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Database: PDB
Entry: 1CQI
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HEADER    LIGASE                                  06-AUG-99   1CQI              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX OF ADP AND MG2+ WITH DEPHOSPHORYLATED
TITLE    2 E. COLI SUCCINYL-COA SYNTHETASE                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (SUCCINYL-COA SYNTHETASE ALPHA CHAIN);             
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 FRAGMENT: ALPHA SUBUNIT;                                             
COMPND   5 SYNONYM: SCS-ALPHA;                                                  
COMPND   6 EC: 6.2.1.5;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PROTEIN (SUCCINYL-COA SYNTHETASE BETA CHAIN);              
COMPND  10 CHAIN: B, E;                                                         
COMPND  11 FRAGMENT: BETA SUBUNIT;                                              
COMPND  12 SYNONYM: SCS-BETA;                                                   
COMPND  13 EC: 6.2.1.5;                                                         
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   8 ORGANISM_TAXID: 562;                                                 
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ATP-GRASP FOLD, ROSSMANN FOLD, LIGASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.JOYCE,M.E.FRASER,M.N.G.JAMES,W.A.BRIDGER,W.T.WOLODKO              
REVDAT   4   04-OCT-17 1CQI    1       REMARK                                   
REVDAT   3   24-FEB-09 1CQI    1       VERSN                                    
REVDAT   2   01-APR-03 1CQI    1       JRNL                                     
REVDAT   1   07-JAN-00 1CQI    0                                                
JRNL        AUTH   M.A.JOYCE,M.E.FRASER,M.N.JAMES,W.A.BRIDGER,W.T.WOLODKO       
JRNL        TITL   ADP-BINDING SITE OF ESCHERICHIA COLI SUCCINYL-COA SYNTHETASE 
JRNL        TITL 2 REVEALED BY X-RAY CRYSTALLOGRAPHY.                           
JRNL        REF    BIOCHEMISTRY                  V.  39    17 2000              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   10625475                                                     
JRNL        DOI    10.1021/BI991696F                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.E.FRASER,M.N.G.JAMES,W.A.BRIDGER,W.T.WOLODKO               
REMARK   1  TITL   A DETAILED STRUCTURAL DESCRIPTION OF ESCHERICHIA COLI        
REMARK   1  TITL 2 SUCCINYL-COA SYNTHETASE                                      
REMARK   1  REF    J.MOL.BIOL.                   V. 285  1633 1999              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  DOI    10.1006/JMBI.1998.2324                                       
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   W.T.WOLODKO,M.E.FRASER,M.N.G.JAMES,W.A.BRIDGER               
REMARK   1  TITL   THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM        
REMARK   1  TITL 2 ESCHERICHIA COLI AT 2.5A RESOLUTION                          
REMARK   1  REF    J.BIOL.CHEM.                  V. 269 10883 1994              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   W.T.WOLODKO,M.N.G.JAMES,W.A.BRIDGER                          
REMARK   1  TITL   CRYSTALLIZATION OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA  
REMARK   1  TITL 2 COLI                                                         
REMARK   1  REF    J.BIOL.CHEM.                  V. 259  5316 1984              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 31753                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.247                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.900                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 3470                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.51                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4543                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2900                       
REMARK   3   BIN FREE R VALUE                    : 0.3380                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 11.20                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 575                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.014                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9892                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 162                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.34                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.42                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 20.0                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.46                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.51                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.017                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.900                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.100                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : GROUP                                     
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.22                                                 
REMARK   3   BSOL        : 10.00                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: MAXIMUM LIKELIHOOD REFINEMENT IN CNS      
REMARK   4                                                                      
REMARK   4 1CQI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000009487.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUN-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 283.0                              
REMARK 200  PH                             : 7.30                               
REMARK 200  NUMBER OF CRYSTALS USED        : 6                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : FUJI                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : WEIS                               
REMARK 200  DATA SCALING SOFTWARE          : SCALKB2, KBAPLY                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31753                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.16400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: BIOMOL                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, POTASSIUM PHOSPHATE,   
REMARK 280  COENZYME A, PH 7.30, VAPOR DIFFUSION, HANGING DROP                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z+1/2                                             
REMARK 290       7555   Y,X,-Z+1/4                                              
REMARK 290       8555   -Y,-X,-Z+3/4                                            
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      203.57500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      305.36250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      101.78750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      203.57500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      101.78750            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      305.36250            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E                            
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 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    CYS A  77   CB    CYS A  77   SG     -0.107                       
REMARK 500    CYS E  47   CB    CYS E  47   SG     -0.137                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A  82   CA  -  CB  -  CG  ANGL. DEV. = -14.9 DEGREES          
REMARK 500    PRO B  92   C   -  N   -  CA  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    PRO E  92   C   -  N   -  CA  ANGL. DEV. =   9.5 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   3      -62.74     60.00                                   
REMARK 500    LYS A   6      -18.91    -40.22                                   
REMARK 500    SER A  18      -75.28    -52.76                                   
REMARK 500    HIS A  47      -79.11   -113.83                                   
REMARK 500    LEU A  48       51.48   -102.54                                   
REMARK 500    ALA A  61      -72.63    -84.16                                   
REMARK 500    THR A  96      140.32    -23.28                                   
REMARK 500    GLU A 113      -33.81    -39.90                                   
REMARK 500    ASN A 122       84.38     73.83                                   
REMARK 500    PRO A 124     -128.15    -95.07                                   
REMARK 500    PHE A 169      -66.84    -22.52                                   
REMARK 500    ASN A 186     -167.07   -112.92                                   
REMARK 500    GLU A 195      -52.44    -29.77                                   
REMARK 500    SER A 212       19.86   -158.53                                   
REMARK 500    ALA A 218      -70.48    -47.49                                   
REMARK 500    ALA A 249       68.70   -107.58                                   
REMARK 500    ALA A 267        1.63    -52.10                                   
REMARK 500    LEU A 276       22.44    -64.72                                   
REMARK 500    THR A 285       49.98    -76.67                                   
REMARK 500    ALA B  88      -34.29    -36.26                                   
REMARK 500    THR B 140       57.28   -143.40                                   
REMARK 500    PRO B 141      -17.22    -49.46                                   
REMARK 500    GLN B 206        4.34    -63.52                                   
REMARK 500    LEU B 255     -160.54   -116.19                                   
REMARK 500    HIS B 279       40.16   -103.27                                   
REMARK 500    ASN B 285      171.93    178.12                                   
REMARK 500    ALA B 293       65.16    -60.32                                   
REMARK 500    LYS B 303      -38.22    -37.96                                   
REMARK 500    ALA B 313      148.86    177.15                                   
REMARK 500    CYS B 325       -2.82    -44.06                                   
REMARK 500    SER B 364      -32.98    -37.88                                   
REMARK 500    LEU B 366     -169.30    -78.77                                   
REMARK 500    ALA B 378      -72.12    -57.05                                   
REMARK 500    ALA B 384       28.82    -66.37                                   
REMARK 500    LEU D   3      -60.35     57.31                                   
REMARK 500    LYS D   6      -18.20    -40.76                                   
REMARK 500    SER D  18      -74.46    -51.50                                   
REMARK 500    HIS D  47      -79.44   -114.45                                   
REMARK 500    LEU D  48       50.83   -101.54                                   
REMARK 500    ALA D  61      -75.51    -86.04                                   
REMARK 500    ALA D  62      -11.64    -47.25                                   
REMARK 500    THR D  96      138.99    -18.55                                   
REMARK 500    GLU D 113      -36.29    -39.53                                   
REMARK 500    ASN D 122       85.41     75.26                                   
REMARK 500    PRO D 124     -130.87    -97.95                                   
REMARK 500    PHE D 169      -68.27    -20.52                                   
REMARK 500    ASN D 186     -162.78   -107.60                                   
REMARK 500    ILE D 209      170.23    -56.60                                   
REMARK 500    SER D 212       20.07   -157.40                                   
REMARK 500    ALA D 218      -72.84    -49.94                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      69 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR B 158         0.07    SIDE CHAIN                              
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 B 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 199   O                                                      
REMARK 620 2 ADP B 801   O3B 139.8                                              
REMARK 620 3 ASP B 213   OD2  66.3  75.9                                        
REMARK 620 4 ADP B 801   O2A  87.5  66.9  70.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN E 199   O                                                      
REMARK 620 2 ADP E 802   O3B 139.0                                              
REMARK 620 3 ASP E 213   OD2  65.7  74.4                                        
REMARK 620 4 ADP E 802   O2A  89.2  69.9  73.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA D 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 802                 
DBREF  1CQI A    1   286  UNP    P07459   SUCD_ECOLI       2    287             
DBREF  1CQI D    1   286  UNP    P07459   SUCD_ECOLI       2    287             
DBREF  1CQI B    1   385  UNP    P07460   SUCC_ECOLI       1    385             
DBREF  1CQI E    1   385  UNP    P07460   SUCC_ECOLI       1    385             
SEQRES   1 A  286  SER ILE LEU ILE ASP LYS ASN THR LYS VAL ILE CYS GLN          
SEQRES   2 A  286  GLY PHE THR GLY SER GLN GLY THR PHE HIS SER GLU GLN          
SEQRES   3 A  286  ALA ILE ALA TYR GLY THR LYS MET VAL GLY GLY VAL THR          
SEQRES   4 A  286  PRO GLY LYS GLY GLY THR THR HIS LEU GLY LEU PRO VAL          
SEQRES   5 A  286  PHE ASN THR VAL ARG GLU ALA VAL ALA ALA THR GLY ALA          
SEQRES   6 A  286  THR ALA SER VAL ILE TYR VAL PRO ALA PRO PHE CYS LYS          
SEQRES   7 A  286  ASP SER ILE LEU GLU ALA ILE ASP ALA GLY ILE LYS LEU          
SEQRES   8 A  286  ILE ILE THR ILE THR GLU GLY ILE PRO THR LEU ASP MET          
SEQRES   9 A  286  LEU THR VAL LYS VAL LYS LEU ASP GLU ALA GLY VAL ARG          
SEQRES  10 A  286  MET ILE GLY PRO ASN CYS PRO GLY VAL ILE THR PRO GLY          
SEQRES  11 A  286  GLU CYS LYS ILE GLY ILE GLN PRO GLY HIS ILE HIS LYS          
SEQRES  12 A  286  PRO GLY LYS VAL GLY ILE VAL SER ARG SER GLY THR LEU          
SEQRES  13 A  286  THR TYR GLU ALA VAL LYS GLN THR THR ASP TYR GLY PHE          
SEQRES  14 A  286  GLY GLN SER THR CYS VAL GLY ILE GLY GLY ASP PRO ILE          
SEQRES  15 A  286  PRO GLY SER ASN PHE ILE ASP ILE LEU GLU MET PHE GLU          
SEQRES  16 A  286  LYS ASP PRO GLN THR GLU ALA ILE VAL MET ILE GLY GLU          
SEQRES  17 A  286  ILE GLY GLY SER ALA GLU GLU GLU ALA ALA ALA TYR ILE          
SEQRES  18 A  286  LYS GLU HIS VAL THR LYS PRO VAL VAL GLY TYR ILE ALA          
SEQRES  19 A  286  GLY VAL THR ALA PRO LYS GLY LYS ARG MET GLY HIS ALA          
SEQRES  20 A  286  GLY ALA ILE ILE ALA GLY GLY LYS GLY THR ALA ASP GLU          
SEQRES  21 A  286  LYS PHE ALA ALA LEU GLU ALA ALA GLY VAL LYS THR VAL          
SEQRES  22 A  286  ARG SER LEU ALA ASP ILE GLY GLU ALA LEU LYS THR VAL          
SEQRES   1 B  385  MET ASN LEU HIS GLU TYR GLN ALA LYS GLN LEU PHE ALA          
SEQRES   2 B  385  ARG TYR GLY LEU PRO ALA PRO VAL GLY TYR ALA CYS THR          
SEQRES   3 B  385  THR PRO ARG GLU ALA GLU GLU ALA ALA SER LYS ILE GLY          
SEQRES   4 B  385  ALA GLY PRO TRP VAL VAL LYS CYS GLN VAL HIS ALA GLY          
SEQRES   5 B  385  GLY ARG GLY LYS ALA GLY GLY VAL LYS VAL VAL ASN SER          
SEQRES   6 B  385  LYS GLU ASP ILE ARG ALA PHE ALA GLU ASN TRP LEU GLY          
SEQRES   7 B  385  LYS ARG LEU VAL THR TYR GLN THR ASP ALA ASN GLY GLN          
SEQRES   8 B  385  PRO VAL ASN GLN ILE LEU VAL GLU ALA ALA THR ASP ILE          
SEQRES   9 B  385  ALA LYS GLU LEU TYR LEU GLY ALA VAL VAL ASP ARG SER          
SEQRES  10 B  385  SER ARG ARG VAL VAL PHE MET ALA SER THR GLU GLY GLY          
SEQRES  11 B  385  VAL GLU ILE GLU LYS VAL ALA GLU GLU THR PRO HIS LEU          
SEQRES  12 B  385  ILE HIS LYS VAL ALA LEU ASP PRO LEU THR GLY PRO MET          
SEQRES  13 B  385  PRO TYR GLN GLY ARG GLU LEU ALA PHE LYS LEU GLY LEU          
SEQRES  14 B  385  GLU GLY LYS LEU VAL GLN GLN PHE THR LYS ILE PHE MET          
SEQRES  15 B  385  GLY LEU ALA THR ILE PHE LEU GLU ARG ASP LEU ALA LEU          
SEQRES  16 B  385  ILE GLU ILE ASN PRO LEU VAL ILE THR LYS GLN GLY ASP          
SEQRES  17 B  385  LEU ILE CYS LEU ASP GLY LYS LEU GLY ALA ASP GLY ASN          
SEQRES  18 B  385  ALA LEU PHE ARG GLN PRO ASP LEU ARG GLU MET ARG ASP          
SEQRES  19 B  385  GLN SER GLN GLU ASP PRO ARG GLU ALA GLN ALA ALA GLN          
SEQRES  20 B  385  TRP GLU LEU ASN TYR VAL ALA LEU ASP GLY ASN ILE GLY          
SEQRES  21 B  385  CYS MET VAL ASN GLY ALA GLY LEU ALA MET GLY THR MET          
SEQRES  22 B  385  ASP ILE VAL LYS LEU HIS GLY GLY GLU PRO ALA ASN PHE          
SEQRES  23 B  385  LEU ASP VAL GLY GLY GLY ALA THR LYS GLU ARG VAL THR          
SEQRES  24 B  385  GLU ALA PHE LYS ILE ILE LEU SER ASP ASP LYS VAL LYS          
SEQRES  25 B  385  ALA VAL LEU VAL ASN ILE PHE GLY GLY ILE VAL ARG CYS          
SEQRES  26 B  385  ASP LEU ILE ALA ASP GLY ILE ILE GLY ALA VAL ALA GLU          
SEQRES  27 B  385  VAL GLY VAL ASN VAL PRO VAL VAL VAL ARG LEU GLU GLY          
SEQRES  28 B  385  ASN ASN ALA GLU LEU GLY ALA LYS LYS LEU ALA ASP SER          
SEQRES  29 B  385  GLY LEU ASN ILE ILE ALA ALA LYS GLY LEU THR ASP ALA          
SEQRES  30 B  385  ALA GLN GLN VAL VAL ALA ALA VAL                              
SEQRES   1 D  286  SER ILE LEU ILE ASP LYS ASN THR LYS VAL ILE CYS GLN          
SEQRES   2 D  286  GLY PHE THR GLY SER GLN GLY THR PHE HIS SER GLU GLN          
SEQRES   3 D  286  ALA ILE ALA TYR GLY THR LYS MET VAL GLY GLY VAL THR          
SEQRES   4 D  286  PRO GLY LYS GLY GLY THR THR HIS LEU GLY LEU PRO VAL          
SEQRES   5 D  286  PHE ASN THR VAL ARG GLU ALA VAL ALA ALA THR GLY ALA          
SEQRES   6 D  286  THR ALA SER VAL ILE TYR VAL PRO ALA PRO PHE CYS LYS          
SEQRES   7 D  286  ASP SER ILE LEU GLU ALA ILE ASP ALA GLY ILE LYS LEU          
SEQRES   8 D  286  ILE ILE THR ILE THR GLU GLY ILE PRO THR LEU ASP MET          
SEQRES   9 D  286  LEU THR VAL LYS VAL LYS LEU ASP GLU ALA GLY VAL ARG          
SEQRES  10 D  286  MET ILE GLY PRO ASN CYS PRO GLY VAL ILE THR PRO GLY          
SEQRES  11 D  286  GLU CYS LYS ILE GLY ILE GLN PRO GLY HIS ILE HIS LYS          
SEQRES  12 D  286  PRO GLY LYS VAL GLY ILE VAL SER ARG SER GLY THR LEU          
SEQRES  13 D  286  THR TYR GLU ALA VAL LYS GLN THR THR ASP TYR GLY PHE          
SEQRES  14 D  286  GLY GLN SER THR CYS VAL GLY ILE GLY GLY ASP PRO ILE          
SEQRES  15 D  286  PRO GLY SER ASN PHE ILE ASP ILE LEU GLU MET PHE GLU          
SEQRES  16 D  286  LYS ASP PRO GLN THR GLU ALA ILE VAL MET ILE GLY GLU          
SEQRES  17 D  286  ILE GLY GLY SER ALA GLU GLU GLU ALA ALA ALA TYR ILE          
SEQRES  18 D  286  LYS GLU HIS VAL THR LYS PRO VAL VAL GLY TYR ILE ALA          
SEQRES  19 D  286  GLY VAL THR ALA PRO LYS GLY LYS ARG MET GLY HIS ALA          
SEQRES  20 D  286  GLY ALA ILE ILE ALA GLY GLY LYS GLY THR ALA ASP GLU          
SEQRES  21 D  286  LYS PHE ALA ALA LEU GLU ALA ALA GLY VAL LYS THR VAL          
SEQRES  22 D  286  ARG SER LEU ALA ASP ILE GLY GLU ALA LEU LYS THR VAL          
SEQRES   1 E  385  MET ASN LEU HIS GLU TYR GLN ALA LYS GLN LEU PHE ALA          
SEQRES   2 E  385  ARG TYR GLY LEU PRO ALA PRO VAL GLY TYR ALA CYS THR          
SEQRES   3 E  385  THR PRO ARG GLU ALA GLU GLU ALA ALA SER LYS ILE GLY          
SEQRES   4 E  385  ALA GLY PRO TRP VAL VAL LYS CYS GLN VAL HIS ALA GLY          
SEQRES   5 E  385  GLY ARG GLY LYS ALA GLY GLY VAL LYS VAL VAL ASN SER          
SEQRES   6 E  385  LYS GLU ASP ILE ARG ALA PHE ALA GLU ASN TRP LEU GLY          
SEQRES   7 E  385  LYS ARG LEU VAL THR TYR GLN THR ASP ALA ASN GLY GLN          
SEQRES   8 E  385  PRO VAL ASN GLN ILE LEU VAL GLU ALA ALA THR ASP ILE          
SEQRES   9 E  385  ALA LYS GLU LEU TYR LEU GLY ALA VAL VAL ASP ARG SER          
SEQRES  10 E  385  SER ARG ARG VAL VAL PHE MET ALA SER THR GLU GLY GLY          
SEQRES  11 E  385  VAL GLU ILE GLU LYS VAL ALA GLU GLU THR PRO HIS LEU          
SEQRES  12 E  385  ILE HIS LYS VAL ALA LEU ASP PRO LEU THR GLY PRO MET          
SEQRES  13 E  385  PRO TYR GLN GLY ARG GLU LEU ALA PHE LYS LEU GLY LEU          
SEQRES  14 E  385  GLU GLY LYS LEU VAL GLN GLN PHE THR LYS ILE PHE MET          
SEQRES  15 E  385  GLY LEU ALA THR ILE PHE LEU GLU ARG ASP LEU ALA LEU          
SEQRES  16 E  385  ILE GLU ILE ASN PRO LEU VAL ILE THR LYS GLN GLY ASP          
SEQRES  17 E  385  LEU ILE CYS LEU ASP GLY LYS LEU GLY ALA ASP GLY ASN          
SEQRES  18 E  385  ALA LEU PHE ARG GLN PRO ASP LEU ARG GLU MET ARG ASP          
SEQRES  19 E  385  GLN SER GLN GLU ASP PRO ARG GLU ALA GLN ALA ALA GLN          
SEQRES  20 E  385  TRP GLU LEU ASN TYR VAL ALA LEU ASP GLY ASN ILE GLY          
SEQRES  21 E  385  CYS MET VAL ASN GLY ALA GLY LEU ALA MET GLY THR MET          
SEQRES  22 E  385  ASP ILE VAL LYS LEU HIS GLY GLY GLU PRO ALA ASN PHE          
SEQRES  23 E  385  LEU ASP VAL GLY GLY GLY ALA THR LYS GLU ARG VAL THR          
SEQRES  24 E  385  GLU ALA PHE LYS ILE ILE LEU SER ASP ASP LYS VAL LYS          
SEQRES  25 E  385  ALA VAL LEU VAL ASN ILE PHE GLY GLY ILE VAL ARG CYS          
SEQRES  26 E  385  ASP LEU ILE ALA ASP GLY ILE ILE GLY ALA VAL ALA GLU          
SEQRES  27 E  385  VAL GLY VAL ASN VAL PRO VAL VAL VAL ARG LEU GLU GLY          
SEQRES  28 E  385  ASN ASN ALA GLU LEU GLY ALA LYS LYS LEU ALA ASP SER          
SEQRES  29 E  385  GLY LEU ASN ILE ILE ALA ALA LYS GLY LEU THR ASP ALA          
SEQRES  30 E  385  ALA GLN GLN VAL VAL ALA ALA VAL                              
HET    PO4  A 601       5                                                       
HET    COA  A 701      48                                                       
HET     MG  B 501       1                                                       
HET    ADP  B 801      27                                                       
HET    PO4  D 602       5                                                       
HET    COA  D 702      48                                                       
HET     MG  E 502       1                                                       
HET    ADP  E 802      27                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     COA COENZYME A                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   5  PO4    2(O4 P 3-)                                                   
FORMUL   6  COA    2(C21 H36 N7 O16 P3 S)                                       
FORMUL   7   MG    2(MG 2+)                                                     
FORMUL   8  ADP    2(C10 H15 N5 O10 P2)                                         
HELIX    1   1 GLY A   17  TYR A   30  1                                  14    
HELIX    2   2 THR A   55  THR A   63  1                                   9    
HELIX    3   3 PRO A   73  ALA A   87  1                                  15    
HELIX    4   4 PRO A  100  ALA A  114  1                                  15    
HELIX    5   5 PRO A  138  HIS A  142  5                                   5    
HELIX    6   6 GLY A  154  TYR A  167  1                                  14    
HELIX    7   7 ASN A  186  LYS A  196  1                                  11    
HELIX    8   8 SER A  212  VAL A  225  1                                  14    
HELIX    9   9 THR A  257  ALA A  267  1                                  11    
HELIX   10  10 ASP A  278  THR A  285  1                                   8    
HELIX   11  11 HIS B    4  TYR B   15  1                                  12    
HELIX   12  12 THR B   27  GLY B   39  1                                  13    
HELIX   13  13 ARG B   54  GLY B   58  5                                   5    
HELIX   14  14 SER B   65  LEU B   77  1                                  13    
HELIX   15  15 GLU B  132  THR B  140  1                                   9    
HELIX   16  16 MET B  156  LEU B  167  1                                  12    
HELIX   17  17 GLY B  171  ARG B  191  1                                  21    
HELIX   18  18 GLY B  220  ARG B  225  5                                   6    
HELIX   19  19 GLN B  226  GLU B  231  1                                   6    
HELIX   20  20 MET B  232  ARG B  233  5                                   2    
HELIX   21  21 ASP B  234  GLU B  238  5                                   5    
HELIX   22  22 ASP B  239  GLN B  247  1                                   9    
HELIX   23  23 GLY B  265  LEU B  278  1                                  14    
HELIX   24  24 THR B  294  LEU B  306  1                                  13    
HELIX   25  25 ARG B  324  GLY B  340  1                                  17    
HELIX   26  26 ASN B  353  GLY B  365  1                                  13    
HELIX   27  27 GLY B  373  ALA B  384  1                                  12    
HELIX   28  28 GLY D   17  TYR D   30  1                                  14    
HELIX   29  29 THR D   55  THR D   63  1                                   9    
HELIX   30  30 PRO D   73  ALA D   87  1                                  15    
HELIX   31  31 PRO D  100  ALA D  114  1                                  15    
HELIX   32  32 PRO D  138  HIS D  142  5                                   5    
HELIX   33  33 GLY D  154  TYR D  167  1                                  14    
HELIX   34  34 ASN D  186  LYS D  196  1                                  11    
HELIX   35  35 SER D  212  VAL D  225  1                                  14    
HELIX   36  36 THR D  257  ALA D  267  1                                  11    
HELIX   37  37 ASP D  278  THR D  285  1                                   8    
HELIX   38  38 HIS E    4  TYR E   15  1                                  12    
HELIX   39  39 THR E   27  GLY E   39  1                                  13    
HELIX   40  40 ARG E   54  GLY E   58  5                                   5    
HELIX   41  41 SER E   65  LEU E   77  1                                  13    
HELIX   42  42 GLU E  132  THR E  140  1                                   9    
HELIX   43  43 MET E  156  LEU E  167  1                                  12    
HELIX   44  44 GLY E  171  ARG E  191  1                                  21    
HELIX   45  45 GLY E  220  ARG E  225  5                                   6    
HELIX   46  46 GLN E  226  ARG E  233  1                                   8    
HELIX   47  47 ASP E  234  GLU E  238  5                                   5    
HELIX   48  48 ASP E  239  GLN E  247  1                                   9    
HELIX   49  49 GLY E  265  LEU E  278  1                                  14    
HELIX   50  50 THR E  294  LEU E  306  1                                  13    
HELIX   51  51 ARG E  324  GLY E  340  1                                  17    
HELIX   52  52 ASN E  353  SER E  364  1                                  12    
HELIX   53  53 GLY E  373  ALA E  384  1                                  12    
SHEET    1   A 7 THR A  45  THR A  46  0                                        
SHEET    2   A 7 PRO A  51  PHE A  53 -1  N  VAL A  52   O  THR A  45           
SHEET    3   A 7 MET A  34  VAL A  38  1  O  GLY A  37   N  PHE A  53           
SHEET    4   A 7 VAL A  10  GLN A  13  1  O  VAL A  10   N  VAL A  35           
SHEET    5   A 7 ALA A  67  ILE A  70  1  O  ALA A  67   N  ILE A  11           
SHEET    6   A 7 LEU A  91  THR A  94  1  O  LEU A  91   N  SER A  68           
SHEET    7   A 7 ARG A 117  ILE A 119  1  O  ARG A 117   N  ILE A  92           
SHEET    1   B 7 CYS A 132  ILE A 134  0                                        
SHEET    2   B 7 GLY A 125  THR A 128 -1  N  VAL A 126   O  ILE A 134           
SHEET    3   B 7 GLN A 171  GLY A 176 -1  N  CYS A 174   O  ILE A 127           
SHEET    4   B 7 PRO A 144  SER A 151  1  N  GLY A 145   O  GLN A 171           
SHEET    5   B 7 ALA A 202  GLU A 208  1  O  ALA A 202   N  GLY A 148           
SHEET    6   B 7 VAL A 229  ALA A 234  1  N  VAL A 230   O  ILE A 203           
SHEET    7   B 7 LYS A 271  THR A 272  1  N  LYS A 271   O  VAL A 229           
SHEET    1   C 4 GLY B  22  CYS B  25  0                                        
SHEET    2   C 4 ILE B  96  ALA B 100 -1  N  ILE B  96   O  CYS B  25           
SHEET    3   C 4 TRP B  43  CYS B  47 -1  N  VAL B  44   O  GLU B  99           
SHEET    4   C 4 VAL B  60  VAL B  63 -1  O  LYS B  61   N  VAL B  45           
SHEET    1   D 2 LYS B  79  LEU B  81  0                                        
SHEET    2   D 2 GLN B  91  VAL B  93 -1  O  GLN B  91   N  LEU B  81           
SHEET    1   E 5 ILE B 144  ALA B 148  0                                        
SHEET    2   E 5 ARG B 120  SER B 126 -1  N  PHE B 123   O  VAL B 147           
SHEET    3   E 5 ILE B 104  ASP B 115 -1  N  TYR B 109   O  SER B 126           
SHEET    4   E 5 LEU B 193  THR B 204 -1  O  ALA B 194   N  VAL B 114           
SHEET    5   E 5 LEU B 209  CYS B 211 -1  O  ILE B 210   N  VAL B 202           
SHEET    1  E1 5 ILE B 144  ALA B 148  0                                        
SHEET    2  E1 5 ARG B 120  SER B 126 -1  N  PHE B 123   O  VAL B 147           
SHEET    3  E1 5 ILE B 104  ASP B 115 -1  N  TYR B 109   O  SER B 126           
SHEET    4  E1 5 LEU B 193  THR B 204 -1  O  ALA B 194   N  VAL B 114           
SHEET    5  E1 5 LYS B 215  ALA B 218 -1  O  LYS B 215   N  GLU B 197           
SHEET    1   F 2 LEU B 250  ALA B 254  0                                        
SHEET    2   F 2 ASN B 285  VAL B 289 -1  N  PHE B 286   O  VAL B 253           
SHEET    1   G 3 GLY B 260  VAL B 263  0                                        
SHEET    2   G 3 VAL B 314  ASN B 317  1  N  LEU B 315   O  GLY B 260           
SHEET    3   G 3 VAL B 345  VAL B 346  1  N  VAL B 346   O  VAL B 314           
SHEET    1   H 7 THR D  45  THR D  46  0                                        
SHEET    2   H 7 PRO D  51  PHE D  53 -1  N  VAL D  52   O  THR D  45           
SHEET    3   H 7 LYS D  33  VAL D  38  1  O  GLY D  37   N  PHE D  53           
SHEET    4   H 7 LYS D   9  GLN D  13  1  O  VAL D  10   N  VAL D  35           
SHEET    5   H 7 ALA D  67  ILE D  70  1  O  ALA D  67   N  ILE D  11           
SHEET    6   H 7 LEU D  91  THR D  94  1  O  LEU D  91   N  SER D  68           
SHEET    7   H 7 ARG D 117  ILE D 119  1  O  ARG D 117   N  ILE D  92           
SHEET    1   I 7 CYS D 132  ILE D 134  0                                        
SHEET    2   I 7 GLY D 125  THR D 128 -1  N  VAL D 126   O  ILE D 134           
SHEET    3   I 7 GLN D 171  GLY D 176 -1  N  CYS D 174   O  ILE D 127           
SHEET    4   I 7 PRO D 144  SER D 151  1  N  GLY D 145   O  GLN D 171           
SHEET    5   I 7 ALA D 202  GLU D 208  1  O  ALA D 202   N  GLY D 148           
SHEET    6   I 7 VAL D 229  ALA D 234  1  N  VAL D 230   O  ILE D 203           
SHEET    7   I 7 LYS D 271  THR D 272  1  N  LYS D 271   O  VAL D 229           
SHEET    1   J 4 GLY E  22  CYS E  25  0                                        
SHEET    2   J 4 ILE E  96  ALA E 100 -1  N  ILE E  96   O  CYS E  25           
SHEET    3   J 4 TRP E  43  CYS E  47 -1  N  VAL E  44   O  GLU E  99           
SHEET    4   J 4 VAL E  60  VAL E  63 -1  O  LYS E  61   N  VAL E  45           
SHEET    1   K 2 LYS E  79  LEU E  81  0                                        
SHEET    2   K 2 GLN E  91  VAL E  93 -1  O  GLN E  91   N  LEU E  81           
SHEET    1   L 5 ILE E 144  ALA E 148  0                                        
SHEET    2   L 5 ARG E 120  SER E 126 -1  N  PHE E 123   O  VAL E 147           
SHEET    3   L 5 ILE E 104  ASP E 115 -1  N  TYR E 109   O  SER E 126           
SHEET    4   L 5 LEU E 193  THR E 204 -1  O  ALA E 194   N  VAL E 114           
SHEET    5   L 5 LEU E 209  CYS E 211 -1  O  ILE E 210   N  VAL E 202           
SHEET    1  L1 5 ILE E 144  ALA E 148  0                                        
SHEET    2  L1 5 ARG E 120  SER E 126 -1  N  PHE E 123   O  VAL E 147           
SHEET    3  L1 5 ILE E 104  ASP E 115 -1  N  TYR E 109   O  SER E 126           
SHEET    4  L1 5 LEU E 193  THR E 204 -1  O  ALA E 194   N  VAL E 114           
SHEET    5  L1 5 LYS E 215  ALA E 218 -1  O  LYS E 215   N  GLU E 197           
SHEET    1   M 2 LEU E 250  ALA E 254  0                                        
SHEET    2   M 2 ASN E 285  VAL E 289 -1  N  PHE E 286   O  VAL E 253           
SHEET    1   N 4 GLY E 260  VAL E 263  0                                        
SHEET    2   N 4 VAL E 314  PHE E 319  1  N  LEU E 315   O  GLY E 260           
SHEET    3   N 4 VAL E 345  VAL E 347  1  N  VAL E 346   O  VAL E 314           
SHEET    4   N 4 ILE E 368  ALA E 370  1  N  ILE E 369   O  VAL E 345           
SHEET    1  N1 3 GLY E 260  VAL E 263  0                                        
SHEET    2  N1 3 VAL E 314  PHE E 319  1  N  LEU E 315   O  GLY E 260           
SHEET    3  N1 3 LEU E 349  GLU E 350  1  N  GLU E 350   O  ILE E 318           
LINK         O   ASN B 199                MG    MG B 501     1555   1555  2.41  
LINK         O   ASN E 199                MG    MG E 502     1555   1555  2.37  
LINK        MG    MG B 501                 O3B ADP B 801     1555   1555  2.33  
LINK        MG    MG E 502                 O3B ADP E 802     1555   1555  2.34  
LINK         SG  CYS A 123                 S1P COA A 701     1555   1555  2.04  
LINK        MG    MG B 501                 OD2 ASP B 213     1555   1555  2.59  
LINK        MG    MG B 501                 O2A ADP B 801     1555   1555  2.52  
LINK         SG  CYS D 123                 S1P COA D 702     1555   1555  2.03  
LINK        MG    MG E 502                 OD2 ASP E 213     1555   1555  2.61  
LINK        MG    MG E 502                 O2A ADP E 802     1555   1555  2.51  
CISPEP   1 GLY A  120    PRO A  121          0        -0.24                     
CISPEP   2 GLY B   41    PRO B   42          0        -0.70                     
CISPEP   3 ASN B  199    PRO B  200          0         0.30                     
CISPEP   4 GLY D  120    PRO D  121          0        -0.26                     
CISPEP   5 GLY E   41    PRO E   42          0        -0.47                     
CISPEP   6 ASN E  199    PRO E  200          0         0.31                     
SITE     1 AC1  3 ASN B 199  ASP B 213  ADP B 801                               
SITE     1 AC2  3 ASN E 199  ASP E 213  ADP E 802                               
SITE     1 AC3  7 SER A 153  GLY A 154  THR A 155  HIS A 246                    
SITE     2 AC3  7 GLY B 265  ALA B 266  GLY B 267                               
SITE     1 AC4  7 SER D 153  GLY D 154  THR D 155  HIS D 246                    
SITE     2 AC4  7 GLY E 265  ALA E 266  GLY E 267                               
SITE     1 AC5 20 GLY A  14  THR A  16  GLY A  17  SER A  18                    
SITE     2 AC5 20 GLN A  19  PRO A  40  LYS A  42  TYR A  71                    
SITE     3 AC5 20 VAL A  72  PRO A  73  ILE A  95  THR A  96                    
SITE     4 AC5 20 GLU A  97  CYS A 123  ILE A 136  ARG B 161                    
SITE     5 AC5 20 ARG E  29  GLU E  33  SER E  36  LYS E  66                    
SITE     1 AC6 19 ARG B  29  GLU B  33  SER B  36  LYS B  66                    
SITE     2 AC6 19 GLY D  14  THR D  16  GLY D  17  SER D  18                    
SITE     3 AC6 19 GLN D  19  PRO D  40  LYS D  42  TYR D  71                    
SITE     4 AC6 19 VAL D  72  PRO D  73  ILE D  95  THR D  96                    
SITE     5 AC6 19 GLU D  97  CYS D 123  ILE D 136                               
SITE     1 AC7 15 VAL B  44  LYS B  46  GLY B  53  ARG B  54                    
SITE     2 AC7 15 GLY B  55  GLU B  99  ALA B 100  ALA B 101                    
SITE     3 AC7 15 THR B 102  GLU B 107  ASN B 199  PRO B 200                    
SITE     4 AC7 15 LEU B 212  ASP B 213   MG B 501                               
SITE     1 AC8 15 VAL E  44  LYS E  46  GLY E  53  ARG E  54                    
SITE     2 AC8 15 GLY E  55  GLU E  99  ALA E 100  ALA E 101                    
SITE     3 AC8 15 THR E 102  GLU E 107  ASN E 199  PRO E 200                    
SITE     4 AC8 15 LEU E 212  ASP E 213   MG E 502                               
CRYST1   99.860   99.860  407.150  90.00  90.00  90.00 P 43 2 2     16          
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      0.010014  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010014  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002456        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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