GenomeNet

Database: PDB
Entry: 3H2E
LinkDB: 3H2E
Original site: 3H2E 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       14-APR-09   3H2E              
TITLE     STRUCTURAL STUDIES OF PTERIN-BASED INHIBITORS OF DIHYDROPTEROATE      
TITLE    2 SYNTHASE                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROPTEROATE SYNTHASE;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.5.1.15;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS STR. A2012;                  
SOURCE   3 ORGANISM_TAXID: 191218;                                              
SOURCE   4 GENE: FOLP, BAO_0074;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-28A                                   
KEYWDS    ANTHRACIS, FOLATE BIOSYNTHESIS, DIHYDROPTEROATE, PTERINE,             
KEYWDS   2 TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.-K.YUN,S.W.WHITE                                                    
REVDAT   3   13-JUL-11 3H2E    1       VERSN                                    
REVDAT   2   26-JAN-10 3H2E    1       JRNL                                     
REVDAT   1   08-DEC-09 3H2E    0                                                
JRNL        AUTH   K.E.HEVENER,M.K.YUN,J.QI,I.D.KERR,K.BABAOGLU,J.G.HURDLE,     
JRNL        AUTH 2 K.BALAKRISHNA,S.W.WHITE,R.E.LEE                              
JRNL        TITL   STRUCTURAL STUDIES OF PTERIN-BASED INHIBITORS OF             
JRNL        TITL 2 DIHYDROPTEROATE SYNTHASE.                                    
JRNL        REF    J.MED.CHEM.                   V.  53   166 2010              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   19899766                                                     
JRNL        DOI    10.1021/JM900861D                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 48.21                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 48547                          
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) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2447                            
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) : 2050                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 58.14                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2240                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 101                          
REMARK   3   BIN FREE R VALUE                    : 0.2650                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4131                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 73                                      
REMARK   3   SOLVENT ATOMS            : 256                                     
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) : 40.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.43000                                              
REMARK   3    B22 (A**2) : 1.43000                                              
REMARK   3    B33 (A**2) : -2.15000                                             
REMARK   3    B12 (A**2) : 0.72000                                              
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): 0.167         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.153         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.111         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.966         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4267 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5765 ; 1.317 ; 1.990       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   533 ; 5.240 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   187 ;30.220 ;25.080       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   785 ;15.785 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;18.807 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   643 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3141 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1780 ; 0.202 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2915 ; 0.298 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   228 ; 0.137 ; 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):    72 ; 0.194 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.350 ; 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):  2743 ; 1.007 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4255 ; 1.482 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1810 ; 2.340 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1508 ; 3.786 ; 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     2        A   274                          
REMARK   3    ORIGIN FOR THE GROUP (A): -78.4390  80.8340  91.3390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0782 T22:  -0.0335                                     
REMARK   3      T33:  -0.2085 T12:   0.1137                                     
REMARK   3      T13:   0.0103 T23:   0.0289                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3800 L22:   0.8962                                     
REMARK   3      L33:   2.0022 L12:  -0.0702                                     
REMARK   3      L13:   0.5303 L23:   0.0871                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0288 S12:   0.0071 S13:  -0.0025                       
REMARK   3      S21:   0.0645 S22:   0.0322 S23:   0.0277                       
REMARK   3      S31:   0.0236 S32:   0.1465 S33:  -0.0035                       
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     2        B   274                          
REMARK   3    ORIGIN FOR THE GROUP (A): -68.2670  61.3510 138.4260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0559 T22:  -0.1046                                     
REMARK   3      T33:  -0.1959 T12:  -0.0151                                     
REMARK   3      T13:  -0.0453 T23:   0.0352                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7923 L22:   1.1985                                     
REMARK   3      L33:   1.5735 L12:   0.0247                                     
REMARK   3      L13:  -0.2446 L23:  -0.2525                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0089 S12:   0.0538 S13:  -0.0109                       
REMARK   3      S21:  -0.1512 S22:  -0.0733 S23:  -0.0245                       
REMARK   3      S31:  -0.2367 S32:   0.0908 S33:   0.0822                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3H2E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052605.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48615                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.210                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : 11.500                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 32.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 60.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.34600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1TX0                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM SULFATE, PROPANE, BIS-TRIS, PH   
REMARK 280  9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+2/3                                            
REMARK 290       6555   X-Y,X,Z+1/3                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+2/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+1/3                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      175.96333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       87.98167            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      175.96333            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       87.98167            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      175.96333            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       87.98167            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      175.96333            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       87.98167            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -108.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     -196.12600            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      169.85010            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL                        
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     -147.09450            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       84.92505            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A   275                                                      
REMARK 465     VAL A   276                                                      
REMARK 465     LYS A   277                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B    30                                                      
REMARK 465     ASP B    31                                                      
REMARK 465     SER B    32                                                      
REMARK 465     PHE B    33                                                      
REMARK 465     GLU B    65                                                      
REMARK 465     SER B    66                                                      
REMARK 465     THR B    67                                                      
REMARK 465     ARG B    68                                                      
REMARK 465     PRO B    69                                                      
REMARK 465     GLY B    70                                                      
REMARK 465     PHE B    71                                                      
REMARK 465     ALA B    72                                                      
REMARK 465     LYS B    73                                                      
REMARK 465     GLY B   275                                                      
REMARK 465     VAL B   276                                                      
REMARK 465     LYS B   277                                                      
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    ASN B  27      100.84    -59.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 278                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 279                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 280                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 281                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B59 B 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B59 B 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 278                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 279                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 280                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 281                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1TWW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1TWZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1TX0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1TX2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1TWS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H21   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H22   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H23   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H24   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H26   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H2A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H2C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H2F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H2M   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H2N   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H2O   RELATED DB: PDB                                   
DBREF  3H2E A    1   277  UNP    B1UXN2   B1UXN2_BACAN     1    277             
DBREF  3H2E B    1   277  UNP    B1UXN2   B1UXN2_BACAN     1    277             
SEQADV 3H2E MET A  -19  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E GLY A  -18  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E SER A  -17  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E SER A  -16  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E HIS A  -15  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E HIS A  -14  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E HIS A  -13  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E HIS A  -12  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E HIS A  -11  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E HIS A  -10  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E SER A   -9  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E SER A   -8  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E GLY A   -7  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E LEU A   -6  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E VAL A   -5  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E PRO A   -4  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E ARG A   -3  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E GLY A   -2  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E SER A   -1  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E HIS A    0  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E MET B  -19  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E GLY B  -18  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E SER B  -17  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E SER B  -16  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E HIS B  -15  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E HIS B  -14  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E HIS B  -13  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E HIS B  -12  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E HIS B  -11  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E HIS B  -10  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E SER B   -9  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E SER B   -8  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E GLY B   -7  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E LEU B   -6  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E VAL B   -5  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E PRO B   -4  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E ARG B   -3  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E GLY B   -2  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E SER B   -1  UNP  B1UXN2              EXPRESSION TAG                 
SEQADV 3H2E HIS B    0  UNP  B1UXN2              EXPRESSION TAG                 
SEQRES   1 A  297  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  297  LEU VAL PRO ARG GLY SER HIS MET LYS TRP ASP TYR ASP          
SEQRES   3 A  297  LEU ARG CYS GLY GLU TYR THR LEU ASN LEU ASN GLU LYS          
SEQRES   4 A  297  THR LEU ILE MET GLY ILE LEU ASN VAL THR PRO ASP SER          
SEQRES   5 A  297  PHE SER ASP GLY GLY SER TYR ASN GLU VAL ASP ALA ALA          
SEQRES   6 A  297  VAL ARG HIS ALA LYS GLU MET ARG ASP GLU GLY ALA HIS          
SEQRES   7 A  297  ILE ILE ASP ILE GLY GLY GLU SER THR ARG PRO GLY PHE          
SEQRES   8 A  297  ALA LYS VAL SER VAL GLU GLU GLU ILE LYS ARG VAL VAL          
SEQRES   9 A  297  PRO MET ILE GLN ALA VAL SER LYS GLU VAL LYS LEU PRO          
SEQRES  10 A  297  ILE SER ILE ASP THR TYR LYS ALA GLU VAL ALA LYS GLN          
SEQRES  11 A  297  ALA ILE GLU ALA GLY ALA HIS ILE ILE ASN ASP ILE TRP          
SEQRES  12 A  297  GLY ALA LYS ALA GLU PRO LYS ILE ALA GLU VAL ALA ALA          
SEQRES  13 A  297  HIS TYR ASP VAL PRO ILE ILE LEU MET HIS ASN ARG ASP          
SEQRES  14 A  297  ASN MET ASN TYR ARG ASN LEU MET ALA ASP MET ILE ALA          
SEQRES  15 A  297  ASP LEU TYR ASP SER ILE LYS ILE ALA LYS ASP ALA GLY          
SEQRES  16 A  297  VAL ARG ASP GLU ASN ILE ILE LEU ASP PRO GLY ILE GLY          
SEQRES  17 A  297  PHE ALA LYS THR PRO GLU GLN ASN LEU GLU ALA MET ARG          
SEQRES  18 A  297  ASN LEU GLU GLN LEU ASN VAL LEU GLY TYR PRO VAL LEU          
SEQRES  19 A  297  LEU GLY THR SER ARG LYS SER PHE ILE GLY HIS VAL LEU          
SEQRES  20 A  297  ASP LEU PRO VAL GLU GLU ARG LEU GLU GLY THR GLY ALA          
SEQRES  21 A  297  THR VAL CYS LEU GLY ILE GLU LYS GLY CYS GLU PHE VAL          
SEQRES  22 A  297  ARG VAL HIS ASP VAL LYS GLU MET SER ARG MET ALA LYS          
SEQRES  23 A  297  MET MET ASP ALA MET ILE GLY LYS GLY VAL LYS                  
SEQRES   1 B  297  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  297  LEU VAL PRO ARG GLY SER HIS MET LYS TRP ASP TYR ASP          
SEQRES   3 B  297  LEU ARG CYS GLY GLU TYR THR LEU ASN LEU ASN GLU LYS          
SEQRES   4 B  297  THR LEU ILE MET GLY ILE LEU ASN VAL THR PRO ASP SER          
SEQRES   5 B  297  PHE SER ASP GLY GLY SER TYR ASN GLU VAL ASP ALA ALA          
SEQRES   6 B  297  VAL ARG HIS ALA LYS GLU MET ARG ASP GLU GLY ALA HIS          
SEQRES   7 B  297  ILE ILE ASP ILE GLY GLY GLU SER THR ARG PRO GLY PHE          
SEQRES   8 B  297  ALA LYS VAL SER VAL GLU GLU GLU ILE LYS ARG VAL VAL          
SEQRES   9 B  297  PRO MET ILE GLN ALA VAL SER LYS GLU VAL LYS LEU PRO          
SEQRES  10 B  297  ILE SER ILE ASP THR TYR LYS ALA GLU VAL ALA LYS GLN          
SEQRES  11 B  297  ALA ILE GLU ALA GLY ALA HIS ILE ILE ASN ASP ILE TRP          
SEQRES  12 B  297  GLY ALA LYS ALA GLU PRO LYS ILE ALA GLU VAL ALA ALA          
SEQRES  13 B  297  HIS TYR ASP VAL PRO ILE ILE LEU MET HIS ASN ARG ASP          
SEQRES  14 B  297  ASN MET ASN TYR ARG ASN LEU MET ALA ASP MET ILE ALA          
SEQRES  15 B  297  ASP LEU TYR ASP SER ILE LYS ILE ALA LYS ASP ALA GLY          
SEQRES  16 B  297  VAL ARG ASP GLU ASN ILE ILE LEU ASP PRO GLY ILE GLY          
SEQRES  17 B  297  PHE ALA LYS THR PRO GLU GLN ASN LEU GLU ALA MET ARG          
SEQRES  18 B  297  ASN LEU GLU GLN LEU ASN VAL LEU GLY TYR PRO VAL LEU          
SEQRES  19 B  297  LEU GLY THR SER ARG LYS SER PHE ILE GLY HIS VAL LEU          
SEQRES  20 B  297  ASP LEU PRO VAL GLU GLU ARG LEU GLU GLY THR GLY ALA          
SEQRES  21 B  297  THR VAL CYS LEU GLY ILE GLU LYS GLY CYS GLU PHE VAL          
SEQRES  22 B  297  ARG VAL HIS ASP VAL LYS GLU MET SER ARG MET ALA LYS          
SEQRES  23 B  297  MET MET ASP ALA MET ILE GLY LYS GLY VAL LYS                  
MODRES 3H2E LYS B  109  LYS  COVALENT                                           
HET    SO4  A 278       5                                                       
HET    SO4  A 279       5                                                       
HET    SO4  A 280       5                                                       
HET    SO4  A 281       5                                                       
HET    B59  B 901      17                                                       
HET    B59  B 902      16                                                       
HET    SO4  B 278       5                                                       
HET    SO4  B 279       5                                                       
HET    SO4  B 280       5                                                       
HET    SO4  B 281       5                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     B59 1,3-DIMETHYL-2,4,7-TRIOXO-1,2,3,4,7,8-                           
HETNAM   2 B59  HEXAHYDROPTERIDINE-6-CARBALDEHYDE                               
FORMUL   3  SO4    8(O4 S 2-)                                                   
FORMUL   7  B59    2(C9 H8 N4 O4)                                               
FORMUL  13  HOH   *256(H2 O)                                                    
HELIX    1   1 SER A   38  GLU A   55  1                                  18    
HELIX    2   2 SER A   75  VAL A   94  1                                  20    
HELIX    3   3 LYS A  104  GLY A  115  1                                  12    
HELIX    4   4 PRO A  129  ASP A  139  1                                  11    
HELIX    5   5 ASN A  155  ALA A  174  1                                  20    
HELIX    6   6 ARG A  177  GLU A  179  5                                   3    
HELIX    7   7 THR A  192  ASN A  202  1                                  11    
HELIX    8   8 LEU A  203  GLY A  210  5                                   8    
HELIX    9   9 LYS A  220  ASP A  228  1                                   9    
HELIX   10  10 PRO A  230  GLU A  233  5                                   4    
HELIX   11  11 ARG A  234  LYS A  248  1                                  15    
HELIX   12  12 ASP A  257  GLY A  273  1                                  17    
HELIX   13  13 SER B   38  GLU B   55  1                                  18    
HELIX   14  14 SER B   75  VAL B   94  1                                  20    
HELIX   15  15 LYS B  104  GLY B  115  1                                  12    
HELIX   16  16 PRO B  129  ASP B  139  1                                  11    
HELIX   17  17 ASN B  155  ALA B  174  1                                  20    
HELIX   18  18 ARG B  177  GLU B  179  5                                   3    
HELIX   19  19 THR B  192  ASN B  202  1                                  11    
HELIX   20  20 LEU B  203  GLY B  210  5                                   8    
HELIX   21  21 LYS B  220  ASP B  228  1                                   9    
HELIX   22  22 PRO B  230  GLU B  233  5                                   4    
HELIX   23  23 ARG B  234  LYS B  248  1                                  15    
HELIX   24  24 ASP B  257  GLY B  273  1                                  17    
SHEET    1   A 2 LEU A   7  CYS A   9  0                                        
SHEET    2   A 2 TYR A  12  LEU A  14 -1  O  LEU A  14   N  LEU A   7           
SHEET    1   B 8 ILE A 181  ASP A 184  0                                        
SHEET    2   B 8 ILE A 142  MET A 145  1  N  LEU A 144   O  ILE A 182           
SHEET    3   B 8 ILE A 118  ASP A 121  1  N  ILE A 119   O  ILE A 143           
SHEET    4   B 8 ILE A  98  ASP A 101  1  N  ILE A 100   O  ASN A 120           
SHEET    5   B 8 ILE A  59  GLY A  63  1  N  ILE A  62   O  SER A  99           
SHEET    6   B 8 LEU A  21  ASN A  27  1  N  LEU A  26   O  ASP A  61           
SHEET    7   B 8 PHE A 252  VAL A 255  1  O  VAL A 253   N  MET A  23           
SHEET    8   B 8 LEU A 214  LEU A 215  1  N  LEU A 215   O  ARG A 254           
SHEET    1   C 2 LEU B   7  CYS B   9  0                                        
SHEET    2   C 2 TYR B  12  LEU B  14 -1  O  LEU B  14   N  LEU B   7           
SHEET    1   D 8 ILE B 181  ASP B 184  0                                        
SHEET    2   D 8 ILE B 142  MET B 145  1  N  LEU B 144   O  ILE B 182           
SHEET    3   D 8 ILE B 118  ASP B 121  1  N  ILE B 119   O  ILE B 143           
SHEET    4   D 8 ILE B  98  ASP B 101  1  N  ILE B 100   O  ASN B 120           
SHEET    5   D 8 ILE B  59  GLY B  63  1  N  ILE B  62   O  SER B  99           
SHEET    6   D 8 LEU B  21  ILE B  25  1  N  GLY B  24   O  ASP B  61           
SHEET    7   D 8 PHE B 252  VAL B 255  1  O  VAL B 253   N  MET B  23           
SHEET    8   D 8 LEU B 214  LEU B 215  1  N  LEU B 215   O  ARG B 254           
LINK         NZ  LYS B 109                 C11 B59 B 902     1555   1555  1.28  
CISPEP   1 ARG A   68    PRO A   69          0         3.90                     
SITE     1 AC1  7 ASN A  27  ARG A  68  PRO A  69  ARG A 254                    
SITE     2 AC1  7 HIS A 256  HOH A 295  HOH A 395                               
SITE     1 AC2  3 LYS A  50  ARG A  53  HOH A 331                               
SITE     1 AC3  1 ARG A 219                                                     
SITE     1 AC4  2 SER A 221  ARG A 234                                          
SITE     1 AC5  6 PHE A  33  LYS B  81  LYS B 109  HIS B 137                    
SITE     2 AC5  6 TYR B 138  B59 B 902                                          
SITE     1 AC6  6 LYS B  81  GLN B  88  LYS B 109  GLN B 110                    
SITE     2 AC6  6 HOH B 391  B59 B 901                                          
SITE     1 AC7  4 ARG B 254  HIS B 256  HOH B 360  HOH B 368                    
SITE     1 AC8  2 ASN B  27  ARG B 219                                          
SITE     1 AC9  2 LYS B  50  ARG B  53                                          
SITE     1 BC1  3 SER B 221  ARG B 234  HOH B 400                               
CRYST1   98.063   98.063  263.945  90.00  90.00 120.00 P 62 2 2     24          
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      0.010198  0.005888  0.000000        0.00000                         
SCALE2      0.000000  0.011775  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003789        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system