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Database: PDB
Entry: 1KJI
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HEADER    TRANSFERASE                             04-DEC-01   1KJI              
TITLE     CRYSTAL STRUCTURE OF GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE IN     
TITLE    2 COMPLEX WITH MG-AMPPCP                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE 2;             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GART 2; GAR TRANSFORMYLASE 2; 5'-PHOSPHORIBOSYLGLYCINAMIDE; 
COMPND   5 EC: 2.1.2.-;                                                         
COMPND   6 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   4   11-OCT-17 1KJI    1       REMARK                                   
REVDAT   3   24-FEB-09 1KJI    1       VERSN                                    
REVDAT   2   01-APR-03 1KJI    1       JRNL                                     
REVDAT   1   28-JUN-02 1KJI    0                                                
JRNL        AUTH   J.B.THODEN,S.M.FIRESTINE,S.J.BENKOVIC,H.M.HOLDEN             
JRNL        TITL   PURT-ENCODED GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE.      
JRNL        TITL 2 ACCOMMODATION OF ADENOSINE NUCLEOTIDE ANALOGS WITHIN THE     
JRNL        TITL 3 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   2                                                                      
REMARK   2 RESOLUTION.    1.60 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) : 1.60                           
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             : 105396                         
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) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 10541                           
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.1840                 
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) : 105396                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5930                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 87                                      
REMARK   3   SOLVENT ATOMS            : 944                                     
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) : 0.011 ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : 2.350 ; 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 1KJI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-01.                  
REMARK 100 THE DEPOSITION ID IS D_1000015015.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 6.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GOEBEL OPTICS                      
REMARK 200  OPTICS                         : GOEBEL OPTICS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS HI-STAR                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : FRAMBO                             
REMARK 200  DATA SCALING SOFTWARE          : SAINT                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 105396                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
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                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.04600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
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   (%): 50.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 5000, NACL, MGCL2, MOPS, AMPPCP,     
REMARK 280  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       31.10000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       89.60000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.10000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       89.60000            
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: 7610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 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     GLY A   188                                                      
REMARK 465     ALA A   189                                                      
REMARK 465     GLY B   188                                                      
REMARK 465     ALA B   189                                                      
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   582     O    HOH A   754              2.10            
REMARK 500   O    LEU B   125     O    HOH B   694              2.15            
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   NH2  ARG B   191     NH2  ARG B   191     2555     2.01            
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  72   CD    GLU A  72   OE2     0.072                       
REMARK 500    GLU A  96   CD    GLU A  96   OE2     0.071                       
REMARK 500    GLU A 138   CD    GLU A 138   OE2     0.067                       
REMARK 500    GLU A 274   CD    GLU A 274   OE2     0.068                       
REMARK 500    GLU A 279   CD    GLU A 279   OE2     0.067                       
REMARK 500    GLU B  82   CD    GLU B  82   OE2     0.072                       
REMARK 500    GLU B  96   CD    GLU B  96   OE2     0.082                       
REMARK 500    GLU B  97   CD    GLU B  97   OE2     0.068                       
REMARK 500    GLU B 143   CD    GLU B 143   OE2     0.075                       
REMARK 500    GLU B 172   CD    GLU B 172   OE2     0.069                       
REMARK 500    GLU B 195   CD    GLU B 195   OE2     0.069                       
REMARK 500    GLU B 226   CD    GLU B 226   OE2     0.068                       
REMARK 500    GLU B 245   CD    GLU B 245   OE2     0.071                       
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    ARG A   9   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP A  89   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    CYS A 104   N   -  CA  -  CB  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ASP A 136   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    ARG A 186   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 191   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ASP A 201   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP A 201   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    ASP A 213   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 227   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 227   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ASP A 229   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG A 246   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 252   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ASP A 286   CB  -  CG  -  OD1 ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ASP A 286   CB  -  CG  -  OD2 ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    ASP A 296   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A 347   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ASP A 359   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG A 362   CG  -  CD  -  NE  ANGL. DEV. =  17.7 DEGREES          
REMARK 500    ARG A 362   CD  -  NE  -  CZ  ANGL. DEV. =  11.5 DEGREES          
REMARK 500    ARG A 362   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ARG A 362   NE  -  CZ  -  NH2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ASP A 376   CB  -  CG  -  OD2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ARG A 380   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 380   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG B  33   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ASP B  42   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG B  69   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ASP B  89   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP B  89   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    CYS B 104   N   -  CA  -  CB  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    ARG B 142   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ASP B 147   CB  -  CG  -  OD1 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    ASP B 147   CB  -  CG  -  OD2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ARG B 191   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B 191   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP B 201   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP B 201   CB  -  CG  -  OD2 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    GLU B 203   CB  -  CA  -  C   ANGL. DEV. = -14.1 DEGREES          
REMARK 500    ASP B 286   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP B 296   CB  -  CG  -  OD1 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ASP B 296   CB  -  CG  -  OD2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ARG B 363   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG B 363   NE  -  CZ  -  NH2 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       -9.67     81.02                                   
REMARK 500    ALA A  87       73.13    -66.34                                   
REMARK 500    GLU A  97        7.91    -66.73                                   
REMARK 500    ARG A 186      -19.41    -18.76                                   
REMARK 500    SER A 278      -63.94   -109.79                                   
REMARK 500    ARG A 283      175.59    174.09                                   
REMARK 500    LEU A 330     -179.78   -171.69                                   
REMARK 500    ASN A 334       60.64   -160.65                                   
REMARK 500    ASP A 359       73.20   -153.19                                   
REMARK 500    LEU B   8       -9.13     82.47                                   
REMARK 500    ALA B  85       62.85    -66.62                                   
REMARK 500    GLU B 123      -72.06    -84.38                                   
REMARK 500    SER B 161       21.44     48.06                                   
REMARK 500    LEU B 174      -39.91    -38.38                                   
REMARK 500    ARG B 186      -62.38    -92.10                                   
REMARK 500    SER B 278      -63.71   -103.70                                   
REMARK 500    ARG B 283      175.88    177.60                                   
REMARK 500    TYR B 318       40.96    -94.43                                   
REMARK 500    ASN B 334       56.52   -154.22                                   
REMARK 500    ASP B 359       74.06   -154.53                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 393  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ACP A   1   O3G                                                    
REMARK 620 2 ACP A   1   O2B  89.8                                              
REMARK 620 3 HOH A 509   O   107.7  96.7                                        
REMARK 620 4 GLU A 279   OE1  93.2  87.2 158.6                                  
REMARK 620 5 GLU A 279   OE2 148.0  90.4 104.0  54.9                            
REMARK 620 6 HOH A 536   O    93.1 168.8  92.6  81.9  81.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 394  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ACP A   1   O2A                                                    
REMARK 620 2 GLU A 267   OE1 151.0                                              
REMARK 620 3 GLU A 267   OE2  94.0  57.1                                        
REMARK 620 4 GLU A 279   OE1  86.7  88.2  84.8                                  
REMARK 620 5 HOH A 465   O    85.3  95.5  88.8 169.3                            
REMARK 620 6 ACP A   1   O2G 116.0  92.9 150.0  95.7  94.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 395  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 521   O                                                      
REMARK 620 2 HOH B 651   O   162.4                                              
REMARK 620 3 HOH B 456   O    95.4 101.3                                        
REMARK 620 4 ALA A  53   O    89.3  80.2 145.0                                  
REMARK 620 5 ALA B  53   O    74.4 103.9  77.0 137.1                            
REMARK 620 6 HOH B 745   O    84.5  80.3 131.9  83.0  56.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 396  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 637   O                                                      
REMARK 620 2 GLU A  95   OE1 119.9                                              
REMARK 620 3 HOH A 567   O   115.4 111.5                                        
REMARK 620 N                    1     2                                         
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 ACP B 396   O3G                                                    
REMARK 620 2 GLU B 279   OE1  97.8                                              
REMARK 620 3 ACP B 396   O2B  80.6 105.7                                        
REMARK 620 4 HOH B 547   O    95.7 163.0  86.6                                  
REMARK 620 5 HOH B 470   O    89.3  83.5 167.1  86.4                            
REMARK 620 6 GLU B 279   OE2 157.1  60.6 111.1 104.4  81.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 394  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 635   O                                                      
REMARK 620 2 ACP B 396   O2G  95.2                                              
REMARK 620 3 GLU B 267   OE1  92.5  88.9                                        
REMARK 620 4 ACP B 396   O2A 102.1 122.4 143.4                                  
REMARK 620 5 GLU B 279   OE1 165.6  89.2  73.9  86.9                            
REMARK 620 6 GLU B 267   OE2  75.4 136.6  50.3 100.9  92.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 395  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL B 101   O                                                      
REMARK 620 2 PRO B 103   O    82.2                                              
REMARK 620 3 ASN B 100   ND2  91.0 156.3                                        
REMARK 620 4 HOH B 690   O   150.2  87.0 108.9                                  
REMARK 620 5 HOH B 461   O    74.1 125.6  73.1  90.3                            
REMARK 620 N                    1     2     3     4                             
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                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 394                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 393                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 394                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 395                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 396                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 395                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 397                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP B 396                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPO A 398                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 399                 
DBREF  1KJI A    2   392  UNP    P33221   PURT_ECOLI       1    391             
DBREF  1KJI 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  A 394       1                                                       
HET     NA  A 395       1                                                       
HET     NA  A 396       1                                                       
HET     CL  A 397       1                                                       
HET    ACP  A   1      31                                                       
HET    MPO  A 398      13                                                       
HET    EDO  A 399       4                                                       
HET     MG  B 393       1                                                       
HET     MG  B 394       1                                                       
HET     NA  B 395       1                                                       
HET    ACP  B 396      31                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER                     
HETNAM     MPO 3[N-MORPHOLINO]PROPANE SULFONIC ACID                             
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE                 
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3   MG    4(MG 2+)                                                     
FORMUL   5   NA    3(NA 1+)                                                     
FORMUL   7   CL    CL 1-                                                        
FORMUL   8  ACP    2(C11 H18 N5 O12 P3)                                         
FORMUL   9  MPO    C7 H15 N O4 S                                                
FORMUL  10  EDO    C2 H6 O2                                                     
FORMUL  15  HOH   *944(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  MET A  112  1                                   9    
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  184  1                                  12    
HELIX   10  10 SER A  240  GLY A  259  1                                  20    
HELIX   11  11 HIS A  285  MET A  289  5                                   5    
HELIX   12  12 VAL A  290  GLN A  295  1                                   6    
HELIX   13  13 SER A  298  LEU A  308  1                                  11    
HELIX   14  14 ASN A  339  ALA A  343  5                                   5    
HELIX   15  15 SER A  373  VAL A  388  1                                  16    
HELIX   16  16 GLY B   21  ARG B   33  1                                  13    
HELIX   17  17 ALA B   47  VAL B   52  1                                   6    
HELIX   18  18 ASP B   63  LYS B   75  1                                  13    
HELIX   19  19 ALA B   87  GLU B   97  1                                  11    
HELIX   20  20 CYS B  104  MET B  112  1                                   9    
HELIX   21  21 ASN B  113  GLU B  123  1                                  11    
HELIX   22  22 SER B  137  GLY B  149  1                                  13    
HELIX   23  23 SER B  170  GLU B  172  5                                   3    
HELIX   24  24 GLN B  173  GLY B  184  1                                  12    
HELIX   25  25 SER B  240  GLY B  259  1                                  20    
HELIX   26  26 HIS B  285  MET B  289  5                                   5    
HELIX   27  27 VAL B  290  GLN B  295  1                                   6    
HELIX   28  28 SER B  298  LEU B  308  1                                  11    
HELIX   29  29 ASN B  339  ALA B  343  5                                   5    
HELIX   30  30 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  LEU A  17   O  ILE A  39           
SHEET    4   A 5 TYR A  78  PRO A  81  1  O  TYR A  78   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  LYS A 155   O  ILE A 193           
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  LEU A 206   O  VAL A 266           
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  LEU A 206   O  VAL A 266           
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 194   N  ARG B 133           
SHEET    3   H 4 CYS B 152  PRO B 156 -1  N  ILE B 153   O  GLU B 195           
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  PHE B 269   O  ILE B 276           
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  GLY B 214   N  ALA B 211           
SHEET    1   J 8 GLU B 274  SER B 281  0                                        
SHEET    2   J 8 GLY B 262  CYS B 271 -1  N  PHE B 269   O  ILE B 276           
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 369   N  ALA B 322           
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  LYS B 389   N  ASP B 338           
LINK         O3G ACP A   1                MG    MG A 393     1555   1555  2.05  
LINK         O2B ACP A   1                MG    MG A 393     1555   1555  1.96  
LINK        MG    MG A 393                 O   HOH A 509     1555   1555  1.84  
LINK        MG    MG A 393                 OE1 GLU A 279     1555   1555  2.38  
LINK        MG    MG A 393                 OE2 GLU A 279     1555   1555  2.46  
LINK        MG    MG A 393                 O   HOH A 536     1555   1555  2.54  
LINK        MG    MG A 394                 O2A ACP A   1     1555   1555  2.08  
LINK        MG    MG A 394                 OE1 GLU A 267     1555   1555  2.24  
LINK        MG    MG A 394                 OE2 GLU A 267     1555   1555  2.36  
LINK        MG    MG A 394                 OE1 GLU A 279     1555   1555  2.12  
LINK        MG    MG A 394                 O   HOH A 465     1555   1555  2.20  
LINK        MG    MG A 394                 O2G ACP A   1     1555   1555  2.10  
LINK        NA    NA A 395                 O   HOH A 521     1555   1555  2.42  
LINK        NA    NA A 395                 O   HOH B 651     1555   1555  2.38  
LINK        NA    NA A 395                 O   HOH B 456     1555   1555  2.47  
LINK        NA    NA A 396                 O   HOH A 637     1555   1555  2.58  
LINK        MG    MG B 393                 O3G ACP B 396     1555   1555  2.10  
LINK        MG    MG B 393                 OE1 GLU B 279     1555   1555  2.11  
LINK        MG    MG B 393                 O2B ACP B 396     1555   1555  2.05  
LINK        MG    MG B 393                 O   HOH B 547     1555   1555  1.71  
LINK        MG    MG B 393                 O   HOH B 470     1555   1555  2.85  
LINK        MG    MG B 393                 OE2 GLU B 279     1555   1555  2.27  
LINK        MG    MG B 394                 O   HOH B 635     1555   1555  2.45  
LINK        MG    MG B 394                 O2G ACP B 396     1555   1555  1.90  
LINK        MG    MG B 394                 OE1 GLU B 267     1555   1555  2.81  
LINK        MG    MG B 394                 O2A ACP B 396     1555   1555  1.85  
LINK        MG    MG B 394                 OE1 GLU B 279     1555   1555  2.27  
LINK        MG    MG B 394                 OE2 GLU B 267     1555   1555  2.29  
LINK        NA    NA B 395                 O   VAL B 101     1555   1555  2.48  
LINK        NA    NA B 395                 O   PRO B 103     1555   1555  2.49  
LINK        NA    NA B 395                 ND2 ASN B 100     1555   1555  2.47  
LINK        NA    NA B 395                 O   HOH B 690     1555   1555  2.46  
LINK         O   ALA A  53                NA    NA A 395     1555   1555  2.68  
LINK         OE1 GLU A  95                NA    NA A 396     1555   1555  2.69  
LINK         O   ALA B  53                NA    NA A 395     1555   1555  2.98  
LINK        NA    NA A 395                 O   HOH B 745     1555   1555  2.88  
LINK        NA    NA A 396                 O   HOH A 567     1555   1555  2.64  
LINK        NA    NA B 395                 O   HOH B 461     1555   1555  2.92  
CISPEP   1 VAL A  102    PRO A  103          0        -0.66                     
CISPEP   2 TYR A  150    PRO A  151          0        -0.70                     
CISPEP   3 GLN A  235    PRO A  236          0        -2.33                     
CISPEP   4 VAL B  102    PRO B  103          0         1.35                     
CISPEP   5 TYR B  150    PRO B  151          0        -1.29                     
CISPEP   6 GLN B  235    PRO B  236          0        -1.25                     
SITE     1 AC1  4 ACP A   1  GLU A 279  HOH A 509  HOH A 536                    
SITE     1 AC2  4 ACP A   1  GLU A 267  GLU A 279  HOH A 465                    
SITE     1 AC3  4 GLU B 279  ACP B 396  HOH B 470  HOH B 547                    
SITE     1 AC4  4 GLU B 267  GLU B 279  ACP B 396  HOH B 635                    
SITE     1 AC5  7 ALA A  53  HOH A 453  HOH A 521  ALA B  53                    
SITE     2 AC5  7 HOH B 456  HOH B 651  HOH B 745                               
SITE     1 AC6  5 GLU A  95  ASN A 100  VAL A 101  HOH A 567                    
SITE     2 AC6  5 HOH A 637                                                     
SITE     1 AC7  5 ASN B 100  VAL B 101  PRO B 103  HOH B 461                    
SITE     2 AC7  5 HOH B 690                                                     
SITE     1 AC8  6 ARG A  43  VAL A  58  ARG A 119  ARG A 133                    
SITE     2 AC8  6 PHE A 134  HOH A 590                                          
SITE     1 AC9 26 ARG A 114  ILE A 153  LYS A 155  SER A 160                    
SITE     2 AC9 26 SER A 161  GLY A 162  GLN A 165  GLU A 195                    
SITE     3 AC9 26 GLY A 196  VAL A 198  GLU A 203  GLN A 225                    
SITE     4 AC9 26 GLU A 267  PHE A 269  GLU A 279   MG A 393                    
SITE     5 AC9 26  MG A 394  HOH A 432  HOH A 465  HOH A 475                    
SITE     6 AC9 26 HOH A 485  HOH A 509  HOH A 562  HOH A 563                    
SITE     7 AC9 26 HOH A 644  HOH A 758                                          
SITE     1 BC1 20 ARG B 114  SER B 130  LYS B 155  SER B 159                    
SITE     2 BC1 20 SER B 160  SER B 161  GLY B 162  GLU B 195                    
SITE     3 BC1 20 GLY B 196  VAL B 198  GLU B 203  GLU B 267                    
SITE     4 BC1 20 GLU B 279   MG B 393   MG B 394  HOH B 547                    
SITE     5 BC1 20 HOH B 553  HOH B 572  HOH B 635  HOH B 767                    
SITE     1 BC2 13 ASP A  46  MET A  50  HIS A  51  ARG A  55                    
SITE     2 BC2 13 SER A  56  GLU A 143  HOH A 437  HOH A 453                    
SITE     3 BC2 13 HOH A 468  HOH A 685  HOH A 727  LEU B   8                    
SITE     4 BC2 13 HIS B  54                                                     
SITE     1 BC3  6 ASP A  63  THR A 129  SER A 130  THR A 131                    
SITE     2 BC3  6 TYR A 132  HOH A 502                                          
CRYST1   62.200  179.200   76.200  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      0.016077  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005580  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013123        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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