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Database: PDB
Entry: 2P9C
LinkDB: 2P9C
Original site: 2P9C 
HEADER    OXIDOREDUCTASE                          24-MAR-07   2P9C              
TITLE     CRYSTAL STRUCTURE OF SERINE BOUND G336V MUTANT OF E.COLI              
TITLE    2 PHOSPHOGLYCERATE DEHYDROGENASE                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-3-PHOSPHOGLYCERATE DEHYDROGENASE;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PGDH;                                                       
COMPND   5 EC: 1.1.1.95;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: SERA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;                                  
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTRC99                                    
KEYWDS    OXIDOREDUCTASE, PHOSPHOGLYCERATE DEHYDROGENASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.DEY,J.C.SACCHETTINI                                                 
REVDAT   4   13-JUL-11 2P9C    1       VERSN                                    
REVDAT   3   24-FEB-09 2P9C    1       VERSN                                    
REVDAT   2   17-JUL-07 2P9C    1       JRNL                                     
REVDAT   1   24-APR-07 2P9C    0                                                
JRNL        AUTH   S.DEY,Z.HU,X.L.XU,J.C.SACCHETTINI,G.A.GRANT                  
JRNL        TITL   THE EFFECT OF HINGE MUTATIONS ON EFFECTOR BINDING AND DOMAIN 
JRNL        TITL 2 ROTATION IN ESCHERICHIA COLI D-3-PHOSPHOGLYCERATE            
JRNL        TITL 3 DEHYDROGENASE                                                
JRNL        REF    J.BIOL.CHEM.                  V. 282 18418 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17459882                                                     
JRNL        DOI    10.1074/JBC.M701174200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.46 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.46                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 29392                          
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 + TEST SET) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1556                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.46                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.52                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1704                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 70.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : 0.3790                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6140                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 102                                     
REMARK   3   SOLVENT ATOMS            : 54                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.57000                                             
REMARK   3    B22 (A**2) : -2.76000                                             
REMARK   3    B33 (A**2) : 4.33000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.698         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.338         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.244         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.873        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.898                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6354 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8630 ; 1.394 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   808 ; 5.881 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   262 ;36.950 ;24.962       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1074 ;18.637 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;20.187 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1008 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4718 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2789 ; 0.255 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4358 ; 0.328 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   374 ; 0.189 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    57 ; 0.214 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.326 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4111 ; 2.900 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6448 ; 4.389 ; 7.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2442 ; 5.942 ; 9.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2182 ; 7.547 ;11.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     7        A   107                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.6913 -24.6772   5.4762              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0291 T22:  -0.0647                                     
REMARK   3      T33:   0.0012 T12:   0.0003                                     
REMARK   3      T13:   0.0134 T23:   0.0271                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5905 L22:   4.3302                                     
REMARK   3      L33:   3.8525 L12:  -0.1727                                     
REMARK   3      L13:   0.3937 L23:  -1.1077                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0512 S12:   0.3618 S13:   0.0959                       
REMARK   3      S21:  -0.3951 S22:   0.1769 S23:   0.5885                       
REMARK   3      S31:  -0.0302 S32:  -0.5294 S33:  -0.2281                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   108        A   294                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.4601   0.6337  28.4783              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0606 T22:  -0.1585                                     
REMARK   3      T33:  -0.0632 T12:   0.0005                                     
REMARK   3      T13:  -0.0020 T23:   0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2688 L22:   1.6870                                     
REMARK   3      L33:   1.4569 L12:  -0.5605                                     
REMARK   3      L13:  -0.0356 L23:   0.0213                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0685 S12:  -0.1533 S13:  -0.1155                       
REMARK   3      S21:   0.1012 S22:   0.0585 S23:  -0.1210                       
REMARK   3      S31:   0.1034 S32:   0.1390 S33:   0.0100                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   337        A   410                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.1295 -47.3973  11.1192              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0638 T22:  -0.1347                                     
REMARK   3      T33:   0.0449 T12:   0.0382                                     
REMARK   3      T13:   0.0508 T23:   0.0387                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9981 L22:   1.0675                                     
REMARK   3      L33:   1.4229 L12:   1.5253                                     
REMARK   3      L13:   0.4510 L23:   0.8578                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0105 S12:   0.3946 S13:  -0.2010                       
REMARK   3      S21:  -0.4222 S22:   0.0432 S23:  -0.2286                       
REMARK   3      S31:  -0.0746 S32:  -0.2182 S33:  -0.0537                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     7        B   107                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.2209  39.5814  30.5436              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0993 T22:  -0.0332                                     
REMARK   3      T33:   0.1586 T12:  -0.0262                                     
REMARK   3      T13:  -0.0030 T23:  -0.0471                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6152 L22:   2.1783                                     
REMARK   3      L33:   1.5026 L12:   0.7509                                     
REMARK   3      L13:  -1.4695 L23:  -0.9079                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0258 S12:  -0.2562 S13:   0.3273                       
REMARK   3      S21:   0.0864 S22:   0.0408 S23:   0.6020                       
REMARK   3      S31:   0.0293 S32:  -0.1717 S33:  -0.0667                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   108        B   294                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.9239  14.3459   7.7541              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0691 T22:  -0.1216                                     
REMARK   3      T33:  -0.0356 T12:  -0.0412                                     
REMARK   3      T13:   0.0651 T23:  -0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4304 L22:   1.3462                                     
REMARK   3      L33:   1.4845 L12:  -0.2105                                     
REMARK   3      L13:  -0.5752 L23:  -0.2197                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0920 S12:   0.1214 S13:   0.0369                       
REMARK   3      S21:  -0.2923 S22:  -0.0730 S23:  -0.1994                       
REMARK   3      S31:  -0.0671 S32:   0.1844 S33:  -0.0190                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   337        B   410                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3732  50.8428  25.4795              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0547 T22:  -0.1049                                     
REMARK   3      T33:   0.0473 T12:  -0.0605                                     
REMARK   3      T13:  -0.0369 T23:  -0.0345                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2894 L22:   1.6549                                     
REMARK   3      L33:   2.7296 L12:  -1.1582                                     
REMARK   3      L13:  -0.4342 L23:   1.8245                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1444 S12:  -0.4940 S13:   0.2845                       
REMARK   3      S21:   0.1203 S22:   0.0427 S23:   0.1783                       
REMARK   3      S31:   0.1251 S32:  -0.0741 S33:  -0.1871                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2P9C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB042129.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAY-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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          : OTHER                              
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.541                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31001                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.460                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.7                               
REMARK 200  DATA REDUNDANCY                : 7.600                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.46                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2PA3                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG3000, 0.1M CACODYLATE, 0.2M       
REMARK 280  MGCL2, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K      
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       71.07100            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       65.39250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       71.07100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       65.39250            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 19840 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 63210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     SER B     5                                                      
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    VAL A  19     -178.69    -69.13                                   
REMARK 500    ARG A  60      -92.63   -119.60                                   
REMARK 500    ALA A  73       96.18    -49.79                                   
REMARK 500    THR A  86       16.19   -144.95                                   
REMARK 500    ASN A 103     -159.09   -153.13                                   
REMARK 500    TYR A 159       71.40   -104.10                                   
REMARK 500    PRO A 215      -36.00    -37.14                                   
REMARK 500    SER A 239      -91.71    -80.90                                   
REMARK 500    ASN A 318        8.37   -151.30                                   
REMARK 500    SER A 323       -0.87     80.77                                   
REMARK 500    ASP A 386      165.57    -40.02                                   
REMARK 500    GLU B   7       50.09     39.09                                   
REMARK 500    LYS B   8      -26.85   -164.71                                   
REMARK 500    ARG B  60     -140.43   -114.45                                   
REMARK 500    ALA B  83     -176.97   -174.93                                   
REMARK 500    ASN B 108       34.11   -150.57                                   
REMARK 500    TYR B 159       69.41   -100.53                                   
REMARK 500    PRO B 215      -33.74    -30.13                                   
REMARK 500    SER B 239      -94.97    -97.83                                   
REMARK 500    ASP B 245       97.12    -65.22                                   
REMARK 500    PRO B 270      123.24    -37.08                                   
REMARK 500    ASN B 318       -0.11   -153.01                                   
REMARK 500    SER B 323        6.72     80.22                                   
REMARK 500    HIS B 335      -75.52   -109.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI A 450                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI B 550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SER A 451                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SER A 551                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2P9E   RELATED DB: PDB                                   
DBREF  2P9C A    1   410  UNP    P0A9T0   SERA_ECOLI       1    410             
DBREF  2P9C B    1   410  UNP    P0A9T0   SERA_ECOLI       1    410             
SEQADV 2P9C ALA A   81  UNP  P0A9T0    CYS    81 ENGINEERED                     
SEQADV 2P9C ALA A   83  UNP  P0A9T0    CYS    83 ENGINEERED                     
SEQADV 2P9C ALA A  250  UNP  P0A9T0    CYS   250 ENGINEERED                     
SEQADV 2P9C ALA A  282  UNP  P0A9T0    CYS   282 ENGINEERED                     
SEQADV 2P9C VAL A  336  UNP  P0A9T0    GLY   336 ENGINEERED                     
SEQADV 2P9C ALA B   81  UNP  P0A9T0    CYS    81 ENGINEERED                     
SEQADV 2P9C ALA B   83  UNP  P0A9T0    CYS    83 ENGINEERED                     
SEQADV 2P9C ALA B  250  UNP  P0A9T0    CYS   250 ENGINEERED                     
SEQADV 2P9C ALA B  282  UNP  P0A9T0    CYS   282 ENGINEERED                     
SEQADV 2P9C VAL B  336  UNP  P0A9T0    GLY   336 ENGINEERED                     
SEQRES   1 A  410  MET ALA LYS VAL SER LEU GLU LYS ASP LYS ILE LYS PHE          
SEQRES   2 A  410  LEU LEU VAL GLU GLY VAL HIS GLN LYS ALA LEU GLU SER          
SEQRES   3 A  410  LEU ARG ALA ALA GLY TYR THR ASN ILE GLU PHE HIS LYS          
SEQRES   4 A  410  GLY ALA LEU ASP ASP GLU GLN LEU LYS GLU SER ILE ARG          
SEQRES   5 A  410  ASP ALA HIS PHE ILE GLY LEU ARG SER ARG THR HIS LEU          
SEQRES   6 A  410  THR GLU ASP VAL ILE ASN ALA ALA GLU LYS LEU VAL ALA          
SEQRES   7 A  410  ILE GLY ALA PHE ALA ILE GLY THR ASN GLN VAL ASP LEU          
SEQRES   8 A  410  ASP ALA ALA ALA LYS ARG GLY ILE PRO VAL PHE ASN ALA          
SEQRES   9 A  410  PRO PHE SER ASN THR ARG SER VAL ALA GLU LEU VAL ILE          
SEQRES  10 A  410  GLY GLU LEU LEU LEU LEU LEU ARG GLY VAL PRO GLU ALA          
SEQRES  11 A  410  ASN ALA LYS ALA HIS ARG GLY VAL TRP ASN LYS LEU ALA          
SEQRES  12 A  410  ALA GLY SER PHE GLU ALA ARG GLY LYS LYS LEU GLY ILE          
SEQRES  13 A  410  ILE GLY TYR GLY HIS ILE GLY THR GLN LEU GLY ILE LEU          
SEQRES  14 A  410  ALA GLU SER LEU GLY MET TYR VAL TYR PHE TYR ASP ILE          
SEQRES  15 A  410  GLU ASN LYS LEU PRO LEU GLY ASN ALA THR GLN VAL GLN          
SEQRES  16 A  410  HIS LEU SER ASP LEU LEU ASN MET SER ASP VAL VAL SER          
SEQRES  17 A  410  LEU HIS VAL PRO GLU ASN PRO SER THR LYS ASN MET MET          
SEQRES  18 A  410  GLY ALA LYS GLU ILE SER LEU MET LYS PRO GLY SER LEU          
SEQRES  19 A  410  LEU ILE ASN ALA SER ARG GLY THR VAL VAL ASP ILE PRO          
SEQRES  20 A  410  ALA LEU ALA ASP ALA LEU ALA SER LYS HIS LEU ALA GLY          
SEQRES  21 A  410  ALA ALA ILE ASP VAL PHE PRO THR GLU PRO ALA THR ASN          
SEQRES  22 A  410  SER ASP PRO PHE THR SER PRO LEU ALA GLU PHE ASP ASN          
SEQRES  23 A  410  VAL LEU LEU THR PRO HIS ILE GLY GLY SER THR GLN GLU          
SEQRES  24 A  410  ALA GLN GLU ASN ILE GLY LEU GLU VAL ALA GLY LYS LEU          
SEQRES  25 A  410  ILE LYS TYR SER ASP ASN GLY SER THR LEU SER ALA VAL          
SEQRES  26 A  410  ASN PHE PRO GLU VAL SER LEU PRO LEU HIS VAL GLY ARG          
SEQRES  27 A  410  ARG LEU MET HIS ILE HIS GLU ASN ARG PRO GLY VAL LEU          
SEQRES  28 A  410  THR ALA LEU ASN LYS ILE PHE ALA GLU GLN GLY VAL ASN          
SEQRES  29 A  410  ILE ALA ALA GLN TYR LEU GLN THR SER ALA GLN MET GLY          
SEQRES  30 A  410  TYR VAL VAL ILE ASP ILE GLU ALA ASP GLU ASP VAL ALA          
SEQRES  31 A  410  GLU LYS ALA LEU GLN ALA MET LYS ALA ILE PRO GLY THR          
SEQRES  32 A  410  ILE ARG ALA ARG LEU LEU TYR                                  
SEQRES   1 B  410  MET ALA LYS VAL SER LEU GLU LYS ASP LYS ILE LYS PHE          
SEQRES   2 B  410  LEU LEU VAL GLU GLY VAL HIS GLN LYS ALA LEU GLU SER          
SEQRES   3 B  410  LEU ARG ALA ALA GLY TYR THR ASN ILE GLU PHE HIS LYS          
SEQRES   4 B  410  GLY ALA LEU ASP ASP GLU GLN LEU LYS GLU SER ILE ARG          
SEQRES   5 B  410  ASP ALA HIS PHE ILE GLY LEU ARG SER ARG THR HIS LEU          
SEQRES   6 B  410  THR GLU ASP VAL ILE ASN ALA ALA GLU LYS LEU VAL ALA          
SEQRES   7 B  410  ILE GLY ALA PHE ALA ILE GLY THR ASN GLN VAL ASP LEU          
SEQRES   8 B  410  ASP ALA ALA ALA LYS ARG GLY ILE PRO VAL PHE ASN ALA          
SEQRES   9 B  410  PRO PHE SER ASN THR ARG SER VAL ALA GLU LEU VAL ILE          
SEQRES  10 B  410  GLY GLU LEU LEU LEU LEU LEU ARG GLY VAL PRO GLU ALA          
SEQRES  11 B  410  ASN ALA LYS ALA HIS ARG GLY VAL TRP ASN LYS LEU ALA          
SEQRES  12 B  410  ALA GLY SER PHE GLU ALA ARG GLY LYS LYS LEU GLY ILE          
SEQRES  13 B  410  ILE GLY TYR GLY HIS ILE GLY THR GLN LEU GLY ILE LEU          
SEQRES  14 B  410  ALA GLU SER LEU GLY MET TYR VAL TYR PHE TYR ASP ILE          
SEQRES  15 B  410  GLU ASN LYS LEU PRO LEU GLY ASN ALA THR GLN VAL GLN          
SEQRES  16 B  410  HIS LEU SER ASP LEU LEU ASN MET SER ASP VAL VAL SER          
SEQRES  17 B  410  LEU HIS VAL PRO GLU ASN PRO SER THR LYS ASN MET MET          
SEQRES  18 B  410  GLY ALA LYS GLU ILE SER LEU MET LYS PRO GLY SER LEU          
SEQRES  19 B  410  LEU ILE ASN ALA SER ARG GLY THR VAL VAL ASP ILE PRO          
SEQRES  20 B  410  ALA LEU ALA ASP ALA LEU ALA SER LYS HIS LEU ALA GLY          
SEQRES  21 B  410  ALA ALA ILE ASP VAL PHE PRO THR GLU PRO ALA THR ASN          
SEQRES  22 B  410  SER ASP PRO PHE THR SER PRO LEU ALA GLU PHE ASP ASN          
SEQRES  23 B  410  VAL LEU LEU THR PRO HIS ILE GLY GLY SER THR GLN GLU          
SEQRES  24 B  410  ALA GLN GLU ASN ILE GLY LEU GLU VAL ALA GLY LYS LEU          
SEQRES  25 B  410  ILE LYS TYR SER ASP ASN GLY SER THR LEU SER ALA VAL          
SEQRES  26 B  410  ASN PHE PRO GLU VAL SER LEU PRO LEU HIS VAL GLY ARG          
SEQRES  27 B  410  ARG LEU MET HIS ILE HIS GLU ASN ARG PRO GLY VAL LEU          
SEQRES  28 B  410  THR ALA LEU ASN LYS ILE PHE ALA GLU GLN GLY VAL ASN          
SEQRES  29 B  410  ILE ALA ALA GLN TYR LEU GLN THR SER ALA GLN MET GLY          
SEQRES  30 B  410  TYR VAL VAL ILE ASP ILE GLU ALA ASP GLU ASP VAL ALA          
SEQRES  31 B  410  GLU LYS ALA LEU GLN ALA MET LYS ALA ILE PRO GLY THR          
SEQRES  32 B  410  ILE ARG ALA ARG LEU LEU TYR                                  
HET    NAI  A 450      44                                                       
HET    NAI  B 550      44                                                       
HET    SER  A 451       7                                                       
HET    SER  A 551       7                                                       
HETNAM     NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE                     
HETNAM     SER SERINE                                                           
HETSYN     NAI NADH                                                             
FORMUL   3  NAI    2(C21 H29 N7 O14 P2)                                         
FORMUL   5  SER    2(C3 H7 N O3)                                                
FORMUL   6  HOH   *54(H2 O)                                                     
HELIX    1   1 GLU A    7  ILE A   11  5                                   5    
HELIX    2   2 HIS A   20  ALA A   30  1                                  11    
HELIX    3   3 ASP A   43  ILE A   51  1                                   9    
HELIX    4   4 THR A   66  ALA A   73  1                                   8    
HELIX    5   5 ASP A   90  ARG A   97  1                                   8    
HELIX    6   6 ASN A  108  ARG A  125  1                                  18    
HELIX    7   7 GLY A  126  ARG A  136  1                                  11    
HELIX    8   8 GLY A  160  LEU A  173  1                                  14    
HELIX    9   9 HIS A  196  SER A  204  1                                   9    
HELIX   10  10 GLY A  222  MET A  229  1                                   8    
HELIX   11  11 ASP A  245  SER A  255  1                                  11    
HELIX   12  12 SER A  279  PHE A  284  5                                   6    
HELIX   13  13 THR A  297  GLY A  319  1                                  23    
HELIX   14  14 GLY A  349  GLN A  361  1                                  13    
HELIX   15  15 ASP A  386  ALA A  399  1                                  14    
HELIX   16  16 HIS B   20  ALA B   30  1                                  11    
HELIX   17  17 ASP B   43  ARG B   52  1                                  10    
HELIX   18  18 THR B   66  ALA B   73  1                                   8    
HELIX   19  19 ASP B   90  ARG B   97  1                                   8    
HELIX   20  20 ASN B  108  ARG B  125  1                                  18    
HELIX   21  21 GLY B  126  HIS B  135  1                                  10    
HELIX   22  22 GLY B  160  LEU B  173  1                                  14    
HELIX   23  23 HIS B  196  SER B  204  1                                   9    
HELIX   24  24 GLY B  222  SER B  227  1                                   6    
HELIX   25  25 ASP B  245  SER B  255  1                                  11    
HELIX   26  26 SER B  279  PHE B  284  5                                   6    
HELIX   27  27 THR B  297  GLY B  319  1                                  23    
HELIX   28  28 GLY B  349  GLU B  360  1                                  12    
HELIX   29  29 ASP B  386  ALA B  399  1                                  14    
SHEET    1   A 5 ILE A  35  PHE A  37  0                                        
SHEET    2   A 5 PHE A  13  LEU A  15  1  N  PHE A  13   O  GLU A  36           
SHEET    3   A 5 PHE A  56  LEU A  59  1  O  GLY A  58   N  LEU A  14           
SHEET    4   A 5 VAL A 101  PHE A 102  1                                        
SHEET    1   B 7 THR A 192  GLN A 193  0                                        
SHEET    2   B 7 TYR A 176  TYR A 180  1  N  PHE A 179   O  THR A 192           
SHEET    3   B 7 LYS A 153  ILE A 157  1  N  ILE A 156   O  TYR A 178           
SHEET    4   B 7 VAL A 206  LEU A 209  1  O  VAL A 206   N  GLY A 155           
SHEET    5   B 7 SER A 233  ASN A 237  1  O  LEU A 234   N  VAL A 207           
SHEET    6   B 7 LEU A 258  ILE A 263  1  O  ALA A 259   N  SER A 233           
SHEET    7   B 7 VAL A 287  LEU A 289  1  O  LEU A 288   N  ILE A 263           
SHEET    1   C 4 ASN A 364  THR A 372  0                                        
SHEET    2   C 4 MET A 376  GLU A 384 -1  O  GLU A 384   N  ASN A 364           
SHEET    3   C 4 ARG A 338  GLU A 345 -1  N  HIS A 344   O  GLY A 377           
SHEET    4   C 4 THR A 403  TYR A 410 -1  O  ILE A 404   N  ILE A 343           
SHEET    1   D 5 ILE B  35  PHE B  37  0                                        
SHEET    2   D 5 PHE B  13  LEU B  15  1  N  PHE B  13   O  GLU B  36           
SHEET    3   D 5 PHE B  56  LEU B  59  1  O  PHE B  56   N  LEU B  14           
SHEET    4   D 5 VAL B 101  PHE B 102  1                                        
SHEET    1   E 7 THR B 192  GLN B 193  0                                        
SHEET    2   E 7 TYR B 176  TYR B 180  1  N  VAL B 177   O  THR B 192           
SHEET    3   E 7 LYS B 153  ILE B 157  1  N  ILE B 156   O  TYR B 178           
SHEET    4   E 7 VAL B 206  LEU B 209  1  O  VAL B 206   N  GLY B 155           
SHEET    5   E 7 SER B 233  ASN B 237  1  O  LEU B 234   N  VAL B 207           
SHEET    6   E 7 LEU B 258  ILE B 263  1  O  ALA B 262   N  ASN B 237           
SHEET    7   E 7 VAL B 287  LEU B 289  1  O  LEU B 288   N  ILE B 263           
SHEET    1   F 4 ASN B 364  THR B 372  0                                        
SHEET    2   F 4 MET B 376  GLU B 384 -1  O  VAL B 380   N  TYR B 369           
SHEET    3   F 4 ARG B 338  GLU B 345 -1  N  ARG B 338   O  ILE B 383           
SHEET    4   F 4 THR B 403  TYR B 410 -1  O  ILE B 404   N  ILE B 343           
CISPEP   1 LEU B    6    GLU B    7          0         8.22                     
SITE     1 AC1 25 ILE A  84  PHE A 106  VAL A 112  GLY A 158                    
SITE     2 AC1 25 TYR A 159  GLY A 160  HIS A 161  ILE A 162                    
SITE     3 AC1 25 TYR A 180  ASP A 181  ILE A 182  LYS A 185                    
SITE     4 AC1 25 HIS A 210  VAL A 211  PRO A 212  SER A 216                    
SITE     5 AC1 25 MET A 220  ALA A 238  SER A 239  ARG A 240                    
SITE     6 AC1 25 ASP A 264  HIS A 292  GLY A 294  GLY A 295                    
SITE     7 AC1 25 HOH A 569                                                     
SITE     1 AC2 24 ILE B  84  PHE B 106  ASN B 108  VAL B 112                    
SITE     2 AC2 24 TYR B 159  GLY B 160  HIS B 161  ILE B 162                    
SITE     3 AC2 24 ASP B 181  ILE B 182  LYS B 185  HIS B 210                    
SITE     4 AC2 24 VAL B 211  PRO B 212  SER B 216  THR B 217                    
SITE     5 AC2 24 MET B 220  ALA B 238  SER B 239  ARG B 240                    
SITE     6 AC2 24 ASP B 264  HIS B 292  GLY B 294  GLY B 295                    
SITE     1 AC3 10 HIS A 344  ASN A 346  ARG A 347  PRO A 348                    
SITE     2 AC3 10 GLY A 349  LEU A 351  LEU A 370  HOH A 563                    
SITE     3 AC3 10 ASN B 364  ILE B 365                                          
SITE     1 AC4  8 ASN A 364  ILE A 365  HIS B 344  ASN B 346                    
SITE     2 AC4  8 ARG B 347  GLY B 349  LEU B 351  LEU B 370                    
CRYST1  142.142  130.785   50.188  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      0.007035  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007646  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019925        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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