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Database: PDB
Entry: 1SVD
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Original site: 1SVD 
HEADER    LYASE                                   29-MAR-04   1SVD              
TITLE     THE STRUCTURE OF HALOTHIOBACILLUS NEAPOLITANUS RUBISCO                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE LARGE      
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A;                                                            
COMPND   5 EC: 4.1.1.39;                                                        
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN;             
COMPND   8 CHAIN: M;                                                            
COMPND   9 SYNONYM: RUBISCO SMALL SUBUNIT;                                      
COMPND  10 EC: 4.1.1.39                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HALOTHIOBACILLUS NEAPOLITANUS;                  
SOURCE   3 ORGANISM_TAXID: 927;                                                 
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: HALOTHIOBACILLUS NEAPOLITANUS;                  
SOURCE   6 ORGANISM_TAXID: 927                                                  
KEYWDS    BETA-ALPHA-BARREL, LYASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.A.KERFELD,M.R.SAWAYA,I.PASHKOV,G.CANNON,E.WILLIAMS,K.TRAN,          
AUTHOR   2 T.O.YEATES                                                           
REVDAT   3   13-JUL-11 1SVD    1       VERSN                                    
REVDAT   2   24-FEB-09 1SVD    1       VERSN                                    
REVDAT   1   12-APR-05 1SVD    0                                                
JRNL        AUTH   C.A.KERFELD,M.R.SAWAYA,I.PASHKOV,G.CANNON,E.WILLIAMS,K.TRAN, 
JRNL        AUTH 2 T.O.YEATES                                                   
JRNL        TITL   THE STRUCTURE OF HALOTHIOBACILLUS NEAPOLITANUS RUBISCO       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 87.71                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 58984                          
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) : 0.146                           
REMARK   3   R VALUE            (WORKING SET) : 0.145                           
REMARK   3   FREE R VALUE                     : 0.166                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3095                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4304                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 237                          
REMARK   3   BIN FREE R VALUE                    : 0.1980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4369                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 354                                     
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) : 11.19                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.49000                                              
REMARK   3    B22 (A**2) : 0.49000                                              
REMARK   3    B33 (A**2) : -0.98000                                             
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): 0.092         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.086         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.050         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.538         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4544 ; 0.015 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  4008 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6169 ; 1.519 ; 1.935       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9305 ; 0.910 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   559 ; 5.893 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   643 ; 0.099 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5150 ; 0.015 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   984 ; 0.022 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   881 ; 0.209 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4649 ; 0.246 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2571 ; 0.085 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   302 ; 0.124 ; 0.200       
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):    45 ; 0.223 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):   137 ; 0.304 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    40 ; 0.307 ; 0.200       
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):  2764 ; 0.945 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4432 ; 1.759 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1780 ; 2.665 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1737 ; 4.207 ; 4.500       
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  : 2                                          
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    16        A   460                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.6543  30.1686  12.6002              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0268 T22:   0.0381                                     
REMARK   3      T33:   0.0593 T12:  -0.0179                                     
REMARK   3      T13:   0.0012 T23:  -0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0958 L22:   0.2307                                     
REMARK   3      L33:   0.2864 L12:  -0.0846                                     
REMARK   3      L13:   0.0587 L23:  -0.1110                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0113 S12:  -0.0012 S13:   0.0485                       
REMARK   3      S21:   0.0068 S22:  -0.0080 S23:  -0.0588                       
REMARK   3      S31:  -0.0251 S32:   0.0371 S33:   0.0192                       
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 :   M     3        M   110                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.6119  29.6921  41.0339              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0550 T22:   0.0606                                     
REMARK   3      T33:   0.0131 T12:   0.0010                                     
REMARK   3      T13:   0.0099 T23:  -0.0217                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4816 L22:   0.3182                                     
REMARK   3      L33:   0.1755 L12:   0.1617                                     
REMARK   3      L13:   0.2305 L23:   0.1629                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0296 S12:  -0.1076 S13:   0.0532                       
REMARK   3      S21:   0.0481 S22:  -0.0370 S23:   0.0341                       
REMARK   3      S31:  -0.0184 S32:  -0.0468 S33:   0.0073                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1SVD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAR-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022024.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-NOV-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1271                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : DOUBLE CRYSTAL SI(111)             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62138                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 90.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 9.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.10                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.35500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: PDB ENTRY 1RBL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, CITRATE, COBALT        
REMARK 280  CHLORIDE, GLYCEROL, PH 5.8, VAPOR DIFFUSION, HANGING DROP,          
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 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   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
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  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        0.00000            
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        0.00000            
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        0.00000            
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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       78.53300            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       78.53300            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       53.80450            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       78.53300            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       78.53300            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       53.80450            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       78.53300            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       78.53300            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       53.80450            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       78.53300            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       78.53300            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       53.80450            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       78.53300            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       78.53300            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       53.80450            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       78.53300            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       78.53300            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       53.80450            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       78.53300            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       78.53300            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       53.80450            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       78.53300            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       78.53300            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       53.80450            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS AN L(8)S(8) OCTAMER GENERATED     
REMARK 300 FROM THE LARGE(L) AND SMALL (S) SUBNITS IN THE ASYMMETRIC UNIT BY    
REMARK 300 THE OPERATIONS: X,Y,Z; -X,-Y,Z; -Y,X,Z; Y,-X,Z; -X,Y,-Z; X,-Y,-Z;    
REMARK 300 Y,X,-Z; -Y,-X,-Z.                                                    
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, M                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC              
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 84410 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 129540 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -520.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, M                                  
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 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14300 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, M                                  
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  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -93.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, M                                  
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 681  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH M 170  LIES ON A SPECIAL POSITION.                          
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     VAL A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     TYR A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     VAL A    10                                                      
REMARK 465     LYS A    11                                                      
REMARK 465     GLU A    12                                                      
REMARK 465     TYR A    13                                                      
REMARK 465     ARG A    14                                                      
REMARK 465     GLN A    15                                                      
REMARK 465     GLU A   461                                                      
REMARK 465     PHE A   462                                                      
REMARK 465     ASP A   463                                                      
REMARK 465     THR A   464                                                      
REMARK 465     VAL A   465                                                      
REMARK 465     ASP A   466                                                      
REMARK 465     LYS A   467                                                      
REMARK 465     LEU A   468                                                      
REMARK 465     ASP A   469                                                      
REMARK 465     THR A   470                                                      
REMARK 465     GLN A   471                                                      
REMARK 465     ASN A   472                                                      
REMARK 465     ARG A   473                                                      
REMARK 465     MET M     1                                                      
REMARK 465     ALA M     2                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN M 110    CB   CG   OD1                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP A   196     ND2  ASN A   198              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 187   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ASP A 209   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 331   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 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    SER A  55      -70.32   -137.45                                   
REMARK 500    HIS A 146      -52.71   -128.75                                   
REMARK 500    ASN A 200      -84.90   -125.64                                   
REMARK 500    MET A 205       93.01   -162.45                                   
REMARK 500    MET A 290       -1.09     80.02                                   
REMARK 500    VAL A 324      -51.53     69.23                                   
REMARK 500    ASP A 350       94.47   -160.41                                   
REMARK 500    TYR M  13       33.58   -143.24                                   
REMARK 500    GLU M  14     -146.52     67.48                                   
REMARK 500    PHE M  16       -1.77     78.22                                   
REMARK 500    LYS M  60     -130.81     54.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 474                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL M 111                 
DBREF  1SVD A    1   473  UNP    O85040   O85040_THINE     1    473             
DBREF  1SVD M    1   110  UNP    P45686   RBS_THINE        1    110             
SEQRES   1 A  473  MET ALA VAL LYS LYS TYR SER ALA GLY VAL LYS GLU TYR          
SEQRES   2 A  473  ARG GLN THR TYR TRP MET PRO GLU TYR THR PRO LEU ASP          
SEQRES   3 A  473  SER ASP ILE LEU ALA CYS PHE LYS ILE THR PRO GLN PRO          
SEQRES   4 A  473  GLY VAL ASP ARG GLU GLU ALA ALA ALA ALA VAL ALA ALA          
SEQRES   5 A  473  GLU SER SER THR GLY THR TRP THR THR VAL TRP THR ASP          
SEQRES   6 A  473  LEU LEU THR ASP MET ASP TYR TYR LYS GLY ARG ALA TYR          
SEQRES   7 A  473  ARG ILE GLU ASP VAL PRO GLY ASP ASP ALA ALA PHE TYR          
SEQRES   8 A  473  ALA PHE ILE ALA TYR PRO ILE ASP LEU PHE GLU GLU GLY          
SEQRES   9 A  473  SER VAL VAL ASN VAL PHE THR SER LEU VAL GLY ASN VAL          
SEQRES  10 A  473  PHE GLY PHE LYS ALA VAL ARG GLY LEU ARG LEU GLU ASP          
SEQRES  11 A  473  VAL ARG PHE PRO LEU ALA TYR VAL LYS THR CYS GLY GLY          
SEQRES  12 A  473  PRO PRO HIS GLY ILE GLN VAL GLU ARG ASP LYS MET ASN          
SEQRES  13 A  473  LYS TYR GLY ARG PRO LEU LEU GLY CYS THR ILE LYS PRO          
SEQRES  14 A  473  LYS LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL          
SEQRES  15 A  473  TYR GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP          
SEQRES  16 A  473  ASP GLU ASN ILE ASN SER GLN PRO PHE MET ARG TRP ARG          
SEQRES  17 A  473  ASP ARG PHE LEU PHE VAL GLN ASP ALA THR GLU THR ALA          
SEQRES  18 A  473  GLU ALA GLN THR GLY GLU ARG LYS GLY HIS TYR LEU ASN          
SEQRES  19 A  473  VAL THR ALA PRO THR PRO GLU GLU MET TYR LYS ARG ALA          
SEQRES  20 A  473  GLU PHE ALA LYS GLU ILE GLY ALA PRO ILE ILE MET HIS          
SEQRES  21 A  473  ASP TYR ILE THR GLY GLY PHE THR ALA ASN THR GLY LEU          
SEQRES  22 A  473  ALA LYS TRP CYS GLN ASP ASN GLY VAL LEU LEU HIS ILE          
SEQRES  23 A  473  HIS ARG ALA MET HIS ALA VAL ILE ASP ARG ASN PRO ASN          
SEQRES  24 A  473  HIS GLY ILE HIS PHE ARG VAL LEU THR LYS ILE LEU ARG          
SEQRES  25 A  473  LEU SER GLY GLY ASP HIS LEU HIS THR GLY THR VAL VAL          
SEQRES  26 A  473  GLY LYS LEU GLU GLY ASP ARG ALA SER THR LEU GLY TRP          
SEQRES  27 A  473  ILE ASP LEU LEU ARG GLU SER PHE ILE PRO GLU ASP ARG          
SEQRES  28 A  473  SER ARG GLY ILE PHE PHE ASP GLN ASP TRP GLY SER MET          
SEQRES  29 A  473  PRO GLY VAL PHE ALA VAL ALA SER GLY GLY ILE HIS VAL          
SEQRES  30 A  473  TRP HIS MET PRO ALA LEU VAL ASN ILE PHE GLY ASP ASP          
SEQRES  31 A  473  SER VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO          
SEQRES  32 A  473  TRP GLY ASN ALA ALA GLY ALA ALA ALA ASN ARG VAL ALA          
SEQRES  33 A  473  LEU GLU ALA CYS VAL GLU ALA ARG ASN GLN GLY ARG ASP          
SEQRES  34 A  473  ILE GLU LYS GLU GLY LYS GLU ILE LEU THR ALA ALA ALA          
SEQRES  35 A  473  GLN HIS SER PRO GLU LEU LYS ILE ALA MET GLU THR TRP          
SEQRES  36 A  473  LYS GLU ILE LYS PHE GLU PHE ASP THR VAL ASP LYS LEU          
SEQRES  37 A  473  ASP THR GLN ASN ARG                                          
SEQRES   1 M  110  MET ALA GLU MET GLN ASP TYR LYS GLN SER LEU LYS TYR          
SEQRES   2 M  110  GLU THR PHE SER TYR LEU PRO PRO MET ASN ALA GLU ARG          
SEQRES   3 M  110  ILE ARG ALA GLN ILE LYS TYR ALA ILE ALA GLN GLY TRP          
SEQRES   4 M  110  SER PRO GLY ILE GLU HIS VAL GLU VAL LYS ASN SER MET          
SEQRES   5 M  110  ASN GLN TYR TRP TYR MET TRP LYS LEU PRO PHE PHE GLY          
SEQRES   6 M  110  GLU GLN ASN VAL ASP ASN VAL LEU ALA GLU ILE GLU ALA          
SEQRES   7 M  110  CYS ARG SER ALA TYR PRO THR HIS GLN VAL LYS LEU VAL          
SEQRES   8 M  110  ALA TYR ASP ASN TYR ALA GLN SER LEU GLY LEU ALA PHE          
SEQRES   9 M  110  VAL VAL TYR ARG GLY ASN                                      
HET    SO4  A 474       5                                                       
HET    SO4  A 475       5                                                       
HET    GOL  M 111       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  GOL    C3 H8 O3                                                     
FORMUL   6  HOH   *354(H2 O)                                                    
HELIX    1   1 ASP A   42  SER A   54  1                                  13    
HELIX    2   2 VAL A   62  THR A   68  5                                   7    
HELIX    3   3 PRO A   97  PHE A  101  5                                   5    
HELIX    4   4 SER A  105  GLY A  115  1                                  11    
HELIX    5   5 ASN A  116  PHE A  120  5                                   5    
HELIX    6   6 PRO A  134  LYS A  139  1                                   6    
HELIX    7   7 GLY A  147  ASN A  156  1                                  10    
HELIX    8   8 SER A  174  GLY A  188  1                                  15    
HELIX    9   9 ARG A  206  GLY A  226  1                                  21    
HELIX   10  10 THR A  239  GLY A  254  1                                  16    
HELIX   11  11 GLY A  266  GLY A  281  1                                  16    
HELIX   12  12 MET A  290  ARG A  296  1                                   7    
HELIX   13  13 HIS A  303  GLY A  315  1                                  13    
HELIX   14  14 LEU A  328  ASP A  331  5                                   4    
HELIX   15  15 ARG A  332  GLU A  344  1                                  13    
HELIX   16  16 ASP A  350  GLY A  354  5                                   5    
HELIX   17  17 HIS A  376  TRP A  378  5                                   3    
HELIX   18  18 HIS A  379  GLY A  388  1                                  10    
HELIX   19  19 GLY A  396  GLY A  401  1                                   6    
HELIX   20  20 GLY A  405  GLN A  426  1                                  22    
HELIX   21  21 GLU A  433  GLN A  443  1                                  11    
HELIX   22  22 SER A  445  LYS A  456  1                                  12    
HELIX   23  23 ASN M   23  GLN M   37  1                                  15    
HELIX   24  24 GLU M   47  SER M   51  5                                   5    
HELIX   25  25 ASN M   68  TYR M   83  1                                  16    
SHEET    1   A 5 ARG A  76  VAL A  83  0                                        
SHEET    2   A 5 ASP A  86  TYR A  96 -1  O  TYR A  91   N  GLU A  81           
SHEET    3   A 5 ILE A  29  PRO A  37 -1  N  ILE A  35   O  PHE A  90           
SHEET    4   A 5 VAL A 123  ARG A 132 -1  O  ARG A 127   N  LYS A  34           
SHEET    5   A 5 GLY A 301  ILE A 302  1  O  GLY A 301   N  LEU A 126           
SHEET    1   B 9 LEU A 162  THR A 166  0                                        
SHEET    2   B 9 PHE A 192  LYS A 194  1  O  PHE A 192   N  LEU A 163           
SHEET    3   B 9 GLY A 230  ASN A 234  1  O  TYR A 232   N  THR A 193           
SHEET    4   B 9 ILE A 257  ASP A 261  1  O  MET A 259   N  LEU A 233           
SHEET    5   B 9 LEU A 283  HIS A 287  1  O  HIS A 285   N  ILE A 258           
SHEET    6   B 9 HIS A 318  HIS A 320  1  O  HIS A 318   N  ILE A 286           
SHEET    7   B 9 PHE A 368  SER A 372  1  O  VAL A 370   N  LEU A 319           
SHEET    8   B 9 SER A 391  GLN A 394  1  O  GLN A 394   N  ALA A 371           
SHEET    9   B 9 LEU A 162  THR A 166  1  N  LEU A 162   O  LEU A 393           
SHEET    1   C 2 PHE A 346  ILE A 347  0                                        
SHEET    2   C 2 GLN A 359  ASP A 360 -1  O  GLN A 359   N  ILE A 347           
SHEET    1   D 4 TYR M  57  TRP M  59  0                                        
SHEET    2   D 4 SER M  40  VAL M  46 -1  N  ILE M  43   O  TRP M  59           
SHEET    3   D 4 GLN M  87  ASP M  94 -1  O  LYS M  89   N  GLU M  44           
SHEET    4   D 4 SER M  99  TYR M 107 -1  O  SER M  99   N  ASP M  94           
CISPEP   1 LYS A  168    PRO A  169          0         0.62                     
SITE     1 AC1  7 ARG A 288  HIS A 320  SER A 372  HOH A 555                    
SITE     2 AC1  7 HOH A 573  HOH A 646  HOH A 725                               
SITE     1 AC2  5 GLY A 374  GLY A 396  GLY A 397  HOH A 527                    
SITE     2 AC2  5 HOH A 572                                                     
SITE     1 AC3  7 ASN A 156  HOH A 642  HOH A 704  TYR M  13                    
SITE     2 AC3  7 SER M  51  LYS M  89  HOH M 135                               
CRYST1  157.066  157.066  107.609  90.00  90.00  90.00 I 4 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      0.006367  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006367  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009293        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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