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Database: PDB
Entry: 2CWX
LinkDB: 2CWX
Original site: 2CWX 
HEADER    LYASE                                   27-JUN-05   2CWX              
TITLE     CRYSTAL STRUCTURE OF OCTAMERIC RIBULOSE-1,5-BISPHOSPHATE              
TITLE    2 CARBOXYLASE/OXYGENASE (RUBISCO) FROM PYROCOCCUS HORIKOSHII OT3 (FORM-
TITLE    3 1 CRYSTAL)                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE;                         
COMPND   3 CHAIN: A, E;                                                         
COMPND   4 SYNONYM: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE, RUBISCO;   
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: PET                                       
KEYWDS    LYASE, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN       
KEYWDS   2 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL                 
KEYWDS   3 GENOMICS/PROTEOMICS INITIATIVE, RSGI                                 
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 2CWX    1       VERSN                                    
REVDAT   2   24-FEB-09 2CWX    1       VERSN                                    
REVDAT   1   27-DEC-05 2CWX    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 OCTAMERIC RIBULOSE-1,5-BISPHOSPHATE     
JRNL        TITL 2 CARBOXYLASE/OXYGENASE (RUBISCO) FROM PYROCOCCUS HORIKOSHII   
JRNL        TITL 3 OT3 (FORM-1 CRYSTAL)                                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 68293                          
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) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3636                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4968                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2280                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 260                          
REMARK   3   BIN FREE R VALUE                    : 0.2700                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6493                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 469                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 22.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.35                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 0.12000                                              
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): 0.149         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.137         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.098         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.559         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6648 ; 0.016 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  6124 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8979 ; 1.494 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14218 ; 0.863 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   819 ; 6.544 ; 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):   952 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7403 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1394 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1428 ; 0.209 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  7247 ; 0.238 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3914 ; 0.087 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   284 ; 0.191 ; 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):    19 ; 0.304 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    89 ; 0.334 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.223 ; 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):  4071 ; 0.919 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6516 ; 1.789 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2577 ; 2.763 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2463 ; 4.679 ; 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     8        A   424                          
REMARK   3    ORIGIN FOR THE GROUP (A):  65.2012  35.0383  41.5877              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0815 T22:   0.0359                                     
REMARK   3      T33:   0.1138 T12:  -0.0117                                     
REMARK   3      T13:  -0.0464 T23:  -0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8727 L22:   0.2819                                     
REMARK   3      L33:   0.6440 L12:   0.2875                                     
REMARK   3      L13:   0.1888 L23:   0.2690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0225 S12:  -0.1140 S13:   0.1628                       
REMARK   3      S21:  -0.0078 S22:  -0.0888 S23:   0.0663                       
REMARK   3      S31:  -0.0764 S32:   0.0057 S33:   0.1113                       
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 :   E    10        E   417                          
REMARK   3    ORIGIN FOR THE GROUP (A):  74.7895  35.1123  16.0648              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1090 T22:   0.0541                                     
REMARK   3      T33:   0.0875 T12:  -0.0017                                     
REMARK   3      T13:  -0.0451 T23:   0.0559                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9801 L22:   0.4031                                     
REMARK   3      L33:   0.6194 L12:   0.3520                                     
REMARK   3      L13:   0.0502 L23:   0.1316                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0482 S12:   0.1829 S13:   0.1670                       
REMARK   3      S21:  -0.0681 S22:   0.0210 S23:   0.0315                       
REMARK   3      S31:  -0.0849 S32:  -0.0065 S33:   0.0272                       
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 2CWX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUL-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB024718.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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   : 71958                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
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: NULL                         
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NACL, PEG6000, TRIS, PH 8, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z                                          
REMARK 290       4555   Y+1/2,-X+1/2,Z                                          
REMARK 290       5555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       6555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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  0.000000 -1.000000  0.000000       71.99600            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       71.99600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       71.99600            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       71.99600            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       71.99600            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       71.99600            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       71.99600            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       71.99600            
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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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   BIOMT1   2 -1.000000  0.000000  0.000000      143.99200            
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       71.99600            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000      -71.99600            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000       71.99600            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000       71.99600            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 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 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     MET A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     ARG A     5                                                      
REMARK 465     MET A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     TRP A    55                                                      
REMARK 465     THR A    56                                                      
REMARK 465     THR A    57                                                      
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 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     GLU E     9                                                      
REMARK 465     GLU E   418                                                      
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLU E    95     O    HOH E   585              2.11            
REMARK 500   O    GLU E    63     O    HOH E   535              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH E   609     O    HOH E   651     4555     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 266   CD    GLU A 266   OE1     0.072                       
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 151   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    VAL A 231   CB  -  CA  -  C   ANGL. DEV. = -11.5 DEGREES          
REMARK 500    ASP A 331   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP E  16   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP E 391   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 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     -108.92   -127.17                                   
REMARK 500    LEU A  61      104.00    -56.71                                   
REMARK 500    THR A 192      -81.54   -106.87                                   
REMARK 500    ASN A 197       81.42   -157.28                                   
REMARK 500    MET A 281      -14.13     88.54                                   
REMARK 500    LYS A 318      -73.21    -46.20                                   
REMARK 500    TRP A 337       73.06   -152.53                                   
REMARK 500    GLU A 338     -132.76     56.82                                   
REMARK 500    SER E  51     -109.84   -133.65                                   
REMARK 500    TRP E  55      135.29    169.55                                   
REMARK 500    THR E  56       23.15   -145.01                                   
REMARK 500    THR E  57      -87.54    -73.16                                   
REMARK 500    TRP E  59       67.61     66.94                                   
REMARK 500    LYS E  60      106.03     44.04                                   
REMARK 500    ASP E 151      -54.87   -124.32                                   
REMARK 500    THR E 192      -79.71   -111.12                                   
REMARK 500    ASN E 197       77.78   -158.01                                   
REMARK 500    MET E 281      -16.54     90.38                                   
REMARK 500    VAL E 316     -137.72   -151.28                                   
REMARK 500    ALA E 320      -94.56     63.36                                   
REMARK 500    TRP E 337       78.76   -152.62                                   
REMARK 500    GLU E 338     -122.04     46.95                                   
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   54     TRP E   55                  142.83                    
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 A 439        DISTANCE =  7.93 ANGSTROMS                       
REMARK 525    HOH A 478        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH A 479        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH A 491        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH A 522        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH A 528        DISTANCE =  5.49 ANGSTROMS                       
REMARK 525    HOH A 535        DISTANCE =  7.56 ANGSTROMS                       
REMARK 525    HOH A 550        DISTANCE =  9.44 ANGSTROMS                       
REMARK 525    HOH A 558        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH A 566        DISTANCE =  7.07 ANGSTROMS                       
REMARK 525    HOH A 567        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH A 578        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH A 586        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH A 603        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH A 612        DISTANCE =  7.35 ANGSTROMS                       
REMARK 525    HOH A 620        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH A 621        DISTANCE =  5.69 ANGSTROMS                       
REMARK 525    HOH A 631        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH A 642        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH A 643        DISTANCE =  5.60 ANGSTROMS                       
REMARK 525    HOH A 645        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH A 649        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH A 654        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH A 656        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH A 673        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH A 675        DISTANCE = 11.39 ANGSTROMS                       
REMARK 525    HOH E 533        DISTANCE =  7.90 ANGSTROMS                       
REMARK 525    HOH E 552        DISTANCE =  5.51 ANGSTROMS                       
REMARK 525    HOH E 558        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH E 559        DISTANCE = 10.00 ANGSTROMS                       
REMARK 525    HOH E 573        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH E 618        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH E 631        DISTANCE =  6.93 ANGSTROMS                       
REMARK 525    HOH E 637        DISTANCE =  5.71 ANGSTROMS                       
REMARK 525    HOH E 639        DISTANCE =  5.77 ANGSTROMS                       
REMARK 525    HOH E 643        DISTANCE =  6.42 ANGSTROMS                       
REMARK 525    HOH E 644        DISTANCE =  7.45 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2CXE   RELATED DB: PDB                                   
REMARK 900 FORM-2 CRYSTAL                                                       
REMARK 900 RELATED ID: PHO001000939.2   RELATED DB: TARGETDB                    
DBREF  2CWX A    1   430  UNP    O58677   RBL_PYRHO        1    430             
DBREF  2CWX 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 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                                                          
FORMUL   3  HOH   *469(H2 O)                                                    
HELIX    1   1 VAL A    8  ASP A   13  1                                   6    
HELIX    2   2 SER A   38  SER A   50  1                                  13    
HELIX    3   3 PRO A   62  SER A   68  1                                   7    
HELIX    4   4 THR A   91  PHE A   93  5                                   3    
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  181  1                                  16    
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  LYS A  407  1                                   7    
HELIX   22  22 SER A  409  SER A  422  1                                  14    
HELIX   23  23 TRP E   10  VAL E   15  5                                   6    
HELIX   24  24 SER E   38  SER E   50  1                                  13    
HELIX   25  25 ALA E   65  MET E   69  5                                   5    
HELIX   26  26 PRO E   89  PHE E   93  5                                   5    
HELIX   27  27 SER E   97  ALA E  106  1                                  10    
HELIX   28  28 GLY E  107  MET E  112  5                                   6    
HELIX   29  29 PRO E  126  ARG E  131  1                                   6    
HELIX   30  30 PHE E  138  GLY E  148  1                                  11    
HELIX   31  31 SER E  166  GLY E  181  1                                  16    
HELIX   32  32 ARG E  198  GLY E  218  1                                  21    
HELIX   33  33 PRO E  230  GLU E  244  1                                  15    
HELIX   34  34 ILE E  253  GLY E  257  1                                   5    
HELIX   35  35 GLY E  257  GLY E  272  1                                  16    
HELIX   36  36 HIS E  282  ARG E  287  1                                   6    
HELIX   37  37 THR E  294  GLY E  306  1                                  13    
HELIX   38  38 ASN E  322  SER E  335  1                                  14    
HELIX   39  39 HIS E  352  GLY E  354  5                                   3    
HELIX   40  40 LEU E  355  GLY E  364  1                                  10    
HELIX   41  41 ALA E  371  GLY E  377  1                                   7    
HELIX   42  42 GLY E  381  GLU E  398  1                                  18    
HELIX   43  43 ASP E  401  LYS E  407  1                                   7    
HELIX   44  44 SER E  409  ARG E  417  1                                   9    
SHEET    1   A 5 LYS A  71  HIS A  78  0                                        
SHEET    2   A 5 GLY A  81  PRO A  89 -1  O  ALA A  87   N  LYS A  71           
SHEET    3   A 5 GLU A  25  PRO A  34 -1  N  LEU A  26   O  TYR A  88           
SHEET    4   A 5 LEU A 115  HIS A 124 -1  O  LYS A 116   N  GLU A  33           
SHEET    5   A 5 GLY A 292  ILE A 293  1  O  GLY A 292   N  LEU A 120           
SHEET    1   B 8 GLU A 222  LEU A 224  0                                        
SHEET    2   B 8 LEU A 184  LYS A 186  1  N  LEU A 185   O  LEU A 224           
SHEET    3   B 8 LEU A 154  THR A 157  1  N  THR A 155   O  LEU A 184           
SHEET    4   B 8 VAL A 368  GLN A 370  1  O  ILE A 369   N  LEU A 154           
SHEET    5   B 8 PHE A 344  ALA A 347  1  N  ALA A 347   O  GLN A 370           
SHEET    6   B 8 GLN A 309  HIS A 311  1  N  ILE A 310   O  VAL A 346           
SHEET    7   B 8 ALA A 274  HIS A 278  1  N  ALA A 277   O  GLN A 309           
SHEET    8   B 8 TYR A 248  ASP A 252  1  N  VAL A 249   O  HIS A 276           
SHEET    1   C 5 LYS E  71  HIS E  78  0                                        
SHEET    2   C 5 GLY E  81  TYR E  88 -1  O  GLY E  81   N  HIS E  78           
SHEET    3   C 5 LEU E  26  PRO E  34 -1  N  LEU E  26   O  TYR E  88           
SHEET    4   C 5 LEU E 115  HIS E 124 -1  O  ASP E 122   N  GLU E  29           
SHEET    5   C 5 GLY E 292  ILE E 293  1  O  GLY E 292   N  LEU E 120           
SHEET    1   D 8 GLU E 222  LEU E 224  0                                        
SHEET    2   D 8 LEU E 184  LYS E 186  1  N  LEU E 185   O  LEU E 224           
SHEET    3   D 8 LEU E 154  THR E 157  1  N  THR E 155   O  LEU E 184           
SHEET    4   D 8 VAL E 368  GLN E 370  1  O  ILE E 369   N  LEU E 154           
SHEET    5   D 8 PHE E 344  SER E 348  1  N  ALA E 347   O  GLN E 370           
SHEET    6   D 8 GLN E 309  HIS E 311  1  N  ILE E 310   O  PHE E 344           
SHEET    7   D 8 ALA E 274  HIS E 278  1  N  ALA E 277   O  GLN E 309           
SHEET    8   D 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         0.89                     
CISPEP   2 LYS E  160    PRO E  161          0        -3.75                     
CRYST1  143.992  143.992  101.417  90.00  90.00  90.00 P 4 21 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      0.006945  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006945  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009860        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system