GenomeNet

Database: PDB
Entry: 3R74
LinkDB: 3R74
Original site: 3R74 
HEADER    LYASE, BIOSYNTHETIC PROTEIN             22-MAR-11   3R74              
TITLE     CRYSTAL STRUCTURE OF 2-AMINO-2-DESOXYISOCHORISMATE SYNTHASE (ADIC)    
TITLE    2 SYNTHASE PHZE FROM BURKHOLDERIA LATA 383                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANTHRANILATE/PARA-AMINOBENZOATE SYNTHASES COMPONENT I;     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 4.1.3.27;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA SP.;                               
SOURCE   3 ORGANISM_TAXID: 269483;                                              
SOURCE   4 STRAIN: 383;                                                         
SOURCE   5 GENE: BCEP18194_B1570;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 PLYS S;                          
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET19MODTEV                               
KEYWDS    AMMONIA CHANNEL, CHORISMATE, TYPE 1 GLUTAMINE AMIDOTRANSFERASE,       
KEYWDS   2 PHENAZINE BIOSYNTHESIS, LYASE, SYNTHASE, BIOSYNTHETIC PROTEIN        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.A.LI,D.V.MAVRODI,L.S.THOMASHOW,M.ROESSLE,W.BLANKENFELDT             
REVDAT   4   21-FEB-24 3R74    1       SEQADV                                   
REVDAT   3   01-JUN-11 3R74    1       JRNL                                     
REVDAT   2   13-APR-11 3R74    1       JRNL                                     
REVDAT   1   30-MAR-11 3R74    0                                                
JRNL        AUTH   Q.A.LI,D.V.MAVRODI,L.S.THOMASHOW,M.ROESSLE,W.BLANKENFELDT    
JRNL        TITL   LIGAND BINDING INDUCES AN AMMONIA CHANNEL IN                 
JRNL        TITL 2 2-AMINO-2-DESOXYISOCHORISMATE (ADIC) SYNTHASE PHZE.          
JRNL        REF    J.BIOL.CHEM.                  V. 286 18213 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21454481                                                     
JRNL        DOI    10.1074/JBC.M110.183418                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0077                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 42357                          
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) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2120                            
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.97                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2881                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.87                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2550                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 157                          
REMARK   3   BIN FREE R VALUE                    : 0.3240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9088                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 80                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 60.36                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 76.07                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.885         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.326         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.237         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.439        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9269 ; 0.017 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  6056 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12629 ; 1.762 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14677 ; 1.305 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1228 ; 7.744 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   393 ;36.482 ;22.672       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1347 ;20.864 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    85 ;20.981 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1454 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10675 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1940 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     6        A   395                          
REMARK   3    RESIDUE RANGE :   B   401        B   427                          
REMARK   3    ORIGIN FOR THE GROUP (A): 110.6252  20.2429 101.1909              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2944 T22:   0.2218                                     
REMARK   3      T33:   0.0731 T12:  -0.0882                                     
REMARK   3      T13:   0.0532 T23:   0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1493 L22:   1.2410                                     
REMARK   3      L33:   1.7614 L12:  -0.3947                                     
REMARK   3      L13:   0.3555 L23:  -0.6524                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0333 S12:   0.1182 S13:   0.1266                       
REMARK   3      S21:  -0.0016 S22:  -0.0270 S23:  -0.2568                       
REMARK   3      S31:  -0.1157 S32:   0.2657 S33:   0.0603                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   440        A   633                          
REMARK   3    ORIGIN FOR THE GROUP (A): 168.0346  46.5934  72.6451              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3394 T22:   0.5988                                     
REMARK   3      T33:   0.1410 T12:   0.0449                                     
REMARK   3      T13:  -0.1666 T23:   0.0699                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5301 L22:   2.3105                                     
REMARK   3      L33:   9.0308 L12:  -0.6246                                     
REMARK   3      L13:   2.5688 L23:  -1.5137                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0455 S12:  -0.0329 S13:   0.2285                       
REMARK   3      S21:  -0.1882 S22:  -0.1065 S23:  -0.1624                       
REMARK   3      S31:   0.2097 S32:   0.6971 S33:   0.0610                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     7        B   395                          
REMARK   3    RESIDUE RANGE :   A   401        A   427                          
REMARK   3    ORIGIN FOR THE GROUP (A): 148.1339  47.4941 103.3023              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4478 T22:   1.5666                                     
REMARK   3      T33:   0.4087 T12:   0.0865                                     
REMARK   3      T13:  -0.1345 T23:   0.1393                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1081 L22:   0.5681                                     
REMARK   3      L33:   2.9210 L12:  -0.5335                                     
REMARK   3      L13:  -0.3159 L23:   0.4442                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2503 S12:  -0.7885 S13:   0.2489                       
REMARK   3      S21:   0.1717 S22:   0.1468 S23:   0.2523                       
REMARK   3      S31:  -0.1949 S32:  -0.8197 S33:   0.1036                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   430        B   635                          
REMARK   3    ORIGIN FOR THE GROUP (A):  85.9496  22.9692  72.7995              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3876 T22:   0.3623                                     
REMARK   3      T33:   0.0558 T12:  -0.1123                                     
REMARK   3      T13:  -0.0047 T23:   0.0905                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2275 L22:   2.3812                                     
REMARK   3      L33:   3.2203 L12:   0.2750                                     
REMARK   3      L13:  -0.1011 L23:   0.3541                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1618 S12:   0.3126 S13:  -0.0071                       
REMARK   3      S21:  -0.2821 S22:   0.1389 S23:   0.2390                       
REMARK   3      S31:  -0.0234 S32:  -0.4372 S33:   0.0230                       
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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 3R74 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000064572.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-NOV-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0, 0.97895, 0.97957, 0.97793     
REMARK 200  MONOCHROMATOR                  : SI(111) MONOCHROMATOR              
REMARK 200  OPTICS                         : SI(111)                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42476                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.924                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.0700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.680                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PROPANE, 0.2 M KSCN,      
REMARK 280  22% (W/V) PEG 3350, 1 MM MG-CHLORIDE, 20 MM CHORISMATE, PH 7.0,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
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      144.29333            
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       72.14667            
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      144.29333            
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       72.14667            
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      144.29333            
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       72.14667            
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      144.29333            
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       72.14667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 49080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 657  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 687  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 664  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     GLY A   429                                                      
REMARK 465     GLY A   430                                                      
REMARK 465     ARG A   431                                                      
REMARK 465     GLN A   432                                                      
REMARK 465     GLY A   433                                                      
REMARK 465     GLU A   434                                                      
REMARK 465     MET A   435                                                      
REMARK 465     ALA A   436                                                      
REMARK 465     ASP A   437                                                      
REMARK 465     GLU A   438                                                      
REMARK 465     LEU A   439                                                      
REMARK 465     ARG A   634                                                      
REMARK 465     GLU A   635                                                      
REMARK 465     LYS A   636                                                      
REMARK 465     ARG A   637                                                      
REMARK 465     MET A   638                                                      
REMARK 465     THR A   639                                                      
REMARK 465     ALA A   640                                                      
REMARK 465     LEU A   641                                                      
REMARK 465     THR A   642                                                      
REMARK 465     ALA A   643                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     ASN B     6                                                      
REMARK 465     GLY B    29                                                      
REMARK 465     SER B    30                                                      
REMARK 465     ALA B    31                                                      
REMARK 465     GLY B    32                                                      
REMARK 465     GLU B    33                                                      
REMARK 465     ARG B    34                                                      
REMARK 465     GLY B   433                                                      
REMARK 465     GLU B   434                                                      
REMARK 465     MET B   435                                                      
REMARK 465     ALA B   436                                                      
REMARK 465     ASP B   437                                                      
REMARK 465     GLU B   438                                                      
REMARK 465     LEU B   439                                                      
REMARK 465     LYS B   636                                                      
REMARK 465     ARG B   637                                                      
REMARK 465     MET B   638                                                      
REMARK 465     THR B   639                                                      
REMARK 465     ALA B   640                                                      
REMARK 465     LEU B   641                                                      
REMARK 465     THR B   642                                                      
REMARK 465     ALA B   643                                                      
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     THR A  28    OG1  CG2                                            
REMARK 470     SER A  30    OG                                                  
REMARK 470     GLU A  33    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  34    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  83    CG   CD   CE   NZ                                   
REMARK 470     SER A 225    OG                                                  
REMARK 470     ARG A 239    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 240    CG   CD   CE   NZ                                   
REMARK 470     GLU A 398    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 403    CG   CD1  CD2                                       
REMARK 470     GLN A 405    CG   CD   OE1  NE2                                  
REMARK 470     HIS A 406    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER A 408    OG                                                  
REMARK 470     VAL A 409    CG1  CG2                                            
REMARK 470     GLN A 410    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 414    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 415    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 418    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 426    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 441    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 446    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 481    CG   OD1  OD2                                       
REMARK 470     GLN A 559    CG   CD   OE1  NE2                                  
REMARK 470     ARG B   7    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B   9    CG   CD1  CD2                                       
REMARK 470     PHE B  10    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP B  11    CG   OD1  OD2                                       
REMARK 470     ARG B  12    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B  13    CG1  CG2                                            
REMARK 470     GLN B  17    CG   CD   OE1  NE2                                  
REMARK 470     MET B  36    CG   SD   CE                                        
REMARK 470     VAL B  44    CG1  CG2                                            
REMARK 470     LYS B  83    CG   CD   CE   NZ                                   
REMARK 470     HIS B  85    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN B 105    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 106    CG   CD1  CD2                                       
REMARK 470     ILE B 111    CG1  CG2  CD1                                       
REMARK 470     ASP B 115    CG   OD1  OD2                                       
REMARK 470     THR B 116    OG1  CG2                                            
REMARK 470     LEU B 118    CG   CD1  CD2                                       
REMARK 470     GLU B 120    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 121    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 125    CG1  CG2  CD1                                       
REMARK 470     GLU B 128    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 130    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B 132    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 135    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 136    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 154    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 159    CG   OD1  OD2                                       
REMARK 470     LEU B 160    CG   CD1  CD2                                       
REMARK 470     ASP B 161    CG   OD1  OD2                                       
REMARK 470     ASP B 162    CG   OD1  OD2                                       
REMARK 470     TYR B 163    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B 173    CG   CD   CE   NZ                                   
REMARK 470     ARG B 174    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 177    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 179    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 192    CG   CD   OE1  OE2                                  
REMARK 470     SER B 225    OG                                                  
REMARK 470     ARG B 239    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 240    CG   CD   CE   NZ                                   
REMARK 470     GLU B 241    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 277    CG   CD1  CD2                                       
REMARK 470     ARG B 319    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS B 320    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG B 322    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 352    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 355    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 358    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 362    CG1  CG2                                            
REMARK 470     SER B 368    OG                                                  
REMARK 470     HIS B 373    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER B 374    OG                                                  
REMARK 470     VAL B 377    CG1  CG2                                            
REMARK 470     GLU B 379    CG   CD   OE1  OE2                                  
REMARK 470     MET B 381    CG   SD   CE                                        
REMARK 470     GLU B 382    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 386    CG   CD   CE   NZ                                   
REMARK 470     SER B 391    OG                                                  
REMARK 470     ASN B 392    CG   OD1  ND2                                       
REMARK 470     PHE B 394    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP B 395    CG   OD1  OD2                                       
REMARK 470     GLU B 398    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 431    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 432    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 441    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 544    CG   CD   OE1  OE2                                  
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    CYS A  20   CB    CYS A  20   SG     -0.118                       
REMARK 500    CYS A 526   CB    CYS A 526   SG      0.184                       
REMARK 500    CYS B 526   CB    CYS B 526   SG      0.127                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  75   CB  -  CA  -  C   ANGL. DEV. = -15.5 DEGREES          
REMARK 500    MET A 300   CG  -  SD  -  CE  ANGL. DEV. = -15.3 DEGREES          
REMARK 500    PRO B 269   C   -  N   -  CD  ANGL. DEV. = -23.3 DEGREES          
REMARK 500    LEU B 469   CA  -  CB  -  CG  ANGL. DEV. =  14.3 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    ASN A   8      -47.59    -23.62                                   
REMARK 500    THR A  28       87.23    -58.32                                   
REMARK 500    SER A  30       39.36    124.42                                   
REMARK 500    GLU A  33       41.66     88.50                                   
REMARK 500    ARG A  34       88.15    175.67                                   
REMARK 500    PRO A  54       81.69    -66.11                                   
REMARK 500    ALA A  56      163.42    -47.43                                   
REMARK 500    LEU A  77      -16.48    -49.67                                   
REMARK 500    GLU A  79      -18.20    -49.49                                   
REMARK 500    GLU A 120       57.80     33.63                                   
REMARK 500    GLU A 141      -69.60   -103.51                                   
REMARK 500    HIS A 203      -69.05    -92.55                                   
REMARK 500    ASN A 214       67.56   -154.62                                   
REMARK 500    ARG A 239       19.74     45.01                                   
REMARK 500    GLU A 241       58.46   -169.09                                   
REMARK 500    SER A 242       19.95    -58.10                                   
REMARK 500    ASP A 243     -117.17    -48.55                                   
REMARK 500    PHE A 301      115.16    117.42                                   
REMARK 500    THR A 306      -77.68   -127.03                                   
REMARK 500    SER A 329       -1.35     78.86                                   
REMARK 500    ASP A 338     -179.41    -67.61                                   
REMARK 500    ALA A 399      -89.81    -70.72                                   
REMARK 500    PRO A 401      104.74    -53.36                                   
REMARK 500    ALA A 402      178.36    151.22                                   
REMARK 500    LEU A 403       33.77    168.23                                   
REMARK 500    SER A 443     -144.96      7.04                                   
REMARK 500    CYS A 445      156.03    169.49                                   
REMARK 500    GLU A 453       41.80     81.75                                   
REMARK 500    HIS A 477       -6.20     81.26                                   
REMARK 500    CYS A 526     -114.43     28.36                                   
REMARK 500    VAL A 583      -10.62   -144.85                                   
REMARK 500    VAL A 618      -82.81    -74.40                                   
REMARK 500    ASP A 619       62.18   -101.77                                   
REMARK 500    LEU B  77      -16.44    -49.67                                   
REMARK 500    ILE B 111      112.86   -166.04                                   
REMARK 500    PRO B 112       46.46    -84.66                                   
REMARK 500    ASP B 115       99.93    -64.52                                   
REMARK 500    ALA B 117     -176.04    -62.91                                   
REMARK 500    ASP B 126      139.61     72.58                                   
REMARK 500    GLU B 141      -70.32   -105.29                                   
REMARK 500    ASP B 162      -40.91     60.30                                   
REMARK 500    TYR B 163     -172.90     71.87                                   
REMARK 500    SER B 164      161.07     97.38                                   
REMARK 500    GLU B 179       44.69    -81.56                                   
REMARK 500    ASN B 214       68.82   -155.45                                   
REMARK 500    PRO B 223     -169.10    -70.17                                   
REMARK 500    ASP B 238       88.71    -38.58                                   
REMARK 500    ARG B 239       31.35    -96.07                                   
REMARK 500    GLU B 241       51.77   -141.60                                   
REMARK 500    ASP B 243     -112.47    -42.64                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      62 RAMACHANDRAN OUTLIERS.                        
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 ASN A    6     ARG A    7                  145.67                    
REMARK 500 MET A  300     PHE A  301                  131.68                    
REMARK 500 THR B  267     GLY B  268                 -147.65                    
REMARK 500 GLY B  268     PRO B  269                 -124.22                    
REMARK 500 MET B  300     PHE B  301                  134.17                    
REMARK 500 TYR B  428     GLY B  429                 -148.38                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3R75   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3R76   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3R77   RELATED DB: PDB                                   
DBREF  3R74 A    1   643  UNP    Q396C7   Q396C7_BURS3     1    643             
DBREF  3R74 B    1   643  UNP    Q396C7   Q396C7_BURS3     1    643             
SEQADV 3R74 GLY A   -1  UNP  Q396C7              EXPRESSION TAG                 
SEQADV 3R74 HIS A    0  UNP  Q396C7              EXPRESSION TAG                 
SEQADV 3R74 GLY B   -1  UNP  Q396C7              EXPRESSION TAG                 
SEQADV 3R74 HIS B    0  UNP  Q396C7              EXPRESSION TAG                 
SEQRES   1 A  645  GLY HIS MET ASN ALA ALA PRO ASN ARG ASN LEU PHE ASP          
SEQRES   2 A  645  ARG VAL LEU HIS GLY GLN ALA PRO CYS PHE ALA LEU ILE          
SEQRES   3 A  645  ALA ARG SER THR GLY SER ALA GLY GLU ARG ALA MET ILE          
SEQRES   4 A  645  ASP VAL PHE ALA GLY ALA VAL SER TYR PRO SER SER LEU          
SEQRES   5 A  645  ALA GLU LEU PRO LEU ALA ALA PRO THR ALA THR GLY ALA          
SEQRES   6 A  645  ASP ARG GLN GLU LEU LEU VAL MET VAL PRO TYR ARG GLN          
SEQRES   7 A  645  LEU HIS GLU ARG GLY PHE LYS THR HIS ASP ASP GLY ALA          
SEQRES   8 A  645  PRO LEU VAL ALA ILE THR CYS ASP GLU HIS GLU THR VAL          
SEQRES   9 A  645  SER ALA GLN LEU ALA LEU ALA ALA ILE PRO ASP ALA ASP          
SEQRES  10 A  645  THR ALA LEU GLY GLU ARG HIS PHE ASP ILE ASP ASP GLU          
SEQRES  11 A  645  ALA TYR ALA GLU ILE VAL GLU ARG VAL ILE THR ASP GLU          
SEQRES  12 A  645  ILE GLY THR GLY ALA GLY SER ASN PHE VAL ILE LYS ARG          
SEQRES  13 A  645  THR LEU GLU GLY ASP LEU ASP ASP TYR SER PRO ALA LYS          
SEQRES  14 A  645  ALA LEU ALA VAL PHE LYS ARG LEU MET ARG ARG GLU VAL          
SEQRES  15 A  645  GLY ALA TYR TRP ILE PHE VAL ILE HIS THR GLY GLU ARG          
SEQRES  16 A  645  THR PHE VAL GLY ALA THR PRO GLU ARG HIS LEU THR LEU          
SEQRES  17 A  645  HIS GLU GLY CYS ALA THR MET ASN PRO ILE SER GLY THR          
SEQRES  18 A  645  TYR ARG TYR PRO GLN SER GLY PRO THR ILE ASP GLY ILE          
SEQRES  19 A  645  ASN ALA PHE LEU GLY ASP ARG LYS GLU SER ASP GLU LEU          
SEQRES  20 A  645  TYR MET VAL LEU ASP GLU GLU LEU LYS MET MET ALA ARG          
SEQRES  21 A  645  ILE CYS PRO ALA GLY GLY GLN VAL THR GLY PRO HIS LEU          
SEQRES  22 A  645  ARG GLU MET ALA ARG LEU ALA HIS THR GLU TYR PHE ILE          
SEQRES  23 A  645  VAL GLY HIS THR GLU ALA ASP VAL ARG ASP LEU LEU ARG          
SEQRES  24 A  645  GLU THR MET PHE ALA PRO THR VAL THR GLY SER PRO ILE          
SEQRES  25 A  645  GLU SER ALA THR ARG VAL ILE ALA ARG HIS GLU ARG ALA          
SEQRES  26 A  645  GLY ARG GLY TYR TYR SER GLY ILE ALA ALA LEU ILE GLY          
SEQRES  27 A  645  ARG ASP ALA ARG GLY GLY ARG THR LEU ASP SER ALA ILE          
SEQRES  28 A  645  LEU ILE ARG THR ALA GLU ILE ASP ARG ALA GLY HIS VAL          
SEQRES  29 A  645  ARG ILE GLY VAL GLY SER THR LEU VAL ARG HIS SER ASP          
SEQRES  30 A  645  ALA VAL SER GLU VAL MET GLU THR HIS ALA LYS VAL ALA          
SEQRES  31 A  645  ALA LEU SER ASN ALA PHE ASP PRO PRO GLU ALA GLY PRO          
SEQRES  32 A  645  ALA LEU GLY GLN HIS PRO SER VAL GLN ALA ALA LEU ARG          
SEQRES  33 A  645  GLU ARG ASN GLU GLY ILE ALA ASP PHE TRP PHE ARG PRO          
SEQRES  34 A  645  TYR GLY GLY ARG GLN GLY GLU MET ALA ASP GLU LEU ALA          
SEQRES  35 A  645  GLU LEU SER GLY CYS ARG ALA LEU ILE VAL ASP ALA GLU          
SEQRES  36 A  645  ASP HIS PHE THR ALA MET ILE ALA GLN GLN LEU SER SER          
SEQRES  37 A  645  LEU GLY LEU ALA THR GLU VAL CYS GLY VAL HIS ASP ALA          
SEQRES  38 A  645  VAL ASP LEU ALA ARG TYR ASP VAL VAL VAL MET GLY PRO          
SEQRES  39 A  645  GLY PRO GLY ASP PRO SER ASP ALA GLY ASP PRO ARG ILE          
SEQRES  40 A  645  ALA ARG LEU TYR ALA TRP LEU ARG HIS LEU ILE ASP GLU          
SEQRES  41 A  645  GLY LYS PRO PHE MET ALA VAL CYS LEU SER HIS GLN ILE          
SEQRES  42 A  645  LEU ASN ALA ILE LEU GLY ILE PRO LEU VAL ARG ARG GLU          
SEQRES  43 A  645  VAL PRO ASN GLN GLY ILE GLN VAL GLU ILE ASP LEU PHE          
SEQRES  44 A  645  GLY GLN ARG GLU ARG VAL GLY PHE TYR ASN THR TYR VAL          
SEQRES  45 A  645  ALA GLN THR VAL ARG ASP GLU MET ASP VAL ASP GLY VAL          
SEQRES  46 A  645  GLY THR VAL ALA ILE SER ARG ASP PRO ARG THR GLY GLU          
SEQRES  47 A  645  VAL HIS ALA LEU ARG GLY PRO THR PHE SER SER MET GLN          
SEQRES  48 A  645  PHE HIS ALA GLU SER VAL LEU THR VAL ASP GLY PRO ARG          
SEQRES  49 A  645  ILE LEU GLY GLU ALA ILE THR HIS ALA ILE ARG ARG GLU          
SEQRES  50 A  645  LYS ARG MET THR ALA LEU THR ALA                              
SEQRES   1 B  645  GLY HIS MET ASN ALA ALA PRO ASN ARG ASN LEU PHE ASP          
SEQRES   2 B  645  ARG VAL LEU HIS GLY GLN ALA PRO CYS PHE ALA LEU ILE          
SEQRES   3 B  645  ALA ARG SER THR GLY SER ALA GLY GLU ARG ALA MET ILE          
SEQRES   4 B  645  ASP VAL PHE ALA GLY ALA VAL SER TYR PRO SER SER LEU          
SEQRES   5 B  645  ALA GLU LEU PRO LEU ALA ALA PRO THR ALA THR GLY ALA          
SEQRES   6 B  645  ASP ARG GLN GLU LEU LEU VAL MET VAL PRO TYR ARG GLN          
SEQRES   7 B  645  LEU HIS GLU ARG GLY PHE LYS THR HIS ASP ASP GLY ALA          
SEQRES   8 B  645  PRO LEU VAL ALA ILE THR CYS ASP GLU HIS GLU THR VAL          
SEQRES   9 B  645  SER ALA GLN LEU ALA LEU ALA ALA ILE PRO ASP ALA ASP          
SEQRES  10 B  645  THR ALA LEU GLY GLU ARG HIS PHE ASP ILE ASP ASP GLU          
SEQRES  11 B  645  ALA TYR ALA GLU ILE VAL GLU ARG VAL ILE THR ASP GLU          
SEQRES  12 B  645  ILE GLY THR GLY ALA GLY SER ASN PHE VAL ILE LYS ARG          
SEQRES  13 B  645  THR LEU GLU GLY ASP LEU ASP ASP TYR SER PRO ALA LYS          
SEQRES  14 B  645  ALA LEU ALA VAL PHE LYS ARG LEU MET ARG ARG GLU VAL          
SEQRES  15 B  645  GLY ALA TYR TRP ILE PHE VAL ILE HIS THR GLY GLU ARG          
SEQRES  16 B  645  THR PHE VAL GLY ALA THR PRO GLU ARG HIS LEU THR LEU          
SEQRES  17 B  645  HIS GLU GLY CYS ALA THR MET ASN PRO ILE SER GLY THR          
SEQRES  18 B  645  TYR ARG TYR PRO GLN SER GLY PRO THR ILE ASP GLY ILE          
SEQRES  19 B  645  ASN ALA PHE LEU GLY ASP ARG LYS GLU SER ASP GLU LEU          
SEQRES  20 B  645  TYR MET VAL LEU ASP GLU GLU LEU LYS MET MET ALA ARG          
SEQRES  21 B  645  ILE CYS PRO ALA GLY GLY GLN VAL THR GLY PRO HIS LEU          
SEQRES  22 B  645  ARG GLU MET ALA ARG LEU ALA HIS THR GLU TYR PHE ILE          
SEQRES  23 B  645  VAL GLY HIS THR GLU ALA ASP VAL ARG ASP LEU LEU ARG          
SEQRES  24 B  645  GLU THR MET PHE ALA PRO THR VAL THR GLY SER PRO ILE          
SEQRES  25 B  645  GLU SER ALA THR ARG VAL ILE ALA ARG HIS GLU ARG ALA          
SEQRES  26 B  645  GLY ARG GLY TYR TYR SER GLY ILE ALA ALA LEU ILE GLY          
SEQRES  27 B  645  ARG ASP ALA ARG GLY GLY ARG THR LEU ASP SER ALA ILE          
SEQRES  28 B  645  LEU ILE ARG THR ALA GLU ILE ASP ARG ALA GLY HIS VAL          
SEQRES  29 B  645  ARG ILE GLY VAL GLY SER THR LEU VAL ARG HIS SER ASP          
SEQRES  30 B  645  ALA VAL SER GLU VAL MET GLU THR HIS ALA LYS VAL ALA          
SEQRES  31 B  645  ALA LEU SER ASN ALA PHE ASP PRO PRO GLU ALA GLY PRO          
SEQRES  32 B  645  ALA LEU GLY GLN HIS PRO SER VAL GLN ALA ALA LEU ARG          
SEQRES  33 B  645  GLU ARG ASN GLU GLY ILE ALA ASP PHE TRP PHE ARG PRO          
SEQRES  34 B  645  TYR GLY GLY ARG GLN GLY GLU MET ALA ASP GLU LEU ALA          
SEQRES  35 B  645  GLU LEU SER GLY CYS ARG ALA LEU ILE VAL ASP ALA GLU          
SEQRES  36 B  645  ASP HIS PHE THR ALA MET ILE ALA GLN GLN LEU SER SER          
SEQRES  37 B  645  LEU GLY LEU ALA THR GLU VAL CYS GLY VAL HIS ASP ALA          
SEQRES  38 B  645  VAL ASP LEU ALA ARG TYR ASP VAL VAL VAL MET GLY PRO          
SEQRES  39 B  645  GLY PRO GLY ASP PRO SER ASP ALA GLY ASP PRO ARG ILE          
SEQRES  40 B  645  ALA ARG LEU TYR ALA TRP LEU ARG HIS LEU ILE ASP GLU          
SEQRES  41 B  645  GLY LYS PRO PHE MET ALA VAL CYS LEU SER HIS GLN ILE          
SEQRES  42 B  645  LEU ASN ALA ILE LEU GLY ILE PRO LEU VAL ARG ARG GLU          
SEQRES  43 B  645  VAL PRO ASN GLN GLY ILE GLN VAL GLU ILE ASP LEU PHE          
SEQRES  44 B  645  GLY GLN ARG GLU ARG VAL GLY PHE TYR ASN THR TYR VAL          
SEQRES  45 B  645  ALA GLN THR VAL ARG ASP GLU MET ASP VAL ASP GLY VAL          
SEQRES  46 B  645  GLY THR VAL ALA ILE SER ARG ASP PRO ARG THR GLY GLU          
SEQRES  47 B  645  VAL HIS ALA LEU ARG GLY PRO THR PHE SER SER MET GLN          
SEQRES  48 B  645  PHE HIS ALA GLU SER VAL LEU THR VAL ASP GLY PRO ARG          
SEQRES  49 B  645  ILE LEU GLY GLU ALA ILE THR HIS ALA ILE ARG ARG GLU          
SEQRES  50 B  645  LYS ARG MET THR ALA LEU THR ALA                              
FORMUL   3  HOH   *80(H2 O)                                                     
HELIX    1   1 ARG A    7  HIS A   15  1                                   9    
HELIX    2   2 SER A   49  LEU A   53  5                                   5    
HELIX    3   3 PRO A   73  GLY A   81  5                                   9    
HELIX    4   4 ALA A  104  ILE A  111  1                                   8    
HELIX    5   5 ASP A  126  GLU A  141  1                                  16    
HELIX    6   6 ILE A  142  GLY A  145  5                                   4    
HELIX    7   7 SER A  164  GLU A  179  1                                  16    
HELIX    8   8 THR A  228  ARG A  239  1                                  12    
HELIX    9   9 SER A  242  CYS A  260  1                                  19    
HELIX   10  10 ASP A  291  THR A  299  1                                   9    
HELIX   11  11 ALA A  302  VAL A  305  5                                   4    
HELIX   12  12 PRO A  309  GLU A  321  1                                  13    
HELIX   13  13 ASP A  375  VAL A  387  1                                  13    
HELIX   14  14 VAL A  387  ASP A  395  1                                   9    
HELIX   15  15 HIS A  406  ARG A  416  1                                  11    
HELIX   16  16 ASN A  417  GLY A  419  5                                   3    
HELIX   17  17 ASP A  422  ARG A  426  5                                   5    
HELIX   18  18 HIS A  455  LEU A  467  1                                  13    
HELIX   19  19 ASP A  481  TYR A  485  5                                   5    
HELIX   20  20 ASP A  502  GLY A  519  1                                  18    
HELIX   21  21 CYS A  526  GLY A  537  1                                  12    
HELIX   22  22 ASP A  619  ILE A  632  1                                  14    
HELIX   23  23 LEU B    9  LEU B   14  1                                   6    
HELIX   24  24 SER B   49  LEU B   53  5                                   5    
HELIX   25  25 PRO B   73  GLY B   81  5                                   9    
HELIX   26  26 ALA B  104  ALA B  110  1                                   7    
HELIX   27  27 ASP B  126  GLU B  141  1                                  16    
HELIX   28  28 ILE B  142  GLY B  145  5                                   4    
HELIX   29  29 SER B  164  GLU B  179  1                                  16    
HELIX   30  30 THR B  228  ASP B  238  1                                  11    
HELIX   31  31 SER B  242  CYS B  260  1                                  19    
HELIX   32  32 ASP B  291  THR B  299  1                                   9    
HELIX   33  33 ALA B  302  VAL B  305  5                                   4    
HELIX   34  34 PRO B  309  ARG B  319  1                                  11    
HELIX   35  35 ASP B  375  VAL B  387  1                                  13    
HELIX   36  36 VAL B  387  ASN B  392  1                                   6    
HELIX   37  37 ALA B  402  GLN B  405  5                                   4    
HELIX   38  38 HIS B  406  ARG B  416  1                                  11    
HELIX   39  39 ASP B  422  ARG B  426  5                                   5    
HELIX   40  40 HIS B  455  LEU B  467  1                                  13    
HELIX   41  41 ASP B  481  TYR B  485  5                                   5    
HELIX   42  42 ASP B  502  GLY B  519  1                                  18    
HELIX   43  43 CYS B  526  GLY B  537  1                                  12    
HELIX   44  44 ASP B  619  ARG B  633  1                                  15    
SHEET    1   A 9 GLU A  98  SER A 103  0                                        
SHEET    2   A 9 MET A  36  ALA A  41 -1  N  VAL A  39   O  GLU A 100           
SHEET    3   A 9 PHE A  21  ARG A  26 -1  N  ILE A  24   O  ASP A  38           
SHEET    4   A 9 TRP A 184  HIS A 189 -1  O  HIS A 189   N  PHE A  21           
SHEET    5   A 9 ARG A 193  THR A 199 -1  O  PHE A 195   N  ILE A 188           
SHEET    6   A 9 THR A 353  ASP A 357 -1  O  ALA A 354   N  VAL A 196           
SHEET    7   A 9 HIS A 361  LEU A 370 -1  O  ARG A 363   N  GLU A 355           
SHEET    8   A 9 ASN A 149  LEU A 160 -1  N  LEU A 156   O  ILE A 364           
SHEET    9   A 9 LEU A 118  PHE A 123 -1  N  GLY A 119   O  ASP A 159           
SHEET    1   B 9 GLU A  98  SER A 103  0                                        
SHEET    2   B 9 MET A  36  ALA A  41 -1  N  VAL A  39   O  GLU A 100           
SHEET    3   B 9 PHE A  21  ARG A  26 -1  N  ILE A  24   O  ASP A  38           
SHEET    4   B 9 TRP A 184  HIS A 189 -1  O  HIS A 189   N  PHE A  21           
SHEET    5   B 9 ARG A 193  THR A 199 -1  O  PHE A 195   N  ILE A 188           
SHEET    6   B 9 THR A 353  ASP A 357 -1  O  ALA A 354   N  VAL A 196           
SHEET    7   B 9 HIS A 361  LEU A 370 -1  O  ARG A 363   N  GLU A 355           
SHEET    8   B 9 ASN A 149  LEU A 160 -1  N  LEU A 156   O  ILE A 364           
SHEET    9   B 9 GLY A 307  SER A 308 -1  O  SER A 308   N  ASN A 149           
SHEET    1   C 9 VAL A  44  SER A  45  0                                        
SHEET    2   C 9 VAL A  92  THR A  95 -1  O  ALA A  93   N  SER A  45           
SHEET    3   C 9 ARG A  65  VAL A  72 -1  N  LEU A  69   O  ILE A  94           
SHEET    4   C 9 ILE A 331  ARG A 337 -1  O  ILE A 331   N  VAL A  72           
SHEET    5   C 9 ARG A 343  ILE A 349 -1  O  ASP A 346   N  LEU A 334           
SHEET    6   C 9 ARG A 202  HIS A 207 -1  N  HIS A 203   O  SER A 347           
SHEET    7   C 9 CYS A 210  MET A 213 -1  O  THR A 212   N  THR A 205           
SHEET    8   C 9 LEU A 277  HIS A 287 -1  O  GLY A 286   N  ALA A 211           
SHEET    9   C 9 ILE A 216  ARG A 221 -1  N  TYR A 220   O  ALA A 278           
SHEET    1   D 9 VAL A  44  SER A  45  0                                        
SHEET    2   D 9 VAL A  92  THR A  95 -1  O  ALA A  93   N  SER A  45           
SHEET    3   D 9 ARG A  65  VAL A  72 -1  N  LEU A  69   O  ILE A  94           
SHEET    4   D 9 ILE A 331  ARG A 337 -1  O  ILE A 331   N  VAL A  72           
SHEET    5   D 9 ARG A 343  ILE A 349 -1  O  ASP A 346   N  LEU A 334           
SHEET    6   D 9 ARG A 202  HIS A 207 -1  N  HIS A 203   O  SER A 347           
SHEET    7   D 9 CYS A 210  MET A 213 -1  O  THR A 212   N  THR A 205           
SHEET    8   D 9 LEU A 277  HIS A 287 -1  O  GLY A 286   N  ALA A 211           
SHEET    9   D 9 GLN A 265  GLU A 273 -1  N  HIS A 270   O  GLU A 281           
SHEET    1   E 8 LEU A 469  GLY A 475  0                                        
SHEET    2   E 8 CYS A 445  ASP A 451  1  N  CYS A 445   O  ALA A 470           
SHEET    3   E 8 VAL A 487  MET A 490  1  O  VAL A 489   N  LEU A 448           
SHEET    4   E 8 PHE A 522  VAL A 525  1  O  MET A 523   N  MET A 490           
SHEET    5   E 8 PHE A 605  MET A 608  1  O  MET A 608   N  ALA A 524           
SHEET    6   E 8 VAL A 597  ARG A 601 -1  N  LEU A 600   O  SER A 607           
SHEET    7   E 8 GLY A 584  ARG A 590 -1  N  SER A 589   O  HIS A 598           
SHEET    8   E 8 GLU A 577  VAL A 580 -1  N  VAL A 580   O  GLY A 584           
SHEET    1   F 2 LEU A 540  ARG A 542  0                                        
SHEET    2   F 2 TYR A 569  ALA A 571 -1  O  VAL A 570   N  VAL A 541           
SHEET    1   G 2 ILE A 550  LEU A 556  0                                        
SHEET    2   G 2 GLN A 559  PHE A 565 -1  O  PHE A 565   N  ILE A 550           
SHEET    1   H 9 GLU B  98  SER B 103  0                                        
SHEET    2   H 9 MET B  36  ALA B  41 -1  N  VAL B  39   O  GLU B 100           
SHEET    3   H 9 PHE B  21  ARG B  26 -1  N  ILE B  24   O  ASP B  38           
SHEET    4   H 9 TRP B 184  HIS B 189 -1  O  HIS B 189   N  PHE B  21           
SHEET    5   H 9 THR B 194  THR B 199 -1  O  PHE B 195   N  ILE B 188           
SHEET    6   H 9 THR B 353  ILE B 356 -1  O  ALA B 354   N  VAL B 196           
SHEET    7   H 9 HIS B 361  LEU B 370 -1  O  ARG B 363   N  GLU B 355           
SHEET    8   H 9 ASN B 149  ASP B 159 -1  N  LEU B 156   O  ILE B 364           
SHEET    9   H 9 GLY B 119  PHE B 123 -1  N  HIS B 122   O  GLU B 157           
SHEET    1   I 9 GLU B  98  SER B 103  0                                        
SHEET    2   I 9 MET B  36  ALA B  41 -1  N  VAL B  39   O  GLU B 100           
SHEET    3   I 9 PHE B  21  ARG B  26 -1  N  ILE B  24   O  ASP B  38           
SHEET    4   I 9 TRP B 184  HIS B 189 -1  O  HIS B 189   N  PHE B  21           
SHEET    5   I 9 THR B 194  THR B 199 -1  O  PHE B 195   N  ILE B 188           
SHEET    6   I 9 THR B 353  ILE B 356 -1  O  ALA B 354   N  VAL B 196           
SHEET    7   I 9 HIS B 361  LEU B 370 -1  O  ARG B 363   N  GLU B 355           
SHEET    8   I 9 ASN B 149  ASP B 159 -1  N  LEU B 156   O  ILE B 364           
SHEET    9   I 9 GLY B 307  SER B 308 -1  O  SER B 308   N  ASN B 149           
SHEET    1   J 9 VAL B  44  SER B  45  0                                        
SHEET    2   J 9 VAL B  92  THR B  95 -1  O  ALA B  93   N  SER B  45           
SHEET    3   J 9 ARG B  65  VAL B  72 -1  N  LEU B  69   O  ILE B  94           
SHEET    4   J 9 ILE B 331  ARG B 337 -1  O  ILE B 331   N  VAL B  72           
SHEET    5   J 9 ARG B 343  ILE B 349 -1  O  ASP B 346   N  LEU B 334           
SHEET    6   J 9 ARG B 202  HIS B 207 -1  N  LEU B 206   O  LEU B 345           
SHEET    7   J 9 CYS B 210  MET B 213 -1  O  CYS B 210   N  HIS B 207           
SHEET    8   J 9 LEU B 277  HIS B 287 -1  O  GLY B 286   N  ALA B 211           
SHEET    9   J 9 ILE B 216  ARG B 221 -1  N  TYR B 220   O  ALA B 278           
SHEET    1   K 9 VAL B  44  SER B  45  0                                        
SHEET    2   K 9 VAL B  92  THR B  95 -1  O  ALA B  93   N  SER B  45           
SHEET    3   K 9 ARG B  65  VAL B  72 -1  N  LEU B  69   O  ILE B  94           
SHEET    4   K 9 ILE B 331  ARG B 337 -1  O  ILE B 331   N  VAL B  72           
SHEET    5   K 9 ARG B 343  ILE B 349 -1  O  ASP B 346   N  LEU B 334           
SHEET    6   K 9 ARG B 202  HIS B 207 -1  N  LEU B 206   O  LEU B 345           
SHEET    7   K 9 CYS B 210  MET B 213 -1  O  CYS B 210   N  HIS B 207           
SHEET    8   K 9 LEU B 277  HIS B 287 -1  O  GLY B 286   N  ALA B 211           
SHEET    9   K 9 GLN B 265  GLU B 273 -1  N  ARG B 272   O  HIS B 279           
SHEET    1   L 8 ALA B 470  GLY B 475  0                                        
SHEET    2   L 8 ARG B 446  ASP B 451  1  N  ALA B 447   O  ALA B 470           
SHEET    3   L 8 VAL B 487  MET B 490  1  O  VAL B 489   N  LEU B 448           
SHEET    4   L 8 PHE B 522  VAL B 525  1  O  MET B 523   N  MET B 490           
SHEET    5   L 8 PHE B 605  MET B 608  1  O  MET B 608   N  ALA B 524           
SHEET    6   L 8 VAL B 597  ARG B 601 -1  N  LEU B 600   O  SER B 607           
SHEET    7   L 8 GLY B 584  ARG B 590 -1  N  ALA B 587   O  ARG B 601           
SHEET    8   L 8 GLU B 577  VAL B 580 -1  N  VAL B 580   O  GLY B 584           
SHEET    1   M 2 LEU B 540  ARG B 542  0                                        
SHEET    2   M 2 TYR B 569  ALA B 571 -1  O  VAL B 570   N  VAL B 541           
SHEET    1   N 2 ILE B 550  LEU B 556  0                                        
SHEET    2   N 2 GLN B 559  PHE B 565 -1  O  PHE B 565   N  ILE B 550           
CISPEP   1 GLN A  224    SER A  225          0         6.11                     
CISPEP   2 GLY A  268    PRO A  269          0         3.60                     
CISPEP   3 SER A  308    PRO A  309          0         2.83                     
CISPEP   4 SER B  308    PRO B  309          0         0.24                     
CRYST1  172.360  172.360  216.440  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      0.005802  0.003350  0.000000        0.00000                         
SCALE2      0.000000  0.006699  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004620        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system