ALA ALA THR ARG          
SEQRES   2 A  391  VAL MET LEU LEU GLY SER GLY GLU LEU GLY LYS GLU VAL          
SEQRES   3 A  391  ALA ILE GLU CYS GLN ARG LEU GLY VAL GLU VAL ILE ALA          
SEQRES   4 A  391  VAL ASP ARG TYR ALA ASP ALA PRO ALA MET HIS VAL ALA          
SEQRES   5 A  391  HIS ARG SER HIS VAL ILE ASN MET LEU ASP GLY ASP ALA          
SEQRES   6 A  391  LEU ARG ARG VAL VAL GLU LEU GLU LYS PRO HIS TYR ILE          
SEQRES   7 A  391  VAL PRO GLU ILE GLU ALA ILE ALA THR ASP MET LEU ILE          
SEQRES   8 A  391  GLN LEU GLU GLU GLU GLY LEU ASN VAL VAL PRO CYS ALA          
SEQRES   9 A  391  ARG ALA THR LYS LEU THR MET ASN ARG GLU GLY ILE ARG          
SEQRES  10 A  391  ARG LEU ALA ALA GLU GLU LEU GLN LEU PRO THR SER THR          
SEQRES  11 A  391  TYR ARG PHE ALA ASP SER GLU SER LEU PHE ARG GLU ALA          
SEQRES  12 A  391  VAL ALA ASP ILE GLY TYR PRO CYS ILE VAL LYS PRO VAL          
SEQRES  13 A  391  MET SER SER SER GLY LYS GLY GLN THR PHE ILE ARG SER          
SEQRES  14 A  391  ALA GLU GLN LEU ALA GLN ALA TRP LYS TYR ALA GLN GLN          
SEQRES  15 A  391  GLY GLY ARG ALA GLY ALA GLY ARG VAL ILE VAL GLU GLY          
SEQRES  16 A  391  VAL VAL LYS PHE ASP PHE GLU ILE THR LEU LEU THR VAL          
SEQRES  17 A  391  SER ALA VAL ASP GLY VAL HIS PHE CYS ALA PRO VAL GLY          
SEQRES  18 A  391  HIS ARG GLN GLU ASP GLY ASP TYR ARG GLU SER TRP GLN          
SEQRES  19 A  391  PRO GLN GLN MET SER PRO LEU ALA LEU GLU ARG ALA GLN          
SEQRES  20 A  391  GLU ILE ALA ARG LYS VAL VAL LEU ALA LEU GLY GLY TYR          
SEQRES  21 A  391  GLY LEU PHE GLY VAL GLU LEU PHE VAL CYS GLY ASP GLU          
SEQRES  22 A  391  VAL ILE PHE SER GLU VAL SER PRO ARG PRO HIS ASP THR          
SEQRES  23 A  391  GLY MET VAL THR LEU ILE SER GLN ASP LEU SER GLU PHE          
SEQRES  24 A  391  ALA LEU HIS VAL ARG ALA PHE LEU GLY LEU PRO VAL GLY          
SEQRES  25 A  391  GLY ILE ARG GLN TYR GLY PRO ALA ALA SER ALA VAL ILE          
SEQRES  26 A  391  LEU PRO GLN LEU THR SER GLN ASN VAL THR PHE ASP ASN          
SEQRES  27 A  391  VAL GLN ASN ALA VAL GLY ALA ASP LEU GLN ILE ARG LEU          
SEQRES  28 A  391  PHE GLY LYS PRO GLU ILE ASP GLY SER ARG ARG LEU GLY          
SEQRES  29 A  391  VAL ALA LEU ALA THR ALA GLU SER VAL VAL ASP ALA ILE          
SEQRES  30 A  391  GLU ARG ALA LYS HIS ALA ALA GLY GLN VAL LYS VAL GLN          
SEQRES  31 A  391  GLY                                                          
SEQRES   1 B  391  THR LEU LEU GLY THR ALA LEU ARG PRO ALA ALA THR ARG          
SEQRES   2 B  391  VAL MET LEU LEU GLY SER GLY GLU LEU GLY LYS GLU VAL          
SEQRES   3 B  391  ALA ILE GLU CYS GLN ARG LEU GLY VAL GLU VAL ILE ALA          
SEQRES   4 B  391  VAL ASP ARG TYR ALA ASP ALA PRO ALA MET HIS VAL ALA          
SEQRES   5 B  391  HIS ARG SER HIS VAL ILE ASN MET LEU ASP GLY ASP ALA          
SEQRES   6 B  391  LEU ARG ARG VAL VAL GLU LEU GLU LYS PRO HIS TYR ILE          
SEQRES   7 B  391  VAL PRO GLU ILE GLU ALA ILE ALA THR ASP MET LEU ILE          
SEQRES   8 B  391  GLN LEU GLU GLU GLU GLY LEU ASN VAL VAL PRO CYS ALA          
SEQRES   9 B  391  ARG ALA THR LYS LEU THR MET ASN ARG GLU GLY ILE ARG          
SEQRES  10 B  391  ARG LEU ALA ALA GLU GLU LEU GLN LEU PRO THR SER THR          
SEQRES  11 B  391  TYR ARG PHE ALA ASP SER GLU SER LEU PHE ARG GLU ALA          
SEQRES  12 B  391  VAL ALA ASP ILE GLY TYR PRO CYS ILE VAL LYS PRO VAL          
SEQRES  13 B  391  MET SER SER SER GLY LYS GLY GLN THR PHE ILE ARG SER          
SEQRES  14 B  391  ALA GLU GLN LEU ALA GLN ALA TRP LYS TYR ALA GLN GLN          
SEQRES  15 B  391  GLY GLY ARG ALA GLY ALA GLY ARG VAL ILE VAL GLU GLY          
SEQRES  16 B  391  VAL VAL LYS PHE ASP PHE GLU ILE THR LEU LEU THR VAL          
SEQRES  17 B  391  SER ALA VAL ASP GLY VAL HIS PHE CYS ALA PRO VAL GLY          
SEQRES  18 B  391  HIS ARG GLN GLU ASP GLY ASP TYR ARG GLU SER TRP GLN          
SEQRES  19 B  391  PRO GLN GLN MET SER PRO LEU ALA LEU GLU ARG ALA GLN          
SEQRES  20 B  391  GLU ILE ALA ARG LYS VAL VAL LEU ALA LEU GLY GLY TYR          
SEQRES  21 B  391  GLY LEU PHE GLY VAL GLU LEU PHE VAL CYS GLY ASP GLU          
SEQRES  22 B  391  VAL ILE PHE SER GLU VAL SER PRO ARG PRO HIS ASP THR          
SEQRES  23 B  391  GLY MET VAL THR LEU ILE SER GLN ASP LEU SER GLU PHE          
SEQRES  24 B  391  ALA LEU HIS VAL ARG ALA PHE LEU GLY LEU PRO VAL GLY          
SEQRES  25 B  391  GLY ILE ARG GLN TYR GLY PRO ALA ALA SER ALA VAL ILE          
SEQRES  26 B  391  LEU PRO GLN LEU THR SER GLN ASN VAL THR PHE ASP ASN          
SEQRES  27 B  391  VAL GLN ASN ALA VAL GLY ALA ASP LEU GLN ILE ARG LEU          
SEQRES  28 B  391  PHE GLY LYS PRO GLU ILE ASP GLY SER ARG ARG LEU GLY          
SEQRES  29 B  391  VAL ALA LEU ALA THR ALA GLU SER VAL VAL ASP ALA ILE          
SEQRES  30 B  391  GLU ARG ALA LYS HIS ALA ALA GLY GLN VAL LYS VAL GLN          
SEQRES  31 B  391  GLY                                                          
HET     MG  A 393       1                                                       
HET     MG  B 393       1                                                       
HET     NA  B 394       1                                                       
HET     NA  A 394       1                                                       
HET     CL  A 395       1                                                       
HET     CL  A 396       1                                                       
HET     CL  B 395       1                                                       
HET     CL  B 396       1                                                       
HET    ADP  A   1      27                                                       
HET    ADP  B 397      27                                                       
HET    MPO  A 397      13                                                       
HET    EDO  A 398       4                                                       
HET    EDO  B 398       4                                                       
HET    EDO  A 399       4                                                       
HET    EDO  B 399       4                                                       
HET    EDO  A 400       4                                                       
HET    EDO  A 401       4                                                       
HET    EDO  A 402       4                                                       
HET    EDO  B 400       4                                                       
HET    EDO  A 403       4                                                       
HET    EDO  A 404       4                                                       
HET    EDO  A 405       4                                                       
HET    EDO  B 401       4                                                       
HET    EDO  B 402       4                                                       
HET    EDO  A 406       4                                                       
HET    EDO  A 407       4                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     MPO 3[N-MORPHOLINO]PROPANE SULFONIC ACID                             
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5   NA    2(NA 1+)                                                     
FORMUL   7   CL    4(CL 1-)                                                     
FORMUL  11  ADP    2(C10 H15 N5 O10 P2)                                         
FORMUL  13  MPO    C7 H15 N O4 S                                                
FORMUL  14  EDO    15(C2 H6 O2)                                                 
FORMUL  29  HOH   *1018(H2 O)                                                   
HELIX    1   1 GLY A   21  ARG A   33  1                                  13    
HELIX    2   2 ALA A   47  ALA A   53  5                                   7    
HELIX    3   3 ASP A   63  LYS A   75  1                                  13    
HELIX    4   4 ALA A   87  GLU A   97  1                                  11    
HELIX    5   5 CYS A  104  ASN A  113  1                                  10    
HELIX    6   6 ASN A  113  GLU A  123  1                                  11    
HELIX    7   7 SER A  137  GLY A  149  1                                  13    
HELIX    8   8 SER A  170  GLU A  172  5                                   3    
HELIX    9   9 GLN A  173  GLY A  185  1                                  13    
HELIX   10  10 ARG A  186  ALA A  189  5                                   4    
HELIX   11  11 SER A  240  GLY A  259  1                                  20    
HELIX   12  12 HIS A  285  MET A  289  5                                   5    
HELIX   13  13 VAL A  290  GLN A  295  1                                   6    
HELIX   14  14 SER A  298  LEU A  308  1                                  11    
HELIX   15  15 ASN A  339  ALA A  343  5                                   5    
HELIX   16  16 SER A  373  VAL A  388  1                                  16    
HELIX   17  17 GLY B   21  ARG B   33  1                                  13    
HELIX   18  18 ALA B   47  VAL B   52  1                                   6    
HELIX   19  19 ASP B   63  LYS B   75  1                                  13    
HELIX   20  20 ALA B   87  GLU B   97  1                                  11    
HELIX   21  21 CYS B  104  MET B  112  1                                   9    
HELIX   22  22 ASN B  113  GLU B  123  1                                  11    
HELIX   23  23 SER B  137  GLY B  149  1                                  13    
HELIX   24  24 SER B  170  GLU B  172  5                                   3    
HELIX   25  25 GLN B  173  GLY B  184  1                                  12    
HELIX   26  26 SER B  240  GLY B  259  1                                  20    
HELIX   27  27 HIS B  285  MET B  289  5                                   5    
HELIX   28  28 VAL B  290  GLN B  295  1                                   6    
HELIX   29  29 SER B  298  LEU B  308  1                                  11    
HELIX   30  30 ASN B  339  ALA B  343  5                                   5    
HELIX   31  31 SER B  373  VAL B  388  1                                  16    
SHEET    1   A 5 ARG A  55  VAL A  58  0                                        
SHEET    2   A 5 GLU A  37  ASP A  42  1  N  ALA A  40   O  ARG A  55           
SHEET    3   A 5 ARG A  14  LEU A  18  1  N  VAL A  15   O  GLU A  37           
SHEET    4   A 5 TYR A  78  PRO A  81  1  O  VAL A  80   N  MET A  16           
SHEET    5   A 5 ASN A 100  VAL A 101  1  O  ASN A 100   N  ILE A  79           
SHEET    1   B 4 TYR A 132  ALA A 135  0                                        
SHEET    2   B 4 VAL A 192  GLY A 196 -1  O  VAL A 194   N  ARG A 133           
SHEET    3   B 4 CYS A 152  PRO A 156 -1  N  ILE A 153   O  GLU A 195           
SHEET    4   B 4 THR A 166  ILE A 168 -1  O  ILE A 168   N  CYS A 152           
SHEET    1   C 4 GLU A 274  SER A 281  0                                        
SHEET    2   C 4 GLY A 262  CYS A 271 -1  N  CYS A 271   O  GLU A 274           
SHEET    3   C 4 PHE A 202  ALA A 211 -1  N  THR A 208   O  PHE A 264           
SHEET    4   C 4 GLY A 214  PHE A 217 -1  O  HIS A 216   N  VAL A 209           
SHEET    1   D 8 GLU A 274  SER A 281  0                                        
SHEET    2   D 8 GLY A 262  CYS A 271 -1  N  CYS A 271   O  GLU A 274           
SHEET    3   D 8 PHE A 202  ALA A 211 -1  N  THR A 208   O  PHE A 264           
SHEET    4   D 8 VAL A 221  GLU A 226 -1  O  VAL A 221   N  THR A 205           
SHEET    5   D 8 ASP A 229  GLN A 235 -1  O  ARG A 231   N  ARG A 224           
SHEET    6   D 8 ALA A 321  ILE A 326 -1  O  SER A 323   N  SER A 233           
SHEET    7   D 8 GLY A 365  THR A 370 -1  O  ALA A 367   N  ALA A 324           
SHEET    8   D 8 LEU A 348  LEU A 352 -1  N  GLN A 349   O  LEU A 368           
SHEET    1   E 2 GLN A 329  SER A 332  0                                        
SHEET    2   E 2 ILE A 358  SER A 361 -1  O  GLY A 360   N  LEU A 330           
SHEET    1   F 2 THR A 336  ASP A 338  0                                        
SHEET    2   F 2 LYS A 389  GLN A 391 -1  O  GLN A 391   N  THR A 336           
SHEET    1   G 4 ARG B  55  VAL B  58  0                                        
SHEET    2   G 4 GLU B  37  ASP B  42  1  N  ALA B  40   O  ARG B  55           
SHEET    3   G 4 ARG B  14  LEU B  18  1  N  VAL B  15   O  GLU B  37           
SHEET    4   G 4 TYR B  78  PRO B  81  1  O  VAL B  80   N  MET B  16           
SHEET    1   H 4 TYR B 132  ALA B 135  0                                        
SHEET    2   H 4 VAL B 192  GLY B 196 -1  O  VAL B 192   N  ALA B 135           
SHEET    3   H 4 CYS B 152  PRO B 156 -1  N  LYS B 155   O  ILE B 193           
SHEET    4   H 4 THR B 166  ILE B 168 -1  O  ILE B 168   N  CYS B 152           
SHEET    1   I 4 GLU B 274  SER B 281  0                                        
SHEET    2   I 4 GLY B 262  CYS B 271 -1  N  CYS B 271   O  GLU B 274           
SHEET    3   I 4 PHE B 202  ALA B 211 -1  N  LEU B 206   O  VAL B 266           
SHEET    4   I 4 GLY B 214  PHE B 217 -1  O  HIS B 216   N  VAL B 209           
SHEET    1   J 8 GLU B 274  SER B 281  0                                        
SHEET    2   J 8 GLY B 262  CYS B 271 -1  N  CYS B 271   O  GLU B 274           
SHEET    3   J 8 PHE B 202  ALA B 211 -1  N  LEU B 206   O  VAL B 266           
SHEET    4   J 8 VAL B 221  GLU B 226 -1  O  VAL B 221   N  THR B 205           
SHEET    5   J 8 ASP B 229  GLN B 235 -1  O  ARG B 231   N  ARG B 224           
SHEET    6   J 8 ALA B 321  ILE B 326 -1  O  SER B 323   N  SER B 233           
SHEET    7   J 8 GLY B 365  THR B 370 -1  O  ALA B 367   N  ALA B 324           
SHEET    8   J 8 LEU B 348  LEU B 352 -1  N  GLN B 349   O  LEU B 368           
SHEET    1   K 2 GLN B 329  SER B 332  0                                        
SHEET    2   K 2 ILE B 358  SER B 361 -1  O  GLY B 360   N  LEU B 330           
SHEET    1   L 2 THR B 336  ASP B 338  0                                        
SHEET    2   L 2 LYS B 389  GLN B 391 -1  O  GLN B 391   N  THR B 336           
LINK         O3B ADP A   1                MG    MG A 393     1555   1555  1.79  
LINK         O2A ADP A   1                MG    MG A 393     1555   1555  1.84  
LINK        MG    MG A 393                 O   HOH A 841     1555   1555  1.73  
LINK        MG    MG A 393                 O   HOH A 485     1555   1555  1.92  
LINK        MG    MG A 393                 OE1 GLU A 279     1555   1555  1.88  
LINK        MG    MG A 393                 OE2 GLU A 267     1555   1555  1.88  
LINK        NA    NA A 394                 O   VAL A 101     1555   1555  2.40  
LINK        NA    NA A 394                 ND2 ASN A 100     1555   1555  2.38  
LINK        NA    NA A 394                 O   PRO A 103     1555   1555  2.42  
LINK        NA    NA A 394                 O   HOH A 821     1555   1555  2.42  
LINK        MG    MG B 393                 OE1AGLU B 279     1555   1555  1.88  
LINK        MG    MG B 393                 OE1BGLU B 267     1555   1555  1.93  
LINK        MG    MG B 393                 O   HOH B 767     1555   1555  1.73  
LINK        MG    MG B 393                 O2A ADP B 397     1555   1555  1.95  
LINK        MG    MG B 393                 O3B ADP B 397     1555   1555  1.70  
LINK        MG    MG B 393                 O   HOH B 470     1555   1555  2.11  
LINK        NA    NA B 394                 O   HOH A 811     1555   1555  2.40  
LINK        NA    NA B 394                 O   HOH A 920     1555   1555  2.51  
LINK         O   HIS B  51                NA    NA B 394     1555   1555  2.63  
LINK        NA    NA B 394                 O   HOH A 505     1555   1555  2.91  
LINK        NA    NA B 394                 O   HOH B 555     1555   1555  2.81  
LINK        NA    NA B 394                 O   HOH A 586     1555   1555  2.85  
LINK        NA    NA A 394                 O   HOH A 445     1555   1555  2.62  
CISPEP   1 VAL A  102    PRO A  103          0        -0.57                     
CISPEP   2 TYR A  150    PRO A  151          0        -2.41                     
CISPEP   3 GLN A  235    PRO A  236          0        -5.00                     
CISPEP   4 VAL B  102    PRO B  103          0        -1.80                     
CISPEP   5 TYR B  150    PRO B  151          0        -1.00                     
CISPEP   6 GLN B  235    PRO B  236          0        -4.36                     
SITE     1 AC1  5 ADP A   1  GLU A 267  GLU A 279  HOH A 485                    
SITE     2 AC1  5 HOH A 841                                                     
SITE     1 AC2  5 GLU B 267  GLU B 279  ADP B 397  HOH B 470                    
SITE     2 AC2  5 HOH B 767                                                     
SITE     1 AC3  8 ALA A  53  HOH A 505  HOH A 586  HOH A 811                    
SITE     2 AC3  8 HOH A 920  MET B  50  HIS B  51  HOH B 555                    
SITE     1 AC4  6 ASN A 100  VAL A 101  PRO A 103  HOH A 432                    
SITE     2 AC4  6 HOH A 445  HOH A 821                                          
SITE     1 AC5  7 ARG A  43  VAL A  58  ARG A 119  ARG A 133                    
SITE     2 AC5  7 PHE A 134  HOH A 699  HOH A 809                               
SITE     1 AC6  4 ARG A  43  THR A 131  TYR A 132  HOH A 468                    
SITE     1 AC7  4 HIS B 216  PHE B 217  HOH B 488  HOH B 644                    
SITE     1 AC8  3 HOH A 415  PHE B 337  GLY B 354                               
SITE     1 AC9 24 ARG A 114  SER A 130  ILE A 153  LYS A 155                    
SITE     2 AC9 24 GLN A 165  GLU A 195  GLY A 196  VAL A 197                    
SITE     3 AC9 24 VAL A 198  PHE A 200  GLU A 203  GLN A 225                    
SITE     4 AC9 24 GLU A 267  PHE A 269  GLU A 279   MG A 393                    
SITE     5 AC9 24 HOH A 465  HOH A 479  HOH A 485  HOH A 552                    
SITE     6 AC9 24 HOH A 556  HOH A 595  HOH A 760  HOH A 841                    
SITE     1 BC1 24 ARG B 114  SER B 130  ILE B 153  LYS B 155                    
SITE     2 BC1 24 GLN B 165  GLU B 195  GLY B 196  VAL B 198                    
SITE     3 BC1 24 GLU B 203  GLN B 225  GLU B 267  PHE B 269                    
SITE     4 BC1 24 GLU B 279   MG B 393  HOH B 470  HOH B 492                    
SITE     5 BC1 24 HOH B 505  HOH B 582  HOH B 604  HOH B 756                    
SITE     6 BC1 24 HOH B 761  HOH B 767  HOH B 775  HOH B 776                    
SITE     1 BC2 12 ASP A  46  MET A  50  HIS A  51  ARG A  55                    
SITE     2 BC2 12 SER A  56  GLU A 143  HOH A 460  HOH A 500                    
SITE     3 BC2 12 HOH A 509  HOH A 688  LEU B   8  HIS B  54                    
SITE     1 BC3  6 LEU A  34  ARG A 305  HOH A 438  HOH A 629                    
SITE     2 BC3  6 GLN B 349  ILE B 350                                          
SITE     1 BC4 11 EDO A 406  HOH A 506  HOH A 514  GLU B  30                    
SITE     2 BC4 11 ARG B  33  ASP B 296  LEU B 297  SER B 298                    
SITE     3 BC4 11 ALA B 301  HOH B 406  HOH B 482                               
SITE     1 BC5  3 ILE A 378  HOH A 934  HOH B 627                               
SITE     1 BC6  9 GLY B  21  GLU B  22  LEU B  23  GLY B  24                    
SITE     2 BC6  9 GLU B  82  HOH B 576  HOH B 709  HOH B 714                    
SITE     3 BC6  9 HOH B 807                                                     
SITE     1 BC7  5 ARG A 246  GLU A 274  VAL A 275  HOH A 585                    
SITE     2 BC7  5 HOH A 680                                                     
SITE     1 BC8  4 ARG A  69  HOH A 542  HOH A 578  HOH A 877                    
SITE     1 BC9  6 THR A   2  LEU A   3  TYR A  78  HOH A 549                    
SITE     2 BC9  6 HOH A 700  HOH A 765                                          
SITE     1 CC1  6 PRO B 328  GLN B 329  LEU B 330  VAL B 390                    
SITE     2 CC1  6 HOH B 409  HOH B 483                                          
SITE     1 CC2  8 ASN A  60  ASP A  63  ALA A 122  THR A 129                    
SITE     2 CC2  8 TYR A 132  HOH A 568  HOH A 571  HOH A 898                    
SITE     1 CC3  7 GLU A 379  HIS A 383  HOH A 456  HOH A 675                    
SITE     2 CC3  7 HOH A 803  HOH A 947  HOH A 948                               
SITE     1 CC4  5 ARG A 231  HOH A 497  HOH A 589  HOH A 915                    
SITE     2 CC4  5 HOH A 927                                                     
SITE     1 CC5  6 PHE B 134  ALA B 135  LEU B 140  ALA B 144                    
SITE     2 CC5  6 HOH B 655  HOH B 787                                          
SITE     1 CC6  5 LEU B 244  GLU B 245  GLN B 248  HOH B 559                    
SITE     2 CC6  5 HOH B 583                                                     
SITE     1 CC7 10 LEU A 292  ILE A 293  GLN A 349  ARG A 351                    
SITE     2 CC7 10 HOH A 452  HOH A 478  HOH A 514  HOH A 843                    
SITE     3 CC7 10 ASP B 296  EDO B 398                                          
SITE     1 CC8  4 GLY A  64  ALA A  87  MET A  90  GLN A  93                    
CRYST1   62.350  179.340   75.620  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      0.016038  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005576  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013224        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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