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Database: PDB
Entry: 2D69
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Original site: 2D69 
HEADER    LYASE                                   10-NOV-05   2D69              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX OF SULFATE ION AND OCTAMERIC         
TITLE    2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE (RUBISCO) FROM       
TITLE    3 PYROCOCCUS HORIKOSHII OT3 (FORM-2 CRYSTAL)                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE;                         
COMPND   3 CHAIN: A, B, D, E;                                                   
COMPND   4 SYNONYM: RUBISCO, RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE;   
COMPND   5 EC: 4.1.1.39;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;                          
SOURCE   3 ORGANISM_TAXID: 70601;                                               
SOURCE   4 STRAIN: OT3;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET11A                                    
KEYWDS    ALPHA/BETA BARREL, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON   
KEYWDS   2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL         
KEYWDS   3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, LYASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.MIZOHATA,C.MISHIMA,R.AKASAKA,H.UDA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,  
AUTHOR   2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)               
REVDAT   3   13-JUL-11 2D69    1       VERSN                                    
REVDAT   2   24-FEB-09 2D69    1       VERSN                                    
REVDAT   1   10-MAY-06 2D69    0                                                
JRNL        AUTH   E.MIZOHATA,C.MISHIMA,R.AKASAKA,H.UDA,T.TERADA,M.SHIROUZU,    
JRNL        AUTH 2 S.YOKOYAMA                                                   
JRNL        TITL   CRYSTAL STRUCTURE OF THE COMPLEX OF SULFATE ION AND          
JRNL        TITL 2 OCTAMERIC RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE    
JRNL        TITL 3 (RUBISCO) FROM PYROCOCCUS HORIKOSHII OT3 (FORM-2 CRYSTAL)    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 154541                         
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8084                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10454                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3120                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 550                          
REMARK   3   BIN FREE R VALUE                    : 0.3230                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13217                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 95                                      
REMARK   3   SOLVENT ATOMS            : 750                                     
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) : 19.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.91000                                              
REMARK   3    B22 (A**2) : -1.49000                                             
REMARK   3    B33 (A**2) : 2.57000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.67000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.134         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.124         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.102         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.747         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.952                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13609 ; 0.020 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A): 12486 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18393 ; 1.662 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 28987 ; 0.896 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1667 ; 6.692 ; 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):  1941 ; 0.109 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15055 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2835 ; 0.008 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2811 ; 0.212 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 14430 ; 0.243 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  7824 ; 0.088 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   597 ; 0.160 ; 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):    47 ; 0.182 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):   276 ; 0.293 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    26 ; 0.136 ; 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):  8277 ; 0.910 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13260 ; 1.604 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5332 ; 2.578 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5133 ; 4.066 ; 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  : 4                                          
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     1        A   424                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3950  -0.4684  35.8628              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0853 T22:   0.1920                                     
REMARK   3      T33:   0.1342 T12:   0.0615                                     
REMARK   3      T13:  -0.0334 T23:  -0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5214 L22:   0.7802                                     
REMARK   3      L33:   0.4238 L12:  -0.1016                                     
REMARK   3      L13:  -0.1899 L23:   0.1735                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0073 S12:   0.0503 S13:  -0.0964                       
REMARK   3      S21:  -0.0331 S22:  -0.0261 S23:   0.2410                       
REMARK   3      S31:  -0.0912 S32:  -0.1161 S33:   0.0187                       
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 :   B     8        B   425                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.6478 -30.8985  56.9439              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1100 T22:   0.1039                                     
REMARK   3      T33:   0.1731 T12:  -0.0246                                     
REMARK   3      T13:  -0.0139 T23:   0.0297                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7973 L22:   0.3979                                     
REMARK   3      L33:   0.6928 L12:   0.0908                                     
REMARK   3      L13:  -0.0815 L23:   0.0177                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0502 S12:  -0.0675 S13:  -0.1938                       
REMARK   3      S21:   0.0521 S22:  -0.0580 S23:  -0.0099                       
REMARK   3      S31:   0.0863 S32:  -0.0233 S33:   0.0078                       
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 :   D     1        D   419                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.6481  40.2282  50.9756              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2686 T22:   0.0853                                     
REMARK   3      T33:   0.1064 T12:   0.0273                                     
REMARK   3      T13:   0.0617 T23:  -0.0421                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6284 L22:   0.5070                                     
REMARK   3      L33:   1.0769 L12:  -0.0023                                     
REMARK   3      L13:   0.1854 L23:  -0.1046                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0351 S12:  -0.0938 S13:   0.2259                       
REMARK   3      S21:   0.0593 S22:  -0.0546 S23:   0.0595                       
REMARK   3      S31:  -0.2897 S32:  -0.0838 S33:   0.0195                       
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 :   E     9        E   418                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.9269   9.5152  15.0650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1783 T22:   0.2137                                     
REMARK   3      T33:   0.0339 T12:   0.0736                                     
REMARK   3      T13:  -0.0581 T23:  -0.0162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8648 L22:   0.9957                                     
REMARK   3      L33:   0.5092 L12:  -0.1732                                     
REMARK   3      L13:  -0.2181 L23:   0.0966                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0564 S12:   0.2352 S13:  -0.0389                       
REMARK   3      S21:  -0.2152 S22:  -0.0495 S23:   0.1468                       
REMARK   3      S31:  -0.1137 S32:  -0.1208 S33:  -0.0069                       
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 2D69 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-NOV-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB025038.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-SEP-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL26B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS V                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 162742                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ID: 2CWX                                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM BICARBONATE,    
REMARK 280  MAGNESIUM CHLORIDE, SODIUM ACETATE, 2CABP, TRIS-HCL , PH 5, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       86.29550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       74.38700            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       86.29550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       74.38700            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 THE OCTAMER. BIOLOGICAL ASSEMBLY  
REMARK 300 (SEGID A, B, C, D, E, F, G, H) IS GENERATED FROM THE ASYMMETRIC      
REMARK 300 COMPONENT (A, B, D, E) BY OPERATOR -X+1, Y, -Z+1. (A, B, D, E) ->    
REMARK 300 (G, F, H, C)                                                         
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: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      108.09650            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       87.19114            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 30660 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 86150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -571.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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      108.09650            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       87.19114            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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      108.09650            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       87.19114            
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 D3177  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B2186  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B2181  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH D3175  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     LYS A   425                                                      
REMARK 465     VAL A   426                                                      
REMARK 465     GLY A   427                                                      
REMARK 465     VAL A   428                                                      
REMARK 465     GLN A   429                                                      
REMARK 465     HIS A   430                                                      
REMARK 465     MET B     1                                                      
REMARK 465     MET B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     ARG B     5                                                      
REMARK 465     MET B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     VAL B   426                                                      
REMARK 465     GLY B   427                                                      
REMARK 465     VAL B   428                                                      
REMARK 465     GLN B   429                                                      
REMARK 465     HIS B   430                                                      
REMARK 465     GLY D   420                                                      
REMARK 465     LEU D   421                                                      
REMARK 465     SER D   422                                                      
REMARK 465     LYS D   423                                                      
REMARK 465     ALA D   424                                                      
REMARK 465     LYS D   425                                                      
REMARK 465     VAL D   426                                                      
REMARK 465     GLY D   427                                                      
REMARK 465     VAL D   428                                                      
REMARK 465     GLN D   429                                                      
REMARK 465     HIS D   430                                                      
REMARK 465     MET E     1                                                      
REMARK 465     MET E     2                                                      
REMARK 465     VAL E     3                                                      
REMARK 465     LEU E     4                                                      
REMARK 465     ARG E     5                                                      
REMARK 465     MET E     6                                                      
REMARK 465     LYS E     7                                                      
REMARK 465     VAL E     8                                                      
REMARK 465     VAL E   419                                                      
REMARK 465     GLY E   420                                                      
REMARK 465     LEU E   421                                                      
REMARK 465     SER E   422                                                      
REMARK 465     LYS E   423                                                      
REMARK 465     ALA E   424                                                      
REMARK 465     LYS E   425                                                      
REMARK 465     VAL E   426                                                      
REMARK 465     GLY E   427                                                      
REMARK 465     VAL E   428                                                      
REMARK 465     GLN E   429                                                      
REMARK 465     HIS E   430                                                      
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     ALA A 424    O                                                   
REMARK 470     LYS B 425    O                                                   
REMARK 470     VAL D 419    O                                                   
REMARK 470     GLU E 418    O                                                   
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   OH   TYR B   323     O    HOH B  2101              2.00            
REMARK 500   OD2  ASP E   391     OG   SER E   409              2.02            
REMARK 500   OD1  ASP E   270     O    HOH E  4105              2.05            
REMARK 500   O    GLY E   313     O    HOH E  4128              2.07            
REMARK 500   OH   TYR E   248     NE2  GLN E   309              2.14            
REMARK 500   O    GLU B    63     O    HOH B  2084              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    VAL E 231   CB    VAL E 231   CG2    -0.135                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 331   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    LEU B 261   CB  -  CG  -  CD2 ANGL. DEV. =  12.4 DEGREES          
REMARK 500    ASP B 331   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP D  16   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP D 151   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP D 211   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    LEU D 261   CB  -  CG  -  CD2 ANGL. DEV. =  10.7 DEGREES          
REMARK 500    ASP D 308   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP D 331   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP D 366   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP D 380   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP D 391   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP E  16   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP E 211   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP E 308   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP E 380   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  51     -109.20   -131.63                                   
REMARK 500    ALA A 106       33.62   -140.57                                   
REMARK 500    ASP A 151      -47.41   -130.34                                   
REMARK 500    THR A 192      -78.51   -110.32                                   
REMARK 500    MET A 281      -14.86     90.24                                   
REMARK 500    MET A 319      -11.32   -165.89                                   
REMARK 500    ALA A 320      103.57    -19.65                                   
REMARK 500    TRP A 337       78.83   -152.88                                   
REMARK 500    GLU A 338     -131.01     49.11                                   
REMARK 500    ASP B  16       82.73   -161.26                                   
REMARK 500    SER B  51     -104.09   -132.42                                   
REMARK 500    THR B 192      -83.13   -103.38                                   
REMARK 500    ASN B 197       78.57   -151.80                                   
REMARK 500    MET B 281      -18.13     88.20                                   
REMARK 500    MET B 319     -112.33    -77.69                                   
REMARK 500    ALA B 320      117.62     75.37                                   
REMARK 500    TRP B 337       82.82   -151.47                                   
REMARK 500    GLU B 338     -126.78     50.95                                   
REMARK 500    ALA B 371       58.65   -141.95                                   
REMARK 500    GLU D   9       45.35   -109.37                                   
REMARK 500    SER D  51     -109.67   -130.11                                   
REMARK 500    TRP D  55       30.45   -149.92                                   
REMARK 500    ASP D 151      -55.65   -126.43                                   
REMARK 500    THR D 192      -75.53   -102.39                                   
REMARK 500    MET D 281      -18.15     90.60                                   
REMARK 500    LYS D 318      -70.10   -104.45                                   
REMARK 500    MET D 319     -131.75    -67.45                                   
REMARK 500    ALA D 320      124.16     90.99                                   
REMARK 500    GLU D 338     -130.16     45.63                                   
REMARK 500    ALA D 371       44.51   -147.89                                   
REMARK 500    ASP E  16       89.20   -155.54                                   
REMARK 500    SER E  51     -107.65   -134.98                                   
REMARK 500    TRP E  55     -166.54   -129.13                                   
REMARK 500    THR E  56      117.41    108.05                                   
REMARK 500    THR E  57      137.14    156.61                                   
REMARK 500    LYS E  77      135.60    -37.58                                   
REMARK 500    ASP E 151      -49.22   -139.90                                   
REMARK 500    THR E 192      -77.04   -107.33                                   
REMARK 500    ASN E 197       74.89   -152.92                                   
REMARK 500    MET E 281      -22.19     88.38                                   
REMARK 500    MET E 319     -129.54    -77.94                                   
REMARK 500    ALA E 320      117.46     93.78                                   
REMARK 500    TRP E 337       77.99   -153.62                                   
REMARK 500    GLU E 338     -129.40     50.14                                   
REMARK 500    ALA E 371       46.70   -146.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR E   56     THR E   57                 -145.87                    
REMARK 500 ALA E  315     VAL E  316                 -141.70                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1182        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH A1186        DISTANCE =  5.51 ANGSTROMS                       
REMARK 525    HOH A1211        DISTANCE =  5.77 ANGSTROMS                       
REMARK 525    HOH A1215        DISTANCE =  5.52 ANGSTROMS                       
REMARK 525    HOH A1225        DISTANCE =  6.65 ANGSTROMS                       
REMARK 525    HOH B2109        DISTANCE =  7.63 ANGSTROMS                       
REMARK 525    HOH B2128        DISTANCE =  5.79 ANGSTROMS                       
REMARK 525    HOH B2173        DISTANCE =  5.80 ANGSTROMS                       
REMARK 525    HOH D3119        DISTANCE =  6.97 ANGSTROMS                       
REMARK 525    HOH E4139        DISTANCE =  6.83 ANGSTROMS                       
REMARK 525    HOH E4160        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH E4168        DISTANCE =  6.98 ANGSTROMS                       
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 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 4001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 4002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 4003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 4004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 4005                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2CWX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: PHO001000939.3   RELATED DB: TARGETDB                    
DBREF  2D69 A    1   430  UNP    O58677   RBL_PYRHO        1    430             
DBREF  2D69 B    1   430  UNP    O58677   RBL_PYRHO        1    430             
DBREF  2D69 D    1   430  UNP    O58677   RBL_PYRHO        1    430             
DBREF  2D69 E    1   430  UNP    O58677   RBL_PYRHO        1    430             
SEQRES   1 A  430  MET MET VAL LEU ARG MET LYS VAL GLU TRP TYR LEU ASP          
SEQRES   2 A  430  PHE VAL ASP LEU ASN TYR GLU PRO GLY ARG ASP GLU LEU          
SEQRES   3 A  430  ILE VAL GLU TYR TYR PHE GLU PRO ASN GLY VAL SER PRO          
SEQRES   4 A  430  GLU GLU ALA ALA GLY ARG ILE ALA SER GLU SER SER ILE          
SEQRES   5 A  430  GLY THR TRP THR THR LEU TRP LYS LEU PRO GLU MET ALA          
SEQRES   6 A  430  LYS ARG SER MET ALA LYS VAL PHE TYR LEU GLU LYS HIS          
SEQRES   7 A  430  GLY GLU GLY TYR ILE ALA LYS ILE ALA TYR PRO LEU THR          
SEQRES   8 A  430  LEU PHE GLU GLU GLY SER LEU VAL GLN LEU PHE SER ALA          
SEQRES   9 A  430  VAL ALA GLY ASN VAL PHE GLY MET LYS ALA LEU LYS ASN          
SEQRES  10 A  430  LEU ARG LEU LEU ASP PHE HIS PRO PRO TYR GLU TYR LEU          
SEQRES  11 A  430  ARG HIS PHE LYS GLY PRO GLN PHE GLY VAL GLN GLY ILE          
SEQRES  12 A  430  ARG GLU PHE MET GLY VAL LYS ASP ARG PRO LEU THR ALA          
SEQRES  13 A  430  THR VAL PRO LYS PRO LYS MET GLY TRP SER VAL GLU GLU          
SEQRES  14 A  430  TYR ALA GLU ILE ALA TYR GLU LEU TRP SER GLY GLY ILE          
SEQRES  15 A  430  ASP LEU LEU LYS ASP ASP GLU ASN PHE THR SER PHE PRO          
SEQRES  16 A  430  PHE ASN ARG PHE GLU GLU ARG VAL ARG LYS LEU TYR ARG          
SEQRES  17 A  430  VAL ARG ASP ARG VAL GLU ALA GLU THR GLY GLU THR LYS          
SEQRES  18 A  430  GLU TYR LEU ILE ASN ILE THR GLY PRO VAL ASN ILE MET          
SEQRES  19 A  430  GLU LYS ARG ALA GLU MET VAL ALA ASN GLU GLY GLY GLN          
SEQRES  20 A  430  TYR VAL MET ILE ASP ILE VAL VAL ALA GLY TRP SER ALA          
SEQRES  21 A  430  LEU GLN TYR MET ARG GLU VAL THR GLU ASP LEU GLY LEU          
SEQRES  22 A  430  ALA ILE HIS ALA HIS ARG ALA MET HIS ALA ALA PHE THR          
SEQRES  23 A  430  ARG ASN PRO ARG HIS GLY ILE THR MET LEU ALA LEU ALA          
SEQRES  24 A  430  LYS ALA ALA ARG MET ILE GLY VAL ASP GLN ILE HIS THR          
SEQRES  25 A  430  GLY THR ALA VAL GLY LYS MET ALA GLY ASN TYR GLU GLU          
SEQRES  26 A  430  ILE LYS ARG ILE ASN ASP PHE LEU LEU SER LYS TRP GLU          
SEQRES  27 A  430  HIS ILE ARG PRO VAL PHE PRO VAL ALA SER GLY GLY LEU          
SEQRES  28 A  430  HIS PRO GLY LEU MET PRO GLU LEU ILE ARG LEU PHE GLY          
SEQRES  29 A  430  LYS ASP LEU VAL ILE GLN ALA GLY GLY GLY VAL MET GLY          
SEQRES  30 A  430  HIS PRO ASP GLY PRO ARG ALA GLY ALA LYS ALA LEU ARG          
SEQRES  31 A  430  ASP ALA ILE ASP ALA ALA ILE GLU GLY VAL ASP LEU ASP          
SEQRES  32 A  430  GLU LYS ALA LYS SER SER PRO GLU LEU LYS LYS SER LEU          
SEQRES  33 A  430  ARG GLU VAL GLY LEU SER LYS ALA LYS VAL GLY VAL GLN          
SEQRES  34 A  430  HIS                                                          
SEQRES   1 B  430  MET MET VAL LEU ARG MET LYS VAL GLU TRP TYR LEU ASP          
SEQRES   2 B  430  PHE VAL ASP LEU ASN TYR GLU PRO GLY ARG ASP GLU LEU          
SEQRES   3 B  430  ILE VAL GLU TYR TYR PHE GLU PRO ASN GLY VAL SER PRO          
SEQRES   4 B  430  GLU GLU ALA ALA GLY ARG ILE ALA SER GLU SER SER ILE          
SEQRES   5 B  430  GLY THR TRP THR THR LEU TRP LYS LEU PRO GLU MET ALA          
SEQRES   6 B  430  LYS ARG SER MET ALA LYS VAL PHE TYR LEU GLU LYS HIS          
SEQRES   7 B  430  GLY GLU GLY TYR ILE ALA LYS ILE ALA TYR PRO LEU THR          
SEQRES   8 B  430  LEU PHE GLU GLU GLY SER LEU VAL GLN LEU PHE SER ALA          
SEQRES   9 B  430  VAL ALA GLY ASN VAL PHE GLY MET LYS ALA LEU LYS ASN          
SEQRES  10 B  430  LEU ARG LEU LEU ASP PHE HIS PRO PRO TYR GLU TYR LEU          
SEQRES  11 B  430  ARG HIS PHE LYS GLY PRO GLN PHE GLY VAL GLN GLY ILE          
SEQRES  12 B  430  ARG GLU PHE MET GLY VAL LYS ASP ARG PRO LEU THR ALA          
SEQRES  13 B  430  THR VAL PRO LYS PRO LYS MET GLY TRP SER VAL GLU GLU          
SEQRES  14 B  430  TYR ALA GLU ILE ALA TYR GLU LEU TRP SER GLY GLY ILE          
SEQRES  15 B  430  ASP LEU LEU LYS ASP ASP GLU ASN PHE THR SER PHE PRO          
SEQRES  16 B  430  PHE ASN ARG PHE GLU GLU ARG VAL ARG LYS LEU TYR ARG          
SEQRES  17 B  430  VAL ARG ASP ARG VAL GLU ALA GLU THR GLY GLU THR LYS          
SEQRES  18 B  430  GLU TYR LEU ILE ASN ILE THR GLY PRO VAL ASN ILE MET          
SEQRES  19 B  430  GLU LYS ARG ALA GLU MET VAL ALA ASN GLU GLY GLY GLN          
SEQRES  20 B  430  TYR VAL MET ILE ASP ILE VAL VAL ALA GLY TRP SER ALA          
SEQRES  21 B  430  LEU GLN TYR MET ARG GLU VAL THR GLU ASP LEU GLY LEU          
SEQRES  22 B  430  ALA ILE HIS ALA HIS ARG ALA MET HIS ALA ALA PHE THR          
SEQRES  23 B  430  ARG ASN PRO ARG HIS GLY ILE THR MET LEU ALA LEU ALA          
SEQRES  24 B  430  LYS ALA ALA ARG MET ILE GLY VAL ASP GLN ILE HIS THR          
SEQRES  25 B  430  GLY THR ALA VAL GLY LYS MET ALA GLY ASN TYR GLU GLU          
SEQRES  26 B  430  ILE LYS ARG ILE ASN ASP PHE LEU LEU SER LYS TRP GLU          
SEQRES  27 B  430  HIS ILE ARG PRO VAL PHE PRO VAL ALA SER GLY GLY LEU          
SEQRES  28 B  430  HIS PRO GLY LEU MET PRO GLU LEU ILE ARG LEU PHE GLY          
SEQRES  29 B  430  LYS ASP LEU VAL ILE GLN ALA GLY GLY GLY VAL MET GLY          
SEQRES  30 B  430  HIS PRO ASP GLY PRO ARG ALA GLY ALA LYS ALA LEU ARG          
SEQRES  31 B  430  ASP ALA ILE ASP ALA ALA ILE GLU GLY VAL ASP LEU ASP          
SEQRES  32 B  430  GLU LYS ALA LYS SER SER PRO GLU LEU LYS LYS SER LEU          
SEQRES  33 B  430  ARG GLU VAL GLY LEU SER LYS ALA LYS VAL GLY VAL GLN          
SEQRES  34 B  430  HIS                                                          
SEQRES   1 D  430  MET MET VAL LEU ARG MET LYS VAL GLU TRP TYR LEU ASP          
SEQRES   2 D  430  PHE VAL ASP LEU ASN TYR GLU PRO GLY ARG ASP GLU LEU          
SEQRES   3 D  430  ILE VAL GLU TYR TYR PHE GLU PRO ASN GLY VAL SER PRO          
SEQRES   4 D  430  GLU GLU ALA ALA GLY ARG ILE ALA SER GLU SER SER ILE          
SEQRES   5 D  430  GLY THR TRP THR THR LEU TRP LYS LEU PRO GLU MET ALA          
SEQRES   6 D  430  LYS ARG SER MET ALA LYS VAL PHE TYR LEU GLU LYS HIS          
SEQRES   7 D  430  GLY GLU GLY TYR ILE ALA LYS ILE ALA TYR PRO LEU THR          
SEQRES   8 D  430  LEU PHE GLU GLU GLY SER LEU VAL GLN LEU PHE SER ALA          
SEQRES   9 D  430  VAL ALA GLY ASN VAL PHE GLY MET LYS ALA LEU LYS ASN          
SEQRES  10 D  430  LEU ARG LEU LEU ASP PHE HIS PRO PRO TYR GLU TYR LEU          
SEQRES  11 D  430  ARG HIS PHE LYS GLY PRO GLN PHE GLY VAL GLN GLY ILE          
SEQRES  12 D  430  ARG GLU PHE MET GLY VAL LYS ASP ARG PRO LEU THR ALA          
SEQRES  13 D  430  THR VAL PRO LYS PRO LYS MET GLY TRP SER VAL GLU GLU          
SEQRES  14 D  430  TYR ALA GLU ILE ALA TYR GLU LEU TRP SER GLY GLY ILE          
SEQRES  15 D  430  ASP LEU LEU LYS ASP ASP GLU ASN PHE THR SER PHE PRO          
SEQRES  16 D  430  PHE ASN ARG PHE GLU GLU ARG VAL ARG LYS LEU TYR ARG          
SEQRES  17 D  430  VAL ARG ASP ARG VAL GLU ALA GLU THR GLY GLU THR LYS          
SEQRES  18 D  430  GLU TYR LEU ILE ASN ILE THR GLY PRO VAL ASN ILE MET          
SEQRES  19 D  430  GLU LYS ARG ALA GLU MET VAL ALA ASN GLU GLY GLY GLN          
SEQRES  20 D  430  TYR VAL MET ILE ASP ILE VAL VAL ALA GLY TRP SER ALA          
SEQRES  21 D  430  LEU GLN TYR MET ARG GLU VAL THR GLU ASP LEU GLY LEU          
SEQRES  22 D  430  ALA ILE HIS ALA HIS ARG ALA MET HIS ALA ALA PHE THR          
SEQRES  23 D  430  ARG ASN PRO ARG HIS GLY ILE THR MET LEU ALA LEU ALA          
SEQRES  24 D  430  LYS ALA ALA ARG MET ILE GLY VAL ASP GLN ILE HIS THR          
SEQRES  25 D  430  GLY THR ALA VAL GLY LYS MET ALA GLY ASN TYR GLU GLU          
SEQRES  26 D  430  ILE LYS ARG ILE ASN ASP PHE LEU LEU SER LYS TRP GLU          
SEQRES  27 D  430  HIS ILE ARG PRO VAL PHE PRO VAL ALA SER GLY GLY LEU          
SEQRES  28 D  430  HIS PRO GLY LEU MET PRO GLU LEU ILE ARG LEU PHE GLY          
SEQRES  29 D  430  LYS ASP LEU VAL ILE GLN ALA GLY GLY GLY VAL MET GLY          
SEQRES  30 D  430  HIS PRO ASP GLY PRO ARG ALA GLY ALA LYS ALA LEU ARG          
SEQRES  31 D  430  ASP ALA ILE ASP ALA ALA ILE GLU GLY VAL ASP LEU ASP          
SEQRES  32 D  430  GLU LYS ALA LYS SER SER PRO GLU LEU LYS LYS SER LEU          
SEQRES  33 D  430  ARG GLU VAL GLY LEU SER LYS ALA LYS VAL GLY VAL GLN          
SEQRES  34 D  430  HIS                                                          
SEQRES   1 E  430  MET MET VAL LEU ARG MET LYS VAL GLU TRP TYR LEU ASP          
SEQRES   2 E  430  PHE VAL ASP LEU ASN TYR GLU PRO GLY ARG ASP GLU LEU          
SEQRES   3 E  430  ILE VAL GLU TYR TYR PHE GLU PRO ASN GLY VAL SER PRO          
SEQRES   4 E  430  GLU GLU ALA ALA GLY ARG ILE ALA SER GLU SER SER ILE          
SEQRES   5 E  430  GLY THR TRP THR THR LEU TRP LYS LEU PRO GLU MET ALA          
SEQRES   6 E  430  LYS ARG SER MET ALA LYS VAL PHE TYR LEU GLU LYS HIS          
SEQRES   7 E  430  GLY GLU GLY TYR ILE ALA LYS ILE ALA TYR PRO LEU THR          
SEQRES   8 E  430  LEU PHE GLU GLU GLY SER LEU VAL GLN LEU PHE SER ALA          
SEQRES   9 E  430  VAL ALA GLY ASN VAL PHE GLY MET LYS ALA LEU LYS ASN          
SEQRES  10 E  430  LEU ARG LEU LEU ASP PHE HIS PRO PRO TYR GLU TYR LEU          
SEQRES  11 E  430  ARG HIS PHE LYS GLY PRO GLN PHE GLY VAL GLN GLY ILE          
SEQRES  12 E  430  ARG GLU PHE MET GLY VAL LYS ASP ARG PRO LEU THR ALA          
SEQRES  13 E  430  THR VAL PRO LYS PRO LYS MET GLY TRP SER VAL GLU GLU          
SEQRES  14 E  430  TYR ALA GLU ILE ALA TYR GLU LEU TRP SER GLY GLY ILE          
SEQRES  15 E  430  ASP LEU LEU LYS ASP ASP GLU ASN PHE THR SER PHE PRO          
SEQRES  16 E  430  PHE ASN ARG PHE GLU GLU ARG VAL ARG LYS LEU TYR ARG          
SEQRES  17 E  430  VAL ARG ASP ARG VAL GLU ALA GLU THR GLY GLU THR LYS          
SEQRES  18 E  430  GLU TYR LEU ILE ASN ILE THR GLY PRO VAL ASN ILE MET          
SEQRES  19 E  430  GLU LYS ARG ALA GLU MET VAL ALA ASN GLU GLY GLY GLN          
SEQRES  20 E  430  TYR VAL MET ILE ASP ILE VAL VAL ALA GLY TRP SER ALA          
SEQRES  21 E  430  LEU GLN TYR MET ARG GLU VAL THR GLU ASP LEU GLY LEU          
SEQRES  22 E  430  ALA ILE HIS ALA HIS ARG ALA MET HIS ALA ALA PHE THR          
SEQRES  23 E  430  ARG ASN PRO ARG HIS GLY ILE THR MET LEU ALA LEU ALA          
SEQRES  24 E  430  LYS ALA ALA ARG MET ILE GLY VAL ASP GLN ILE HIS THR          
SEQRES  25 E  430  GLY THR ALA VAL GLY LYS MET ALA GLY ASN TYR GLU GLU          
SEQRES  26 E  430  ILE LYS ARG ILE ASN ASP PHE LEU LEU SER LYS TRP GLU          
SEQRES  27 E  430  HIS ILE ARG PRO VAL PHE PRO VAL ALA SER GLY GLY LEU          
SEQRES  28 E  430  HIS PRO GLY LEU MET PRO GLU LEU ILE ARG LEU PHE GLY          
SEQRES  29 E  430  LYS ASP LEU VAL ILE GLN ALA GLY GLY GLY VAL MET GLY          
SEQRES  30 E  430  HIS PRO ASP GLY PRO ARG ALA GLY ALA LYS ALA LEU ARG          
SEQRES  31 E  430  ASP ALA ILE ASP ALA ALA ILE GLU GLY VAL ASP LEU ASP          
SEQRES  32 E  430  GLU LYS ALA LYS SER SER PRO GLU LEU LYS LYS SER LEU          
SEQRES  33 E  430  ARG GLU VAL GLY LEU SER LYS ALA LYS VAL GLY VAL GLN          
SEQRES  34 E  430  HIS                                                          
HET    SO4  A1001       5                                                       
HET    SO4  A1002       5                                                       
HET    SO4  A1003       5                                                       
HET    SO4  A1004       5                                                       
HET    SO4  A1005       5                                                       
HET    SO4  B2001       5                                                       
HET    SO4  B2002       5                                                       
HET    SO4  B2003       5                                                       
HET    SO4  B2004       5                                                       
HET    SO4  B2005       5                                                       
HET    SO4  D3001       5                                                       
HET    SO4  D3002       5                                                       
HET    SO4  D3003       5                                                       
HET    SO4  D3004       5                                                       
HET    SO4  E4001       5                                                       
HET    SO4  E4002       5                                                       
HET    SO4  E4003       5                                                       
HET    SO4  E4004       5                                                       
HET    SO4  E4005       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  SO4    19(O4 S 2-)                                                  
FORMUL  24  HOH   *750(H2 O)                                                    
HELIX    1   1 TRP A   10  VAL A   15  5                                   6    
HELIX    2   2 SER A   38  SER A   50  1                                  13    
HELIX    3   3 ALA A   65  MET A   69  5                                   5    
HELIX    4   4 PRO A   89  PHE A   93  5                                   5    
HELIX    5   5 SER A   97  ALA A  106  1                                  10    
HELIX    6   6 GLY A  107  MET A  112  5                                   6    
HELIX    7   7 PRO A  126  ARG A  131  1                                   6    
HELIX    8   8 PHE A  138  GLY A  148  1                                  11    
HELIX    9   9 SER A  166  GLY A  180  1                                  15    
HELIX   10  10 ARG A  198  GLY A  218  1                                  21    
HELIX   11  11 PRO A  230  GLU A  244  1                                  15    
HELIX   12  12 ILE A  253  GLY A  257  1                                   5    
HELIX   13  13 GLY A  257  GLY A  272  1                                  16    
HELIX   14  14 HIS A  282  ARG A  287  1                                   6    
HELIX   15  15 THR A  294  GLY A  306  1                                  13    
HELIX   16  16 ASN A  322  SER A  335  1                                  14    
HELIX   17  17 HIS A  352  GLY A  354  5                                   3    
HELIX   18  18 LEU A  355  GLY A  364  1                                  10    
HELIX   19  19 ALA A  371  GLY A  377  1                                   7    
HELIX   20  20 GLY A  381  GLY A  399  1                                  19    
HELIX   21  21 ASP A  401  ALA A  406  1                                   6    
HELIX   22  22 SER A  409  LYS A  423  1                                  15    
HELIX   23  23 TRP B   10  VAL B   15  5                                   6    
HELIX   24  24 SER B   38  SER B   50  1                                  13    
HELIX   25  25 ALA B   65  MET B   69  5                                   5    
HELIX   26  26 PRO B   89  PHE B   93  5                                   5    
HELIX   27  27 SER B   97  ALA B  106  1                                  10    
HELIX   28  28 GLY B  107  MET B  112  5                                   6    
HELIX   29  29 PRO B  126  ARG B  131  1                                   6    
HELIX   30  30 PHE B  138  GLY B  148  1                                  11    
HELIX   31  31 SER B  166  GLY B  181  1                                  16    
HELIX   32  32 ARG B  198  GLY B  218  1                                  21    
HELIX   33  33 PRO B  230  GLU B  244  1                                  15    
HELIX   34  34 ILE B  253  GLY B  257  1                                   5    
HELIX   35  35 GLY B  257  GLY B  272  1                                  16    
HELIX   36  36 HIS B  282  ARG B  287  1                                   6    
HELIX   37  37 THR B  294  GLY B  306  1                                  13    
HELIX   38  38 ASN B  322  SER B  335  1                                  14    
HELIX   39  39 HIS B  352  GLY B  354  5                                   3    
HELIX   40  40 LEU B  355  GLY B  364  1                                  10    
HELIX   41  41 ALA B  371  GLY B  377  1                                   7    
HELIX   42  42 GLY B  381  GLY B  399  1                                  19    
HELIX   43  43 ASP B  401  LYS B  407  1                                   7    
HELIX   44  44 SER B  409  LYS B  423  1                                  15    
HELIX   45  45 GLU D    9  VAL D   15  5                                   7    
HELIX   46  46 SER D   38  SER D   50  1                                  13    
HELIX   47  47 ALA D   65  MET D   69  5                                   5    
HELIX   48  48 THR D   91  PHE D   93  5                                   3    
HELIX   49  49 SER D   97  ALA D  106  1                                  10    
HELIX   50  50 GLY D  107  MET D  112  5                                   6    
HELIX   51  51 PRO D  126  ARG D  131  1                                   6    
HELIX   52  52 PHE D  138  GLY D  148  1                                  11    
HELIX   53  53 SER D  166  GLY D  181  1                                  16    
HELIX   54  54 ARG D  198  GLY D  218  1                                  21    
HELIX   55  55 PRO D  230  GLU D  244  1                                  15    
HELIX   56  56 ILE D  253  GLY D  257  1                                   5    
HELIX   57  57 GLY D  257  GLY D  272  1                                  16    
HELIX   58  58 HIS D  282  ARG D  287  1                                   6    
HELIX   59  59 THR D  294  GLY D  306  1                                  13    
HELIX   60  60 ASN D  322  SER D  335  1                                  14    
HELIX   61  61 HIS D  352  GLY D  354  5                                   3    
HELIX   62  62 LEU D  355  GLY D  364  1                                  10    
HELIX   63  63 ALA D  371  HIS D  378  1                                   8    
HELIX   64  64 GLY D  381  GLU D  398  1                                  18    
HELIX   65  65 ASP D  401  LYS D  407  1                                   7    
HELIX   66  66 SER D  409  VAL D  419  1                                  11    
HELIX   67  67 TRP E   10  VAL E   15  5                                   6    
HELIX   68  68 SER E   38  SER E   50  1                                  13    
HELIX   69  69 ALA E   65  MET E   69  5                                   5    
HELIX   70  70 THR E   91  PHE E   93  5                                   3    
HELIX   71  71 SER E   97  ALA E  106  1                                  10    
HELIX   72  72 GLY E  107  MET E  112  5                                   6    
HELIX   73  73 PRO E  126  ARG E  131  1                                   6    
HELIX   74  74 PHE E  138  GLY E  148  1                                  11    
HELIX   75  75 SER E  166  GLY E  181  1                                  16    
HELIX   76  76 ARG E  198  GLY E  218  1                                  21    
HELIX   77  77 PRO E  230  GLU E  244  1                                  15    
HELIX   78  78 ILE E  253  GLY E  257  1                                   5    
HELIX   79  79 GLY E  257  GLY E  272  1                                  16    
HELIX   80  80 HIS E  282  ARG E  287  1                                   6    
HELIX   81  81 THR E  294  GLY E  306  1                                  13    
HELIX   82  82 ASN E  322  SER E  335  1                                  14    
HELIX   83  83 HIS E  352  GLY E  354  5                                   3    
HELIX   84  84 LEU E  355  GLY E  364  1                                  10    
HELIX   85  85 ALA E  371  HIS E  378  1                                   8    
HELIX   86  86 GLY E  381  GLY E  399  1                                  19    
HELIX   87  87 ASP E  401  ALA E  406  1                                   6    
HELIX   88  88 SER E  409  GLU E  418  1                                  10    
SHEET    1   A 2 LYS A   7  GLU A   9  0                                        
SHEET    2   A 2 TRP A  55  THR A  57 -1  O  THR A  57   N  LYS A   7           
SHEET    1   B 5 LYS A  71  HIS A  78  0                                        
SHEET    2   B 5 GLY A  81  TYR A  88 -1  O  ILE A  83   N  GLU A  76           
SHEET    3   B 5 LEU A  26  PRO A  34 -1  N  LEU A  26   O  TYR A  88           
SHEET    4   B 5 LEU A 115  HIS A 124 -1  O  LYS A 116   N  GLU A  33           
SHEET    5   B 5 GLY A 292  ILE A 293  1  O  GLY A 292   N  LEU A 120           
SHEET    1   C 8 GLU A 222  LEU A 224  0                                        
SHEET    2   C 8 LEU A 184  LYS A 186  1  N  LEU A 185   O  LEU A 224           
SHEET    3   C 8 LEU A 154  THR A 157  1  N  THR A 155   O  LEU A 184           
SHEET    4   C 8 VAL A 368  GLN A 370  1  O  ILE A 369   N  LEU A 154           
SHEET    5   C 8 PHE A 344  SER A 348  1  N  ALA A 347   O  GLN A 370           
SHEET    6   C 8 GLN A 309  HIS A 311  1  N  ILE A 310   O  PHE A 344           
SHEET    7   C 8 ALA A 274  HIS A 278  1  N  ALA A 277   O  GLN A 309           
SHEET    8   C 8 TYR A 248  ASP A 252  1  N  VAL A 249   O  HIS A 276           
SHEET    1   D 5 LYS B  71  HIS B  78  0                                        
SHEET    2   D 5 GLY B  81  TYR B  88 -1  O  GLY B  81   N  HIS B  78           
SHEET    3   D 5 LEU B  26  PRO B  34 -1  N  TYR B  30   O  ALA B  84           
SHEET    4   D 5 LEU B 115  HIS B 124 -1  O  ARG B 119   N  TYR B  31           
SHEET    5   D 5 GLY B 292  ILE B 293  1  O  GLY B 292   N  LEU B 120           
SHEET    1   E 8 GLU B 222  LEU B 224  0                                        
SHEET    2   E 8 LEU B 184  LYS B 186  1  N  LEU B 185   O  LEU B 224           
SHEET    3   E 8 LEU B 154  THR B 157  1  N  THR B 155   O  LEU B 184           
SHEET    4   E 8 VAL B 368  GLN B 370  1  O  ILE B 369   N  LEU B 154           
SHEET    5   E 8 PHE B 344  SER B 348  1  N  ALA B 347   O  GLN B 370           
SHEET    6   E 8 GLN B 309  HIS B 311  1  N  ILE B 310   O  VAL B 346           
SHEET    7   E 8 ALA B 274  HIS B 278  1  N  ALA B 277   O  GLN B 309           
SHEET    8   E 8 TYR B 248  ASP B 252  1  N  VAL B 249   O  HIS B 276           
SHEET    1   F 5 LYS D  71  HIS D  78  0                                        
SHEET    2   F 5 GLY D  81  PRO D  89 -1  O  ILE D  83   N  GLU D  76           
SHEET    3   F 5 GLU D  25  PRO D  34 -1  N  TYR D  30   O  ALA D  84           
SHEET    4   F 5 LEU D 115  HIS D 124 -1  O  LEU D 121   N  GLU D  29           
SHEET    5   F 5 GLY D 292  ILE D 293  1  O  GLY D 292   N  LEU D 118           
SHEET    1   G 8 GLU D 222  LEU D 224  0                                        
SHEET    2   G 8 LEU D 184  LYS D 186  1  N  LEU D 185   O  LEU D 224           
SHEET    3   G 8 LEU D 154  THR D 157  1  N  THR D 155   O  LEU D 184           
SHEET    4   G 8 VAL D 368  GLN D 370  1  O  ILE D 369   N  LEU D 154           
SHEET    5   G 8 PHE D 344  ALA D 347  1  N  ALA D 347   O  GLN D 370           
SHEET    6   G 8 GLN D 309  HIS D 311  1  N  ILE D 310   O  VAL D 346           
SHEET    7   G 8 ALA D 274  HIS D 278  1  N  ALA D 277   O  GLN D 309           
SHEET    8   G 8 TYR D 248  ASP D 252  1  N  VAL D 249   O  HIS D 276           
SHEET    1   H 5 LYS E  71  HIS E  78  0                                        
SHEET    2   H 5 GLY E  81  PRO E  89 -1  O  GLY E  81   N  HIS E  78           
SHEET    3   H 5 GLU E  25  PRO E  34 -1  N  LEU E  26   O  TYR E  88           
SHEET    4   H 5 LEU E 115  HIS E 124 -1  O  ARG E 119   N  TYR E  31           
SHEET    5   H 5 GLY E 292  ILE E 293  1  O  GLY E 292   N  LEU E 120           
SHEET    1   I 8 GLU E 222  LEU E 224  0                                        
SHEET    2   I 8 LEU E 184  LYS E 186  1  N  LEU E 185   O  LEU E 224           
SHEET    3   I 8 LEU E 154  THR E 157  1  N  THR E 155   O  LEU E 184           
SHEET    4   I 8 VAL E 368  GLN E 370  1  O  ILE E 369   N  LEU E 154           
SHEET    5   I 8 PHE E 344  ALA E 347  1  N  ALA E 347   O  GLN E 370           
SHEET    6   I 8 GLN E 309  HIS E 311  1  N  ILE E 310   O  VAL E 346           
SHEET    7   I 8 ALA E 274  HIS E 278  1  N  ALA E 277   O  GLN E 309           
SHEET    8   I 8 TYR E 248  ASP E 252  1  N  VAL E 249   O  HIS E 276           
CISPEP   1 LYS A  160    PRO A  161          0        -3.45                     
CISPEP   2 LYS B  160    PRO B  161          0        -1.36                     
CISPEP   3 LYS D  160    PRO D  161          0        -0.21                     
CISPEP   4 LYS E  160    PRO E  161          0         2.35                     
SITE     1 AC1  8 LYS A 160  GLY A 349  GLY A 350  GLN A 370                    
SITE     2 AC1  8 GLY A 372  GLY A 373  HOH A1094  HOH A1135                    
SITE     1 AC2  5 ARG A 279  HIS A 311  HOH A1141  HOH A1200                    
SITE     2 AC2  5 HOH A1217                                                     
SITE     1 AC3  4 TYR A  31  HIS A  78  ARG A 119  PRO A 289                    
SITE     1 AC4  5 GLY A 148  VAL A 149  LYS A 150  ASP A 151                    
SITE     2 AC4  5 ARG A 152                                                     
SITE     1 AC5  4 LYS A 205  ARG A 208  VAL A 209  ARG A 212                    
SITE     1 AC6  7 GLY B 349  GLY B 350  GLN B 370  GLY B 372                    
SITE     2 AC6  7 GLY B 373  HOH B2076  HOH B2077                               
SITE     1 AC7  6 ARG B 279  HIS B 311  SER B 348  HOH B2149                    
SITE     2 AC7  6 HOH B2150  HOH B2155                                          
SITE     1 AC8  6 TYR B  31  HIS B  78  ARG B 119  LEU B 121                    
SITE     2 AC8  6 PRO B 289  HOH B2082                                          
SITE     1 AC9  3 GLY B 148  VAL B 149  ARG B 152                               
SITE     1 BC1  4 LYS B 205  ARG B 208  VAL B 209  ARG B 212                    
SITE     1 BC2  8 LYS D 160  GLY D 349  GLY D 350  GLN D 370                    
SITE     2 BC2  8 GLY D 372  GLY D 373  HOH D3025  HOH D3108                    
SITE     1 BC3  3 ARG D 279  HIS D 311  HOH D3147                               
SITE     1 BC4  5 TYR D  31  HIS D  78  ARG D 119  PRO D 289                    
SITE     2 BC4  5 HOH D3129                                                     
SITE     1 BC5  3 GLY D 148  VAL D 149  ARG D 152                               
SITE     1 BC6  7 LYS E 160  GLY E 350  GLN E 370  GLY E 372                    
SITE     2 BC6  7 GLY E 373  HOH E4157  HOH E4175                               
SITE     1 BC7  5 ARG E 279  HIS E 311  SER E 348  HOH E4146                    
SITE     2 BC7  5 HOH E4147                                                     
SITE     1 BC8  3 TYR E  31  HIS E  78  PRO E 289                               
SITE     1 BC9  5 GLY E 148  VAL E 149  LYS E 150  ASP E 151                    
SITE     2 BC9  5 ARG E 152                                                     
SITE     1 CC1  3 LYS E 205  ARG E 208  VAL E 209                               
CRYST1  172.591  148.774  108.452  90.00 126.49  90.00 C 1 2 1      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      0.005794  0.000000  0.004285        0.00000                         
SCALE2      0.000000  0.006722  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011468        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system