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Database: PDB
Entry: 3IDE
LinkDB: 3IDE
Original site: 3IDE 
HEADER    VIRUS LIKE PARTICLE                     21-JUL-09   3IDE              
TITLE     STRUCTURE OF IPNV SUBVIRAL PARTICLE                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAPSID PROTEIN VP2;                                        
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 SYNONYM: PP;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: INFECTIOUS PANCREATIC NECROSIS VIRUS -;         
SOURCE   3 ORGANISM_COMMON: IPNV;                                               
SOURCE   4 ORGANISM_TAXID: 11005;                                               
SOURCE   5 STRAIN: SP;                                                          
SOURCE   6 GENE: VP2;                                                           
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_VECTOR: PFASTBAC1                                  
KEYWDS    JELLY ROLL, BETA SANDWICH, ICOSAHEDRAL PARTICLE, VIRION, VIRUS LIKE   
KEYWDS   2 PARTICLE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.COULIBALY,C.CHEVALIER,B.DELMAS,F.A.REY                              
REVDAT   6   01-NOV-17 3IDE    1       REMARK                                   
REVDAT   5   13-JUL-11 3IDE    1       VERSN                                    
REVDAT   4   09-FEB-10 3IDE    1       MTRIX1 MTRIX2 MTRIX3                     
REVDAT   3   02-FEB-10 3IDE    1       JRNL                                     
REVDAT   2   26-JAN-10 3IDE    1       MTRIX1 MTRIX2 MTRIX3                     
REVDAT   1   29-DEC-09 3IDE    0                                                
JRNL        AUTH   F.COULIBALY,C.CHEVALIER,B.DELMAS,F.A.REY                     
JRNL        TITL   CRYSTAL STRUCTURE OF AN AQUABIRNAVIRUS PARTICLE: INSIGHTS    
JRNL        TITL 2 INTO ANTIGENIC DIVERSITY AND VIRULENCE DETERMINISM           
JRNL        REF    J.VIROL.                      V.  84  1792 2010              
JRNL        REFN                   ISSN 0022-538X                               
JRNL        PMID   20007275                                                     
JRNL        DOI    10.1128/JVI.01536-09                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.75                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 65456                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1992                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.7550 -  8.0260    1.00     4707   166  0.1770 0.1790        
REMARK   3     2  8.0260 -  6.3910    1.00     4633   166  0.1690 0.1960        
REMARK   3     3  6.3910 -  5.5890    0.99     4622    83  0.1790 0.2010        
REMARK   3     4  5.5890 -  5.0810    0.99     4572   166  0.1750 0.2020        
REMARK   3     5  5.0810 -  4.7180    0.98     4439   166  0.1680 0.1590        
REMARK   3     6  4.7180 -  4.4410    0.98     4537    83  0.1800 0.2070        
REMARK   3     7  4.4410 -  4.2190    0.98     4442   166  0.2090 0.2190        
REMARK   3     8  4.2190 -  4.0360    0.98     4447   166  0.2350 0.2580        
REMARK   3     9  4.0360 -  3.8810    0.98     4562    83  0.2740 0.3000        
REMARK   3    10  3.8810 -  3.7470    0.99     4493   166  0.2820 0.3120        
REMARK   3    11  3.7470 -  3.6300    0.99     4497   166  0.2840 0.3160        
REMARK   3    12  3.6300 -  3.5270    0.99     4527   166  0.3090 0.2720        
REMARK   3    13  3.5270 -  3.4340    0.98     4540    83  0.3100 0.3720        
REMARK   3    14  3.4340 -  3.3500    0.98     4446   166  0.3340 0.3080        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.27                                          
REMARK   3   B_SOL              : 43.88                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 85.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 99.95                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005          16356                                  
REMARK   3   ANGLE     :  0.918          22267                                  
REMARK   3   CHIRALITY :  0.065           2599                                  
REMARK   3   PLANARITY :  0.003           2897                                  
REMARK   3   DIHEDRAL  : 18.010           6011                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  66.8874 135.3274 127.5307              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6869 T22:   0.5377                                     
REMARK   3      T33:   0.6104 T12:  -0.1461                                     
REMARK   3      T13:   0.0610 T23:  -0.0694                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3118 L22:   2.1103                                     
REMARK   3      L33:   0.9636 L12:   0.0144                                     
REMARK   3      L13:  -0.4907 L23:   0.6123                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2414 S12:   0.1584 S13:  -0.0790                       
REMARK   3      S21:   0.6444 S22:   0.0661 S23:   0.1214                       
REMARK   3      S31:   0.4726 S32:  -0.3203 S33:   0.1728                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  65.9286 137.0218 173.3840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6663 T22:   0.5540                                     
REMARK   3      T33:   0.6837 T12:  -0.1963                                     
REMARK   3      T13:  -0.0266 T23:   0.0289                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4821 L22:   1.8119                                     
REMARK   3      L33:   1.4784 L12:   0.4549                                     
REMARK   3      L13:   0.6654 L23:  -0.1525                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0348 S12:  -0.2208 S13:  -0.1524                       
REMARK   3      S21:  -0.4370 S22:   0.1141 S23:   0.2819                       
REMARK   3      S31:   0.4655 S32:  -0.3935 S33:  -0.1451                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  88.7542 100.6508 189.2645              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6739 T22:   0.6117                                     
REMARK   3      T33:   0.5753 T12:  -0.1018                                     
REMARK   3      T13:   0.0209 T23:   0.1330                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3772 L22:   0.7363                                     
REMARK   3      L33:   0.1988 L12:  -0.0147                                     
REMARK   3      L13:   0.5454 L23:  -0.1278                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0350 S12:   0.1474 S13:   0.0231                       
REMARK   3      S21:  -0.3063 S22:  -0.0284 S23:   0.1405                       
REMARK   3      S31:   0.1555 S32:   0.0570 S33:   0.0489                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN D                                                
REMARK   3    ORIGIN FOR THE GROUP (A): 103.6172  75.9217 153.1406              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5734 T22:   0.7254                                     
REMARK   3      T33:   0.7673 T12:  -0.0687                                     
REMARK   3      T13:   0.0073 T23:   0.0684                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0237 L22:   0.0364                                     
REMARK   3      L33:   1.7925 L12:  -0.5098                                     
REMARK   3      L13:  -0.1972 L23:  -0.1886                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0017 S12:   0.1073 S13:  -0.4298                       
REMARK   3      S21:   0.0061 S22:   0.0782 S23:   0.2259                       
REMARK   3      S31:  -0.1868 S32:  -0.5722 S33:  -0.0852                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN E                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  90.3896  97.7562 115.1380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5384 T22:   0.5468                                     
REMARK   3      T33:   0.4828 T12:  -0.0614                                     
REMARK   3      T13:  -0.0155 T23:  -0.0567                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6045 L22:   0.7601                                     
REMARK   3      L33:   0.5274 L12:   0.1384                                     
REMARK   3      L13:  -0.0412 L23:  -0.2390                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0157 S12:  -0.2083 S13:  -0.0054                       
REMARK   3      S21:   0.2214 S22:   0.0638 S23:   0.1306                       
REMARK   3      S31:  -0.0970 S32:  -0.0609 S33:  -0.0422                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 6:109 OR RESSEQ         
REMARK   3                          118:428 )                                   
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 6:109 OR RESSEQ         
REMARK   3                          118:428 )                                   
REMARK   3     ATOM PAIRS NUMBER  : 3208                                        
REMARK   3     RMSD               : 0.014                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 6:109 OR RESSEQ         
REMARK   3                          118:428 )                                   
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 6:109 OR RESSEQ         
REMARK   3                          118:428 )                                   
REMARK   3     ATOM PAIRS NUMBER  : 3208                                        
REMARK   3     RMSD               : 0.016                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 6:109 OR RESSEQ         
REMARK   3                          118:428 )                                   
REMARK   3     SELECTION          : CHAIN D AND (RESSEQ 6:109 OR RESSEQ         
REMARK   3                          118:428 )                                   
REMARK   3     ATOM PAIRS NUMBER  : 3208                                        
REMARK   3     RMSD               : 0.013                                       
REMARK   3    NCS OPERATOR : 4                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 6:109 OR RESSEQ         
REMARK   3                          118:428 )                                   
REMARK   3     SELECTION          : CHAIN E AND (RESSEQ 6:109 OR RESSEQ         
REMARK   3                          118:428 )                                   
REMARK   3     ATOM PAIRS NUMBER  : 3208                                        
REMARK   3     RMSD               : 0.021                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3IDE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JUL-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000054271.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9500                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66153                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.47                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: SOLVE, RESOLVE                                        
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M 1,6-HEXANEDIOL, 10MM COCL2, 100MM     
REMARK 280  SODIUM ACETATE PH 4.6, VAPOR DIFFUSION, TEMPERATURE 293K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      14555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      15555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      16555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2                                       
REMARK 290      18555   Z+1/2,-X+1/2,-Y+1/2                                     
REMARK 290      19555   -Z+1/2,-X+1/2,Y+1/2                                     
REMARK 290      20555   -Z+1/2,X+1/2,-Y+1/2                                     
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2                                       
REMARK 290      22555   -Y+1/2,Z+1/2,-X+1/2                                     
REMARK 290      23555   Y+1/2,-Z+1/2,-X+1/2                                     
REMARK 290      24555   -Y+1/2,-Z+1/2,X+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
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  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000      151.71550            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000      151.71550            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      151.71550            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000      151.71550            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000      151.71550            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      151.71550            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000      151.71550            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000      151.71550            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000      151.71550            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000      151.71550            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000      151.71550            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      151.71550            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000      151.71550            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000      151.71550            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000      151.71550            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000      151.71550            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000      151.71550            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000      151.71550            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000      151.71550            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000      151.71550            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000      151.71550            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000      151.71550            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000      151.71550            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000      151.71550            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000      151.71550            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000      151.71550            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000      151.71550            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000      151.71550            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000      151.71550            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000      151.71550            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000      151.71550            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000      151.71550            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000      151.71550            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000      151.71550            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000      151.71550            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000      151.71550            
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 300 REMARK: THE ENTRY CONTAINS THE ASYMMETRIC UNIT OF THE T=1            
REMARK 300 ICOSAHEDRAL PARTICLE.                                                
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: 60-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      303.43100            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      303.43100            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000      303.43100            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000      303.43100            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      303.43100            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      303.43100            
REMARK 350   BIOMT1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2   6 -1.000000  0.000000  0.000000      303.43100            
REMARK 350   BIOMT3   6  0.000000 -1.000000  0.000000      303.43100            
REMARK 350   BIOMT1   7  0.000000  0.000000 -1.000000      303.43100            
REMARK 350   BIOMT2   7 -1.000000  0.000000  0.000000      303.43100            
REMARK 350   BIOMT3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1   8  0.000000  0.000000 -1.000000      303.43100            
REMARK 350   BIOMT2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   8  0.000000 -1.000000  0.000000      303.43100            
REMARK 350   BIOMT1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  10  0.000000 -1.000000  0.000000      303.43100            
REMARK 350   BIOMT2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3  10 -1.000000  0.000000  0.000000      303.43100            
REMARK 350   BIOMT1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  11  0.000000  0.000000 -1.000000      303.43100            
REMARK 350   BIOMT3  11 -1.000000  0.000000  0.000000      303.43100            
REMARK 350   BIOMT1  12  0.000000 -1.000000  0.000000      303.43100            
REMARK 350   BIOMT2  12  0.000000  0.000000 -1.000000      303.43100            
REMARK 350   BIOMT3  12  1.000000  0.000000  0.000000        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 CO    CO C 443  LIES ON A SPECIAL POSITION.                          
REMARK 375 CL    CL C 444  LIES ON A SPECIAL POSITION.                          
REMARK 375 CO    CO E 443  LIES ON A SPECIAL POSITION.                          
REMARK 375 CL    CL E 444  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     LEU A   110                                                      
REMARK 465     PRO A   111                                                      
REMARK 465     ALA A   112                                                      
REMARK 465     GLY A   113                                                      
REMARK 465     LEU A   114                                                      
REMARK 465     TYR A   115                                                      
REMARK 465     ALA A   116                                                      
REMARK 465     LEU A   117                                                      
REMARK 465     GLU A   429                                                      
REMARK 465     ILE A   430                                                      
REMARK 465     THR A   431                                                      
REMARK 465     ASP A   432                                                      
REMARK 465     PHE A   433                                                      
REMARK 465     SER A   434                                                      
REMARK 465     SER A   435                                                      
REMARK 465     ASP A   436                                                      
REMARK 465     LEU A   437                                                      
REMARK 465     PRO A   438                                                      
REMARK 465     THR A   439                                                      
REMARK 465     SER A   440                                                      
REMARK 465     LYS A   441                                                      
REMARK 465     ALA A   442                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     ASN B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     PRO B   111                                                      
REMARK 465     ALA B   112                                                      
REMARK 465     GLY B   113                                                      
REMARK 465     LEU B   114                                                      
REMARK 465     TYR B   115                                                      
REMARK 465     ALA B   116                                                      
REMARK 465     LEU B   117                                                      
REMARK 465     GLU B   429                                                      
REMARK 465     ILE B   430                                                      
REMARK 465     THR B   431                                                      
REMARK 465     ASP B   432                                                      
REMARK 465     PHE B   433                                                      
REMARK 465     SER B   434                                                      
REMARK 465     SER B   435                                                      
REMARK 465     ASP B   436                                                      
REMARK 465     LEU B   437                                                      
REMARK 465     PRO B   438                                                      
REMARK 465     THR B   439                                                      
REMARK 465     SER B   440                                                      
REMARK 465     LYS B   441                                                      
REMARK 465     ALA B   442                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ASN C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     ASN C     4                                                      
REMARK 465     LYS C     5                                                      
REMARK 465     LEU C   110                                                      
REMARK 465     PRO C   111                                                      
REMARK 465     ALA C   112                                                      
REMARK 465     GLY C   113                                                      
REMARK 465     LEU C   114                                                      
REMARK 465     TYR C   115                                                      
REMARK 465     ALA C   116                                                      
REMARK 465     LEU C   117                                                      
REMARK 465     GLU C   429                                                      
REMARK 465     ILE C   430                                                      
REMARK 465     THR C   431                                                      
REMARK 465     ASP C   432                                                      
REMARK 465     PHE C   433                                                      
REMARK 465     SER C   434                                                      
REMARK 465     SER C   435                                                      
REMARK 465     ASP C   436                                                      
REMARK 465     LEU C   437                                                      
REMARK 465     PRO C   438                                                      
REMARK 465     THR C   439                                                      
REMARK 465     SER C   440                                                      
REMARK 465     LYS C   441                                                      
REMARK 465     ALA C   442                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ASN D     2                                                      
REMARK 465     THR D     3                                                      
REMARK 465     ASN D     4                                                      
REMARK 465     LYS D     5                                                      
REMARK 465     PRO D   111                                                      
REMARK 465     ALA D   112                                                      
REMARK 465     GLY D   113                                                      
REMARK 465     LEU D   114                                                      
REMARK 465     TYR D   115                                                      
REMARK 465     ALA D   116                                                      
REMARK 465     LEU D   117                                                      
REMARK 465     GLU D   429                                                      
REMARK 465     ILE D   430                                                      
REMARK 465     THR D   431                                                      
REMARK 465     ASP D   432                                                      
REMARK 465     PHE D   433                                                      
REMARK 465     SER D   434                                                      
REMARK 465     SER D   435                                                      
REMARK 465     ASP D   436                                                      
REMARK 465     LEU D   437                                                      
REMARK 465     PRO D   438                                                      
REMARK 465     THR D   439                                                      
REMARK 465     SER D   440                                                      
REMARK 465     LYS D   441                                                      
REMARK 465     ALA D   442                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ASN E     2                                                      
REMARK 465     THR E     3                                                      
REMARK 465     ASN E     4                                                      
REMARK 465     LYS E     5                                                      
REMARK 465     LEU E   110                                                      
REMARK 465     PRO E   111                                                      
REMARK 465     ALA E   112                                                      
REMARK 465     GLY E   113                                                      
REMARK 465     LEU E   114                                                      
REMARK 465     TYR E   115                                                      
REMARK 465     ALA E   116                                                      
REMARK 465     LEU E   117                                                      
REMARK 465     GLU E   429                                                      
REMARK 465     ILE E   430                                                      
REMARK 465     THR E   431                                                      
REMARK 465     ASP E   432                                                      
REMARK 465     PHE E   433                                                      
REMARK 465     SER E   434                                                      
REMARK 465     SER E   435                                                      
REMARK 465     ASP E   436                                                      
REMARK 465     LEU E   437                                                      
REMARK 465     PRO E   438                                                      
REMARK 465     THR E   439                                                      
REMARK 465     SER E   440                                                      
REMARK 465     LYS E   441                                                      
REMARK 465     ALA E   442                                                      
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    ALA A   8        3.39    -65.20                                   
REMARK 500    PRO A  25       41.96    -78.80                                   
REMARK 500    ASP A  26     -158.61   -109.51                                   
REMARK 500    ILE A  28       59.72    -97.70                                   
REMARK 500    PHE A  56       67.27   -116.63                                   
REMARK 500    ASP A  80      -66.29    -98.73                                   
REMARK 500    GLU A 127       42.01    -93.65                                   
REMARK 500    THR A 168       63.07   -101.04                                   
REMARK 500    MET A 188      153.67    -47.77                                   
REMARK 500    ALA A 198      -39.91   -130.62                                   
REMARK 500    ALA A 200       70.73     41.03                                   
REMARK 500    ASN A 267       11.05     53.63                                   
REMARK 500    ASP A 268        5.96     52.56                                   
REMARK 500    THR A 293        8.75   -150.69                                   
REMARK 500    ILE A 314     -159.72   -112.24                                   
REMARK 500    THR A 318       23.24    -75.03                                   
REMARK 500    ASN A 340       -2.94     63.03                                   
REMARK 500    HIS A 405       37.10    -91.23                                   
REMARK 500    LEU A 409     -172.58    -64.29                                   
REMARK 500    ARG A 423        6.68    -68.13                                   
REMARK 500    ARG A 425        4.70    -65.97                                   
REMARK 500    ALA B   8        3.28    -65.07                                   
REMARK 500    PRO B  25       42.20    -78.83                                   
REMARK 500    ASP B  26     -159.38   -110.39                                   
REMARK 500    PHE B  56       67.38   -116.16                                   
REMARK 500    ASP B  80      -66.18    -99.02                                   
REMARK 500    GLU B 127       41.85    -93.77                                   
REMARK 500    THR B 168       63.10   -100.42                                   
REMARK 500    MET B 188      153.96    -47.98                                   
REMARK 500    ALA B 198      -39.38   -130.48                                   
REMARK 500    ALA B 200       71.30     41.53                                   
REMARK 500    ASN B 267       10.87     53.83                                   
REMARK 500    ASP B 268        6.06     52.78                                   
REMARK 500    THR B 293        9.17   -150.10                                   
REMARK 500    ILE B 314     -159.29   -112.66                                   
REMARK 500    THR B 318       23.61    -75.23                                   
REMARK 500    ASN B 340       -3.70     63.48                                   
REMARK 500    HIS B 405       38.40    -92.05                                   
REMARK 500    LEU B 409     -172.41    -63.63                                   
REMARK 500    ARG B 423        6.68    -68.12                                   
REMARK 500    ARG B 425        4.69    -66.19                                   
REMARK 500    ALA C   8        3.72    -65.39                                   
REMARK 500    PRO C  25       42.77    -79.29                                   
REMARK 500    ASP C  26     -158.96   -111.00                                   
REMARK 500    PHE C  56       66.84   -116.76                                   
REMARK 500    ASP C  80      -66.43    -98.57                                   
REMARK 500    GLU C 127       41.40    -93.54                                   
REMARK 500    THR C 168       62.73   -100.49                                   
REMARK 500    MET C 188      153.50    -48.53                                   
REMARK 500    ALA C 198      -38.11   -131.06                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     101 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO A 443  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  27   OD2                                                    
REMARK 620 2 ASP B  27   OD2  74.1                                              
REMARK 620 3 ASP D  27   OD2 129.0  73.4                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 443                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 444                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO C 443                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 444                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO E 443                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 444                  
DBREF  3IDE A    1   442  UNP    Q703G9   POLS_IPNVS       1    442             
DBREF  3IDE B    1   442  UNP    Q703G9   POLS_IPNVS       1    442             
DBREF  3IDE C    1   442  UNP    Q703G9   POLS_IPNVS       1    442             
DBREF  3IDE D    1   442  UNP    Q703G9   POLS_IPNVS       1    442             
DBREF  3IDE E    1   442  UNP    Q703G9   POLS_IPNVS       1    442             
SEQRES   1 A  442  MET ASN THR ASN LYS ALA THR ALA THR TYR LEU LYS SER          
SEQRES   2 A  442  ILE MET LEU PRO GLU THR GLY PRO ALA SER ILE PRO ASP          
SEQRES   3 A  442  ASP ILE THR GLU ARG HIS ILE LEU LYS GLN GLU THR SER          
SEQRES   4 A  442  SER TYR ASN LEU GLU VAL SER GLU SER GLY SER GLY VAL          
SEQRES   5 A  442  LEU VAL CYS PHE PRO GLY ALA PRO GLY SER ARG ILE GLY          
SEQRES   6 A  442  ALA HIS TYR ARG TRP ASN ALA ASN GLN THR GLY LEU GLU          
SEQRES   7 A  442  PHE ASP GLN TRP LEU GLU THR SER GLN ASP LEU LYS LYS          
SEQRES   8 A  442  ALA PHE ASN TYR GLY ARG LEU ILE SER ARG LYS TYR ASP          
SEQRES   9 A  442  ILE GLN SER SER THR LEU PRO ALA GLY LEU TYR ALA LEU          
SEQRES  10 A  442  ASN GLY THR LEU ASN ALA ALA THR PHE GLU GLY SER LEU          
SEQRES  11 A  442  SER GLU VAL GLU SER LEU THR TYR ASN SER LEU MET SER          
SEQRES  12 A  442  LEU THR THR ASN PRO GLN ASP LYS VAL ASN ASN GLN LEU          
SEQRES  13 A  442  VAL THR LYS GLY VAL THR VAL LEU ASN LEU PRO THR GLY          
SEQRES  14 A  442  PHE ASP LYS PRO TYR VAL ARG LEU GLU ASP GLU THR PRO          
SEQRES  15 A  442  GLN GLY LEU GLN SER MET ASN GLY ALA LYS MET ARG CYS          
SEQRES  16 A  442  THR ALA ALA ILE ALA PRO ARG ARG TYR GLU ILE ASP LEU          
SEQRES  17 A  442  PRO SER GLN ARG LEU PRO PRO VAL PRO ALA THR GLY THR          
SEQRES  18 A  442  LEU THR THR LEU TYR GLU GLY ASN ALA ASP ILE VAL ASN          
SEQRES  19 A  442  SER THR THR VAL THR GLY ASP ILE ASN PHE SER LEU ALA          
SEQRES  20 A  442  GLU GLN PRO ALA ASP GLU THR LYS PHE ASP PHE GLN LEU          
SEQRES  21 A  442  ASP PHE MET GLY LEU ASP ASN ASP VAL PRO VAL VAL THR          
SEQRES  22 A  442  VAL VAL SER SER VAL LEU ALA THR ASN ASP ASN TYR ARG          
SEQRES  23 A  442  GLY VAL SER ALA LYS MET THR GLN SER ILE PRO THR GLU          
SEQRES  24 A  442  ASN ILE THR LYS PRO ILE THR ARG VAL LYS LEU SER TYR          
SEQRES  25 A  442  LYS ILE ASN GLN GLN THR ALA ILE GLY ASN VAL ALA THR          
SEQRES  26 A  442  LEU GLY THR MET GLY PRO ALA SER VAL SER PHE SER SER          
SEQRES  27 A  442  GLY ASN GLY ASN VAL PRO GLY VAL LEU ARG PRO ILE THR          
SEQRES  28 A  442  LEU VAL ALA TYR GLU LYS MET THR PRO LEU SER ILE LEU          
SEQRES  29 A  442  THR VAL ALA GLY VAL SER ASN TYR GLU LEU ILE PRO ASN          
SEQRES  30 A  442  PRO GLU LEU LEU LYS ASN MET VAL THR ARG TYR GLY LYS          
SEQRES  31 A  442  TYR ASP PRO GLU GLY LEU ASN TYR ALA LYS MET ILE LEU          
SEQRES  32 A  442  SER HIS ARG GLU GLU LEU ASP ILE ARG THR VAL TRP ARG          
SEQRES  33 A  442  THR GLU GLU TYR LYS GLU ARG THR ARG VAL PHE ASN GLU          
SEQRES  34 A  442  ILE THR ASP PHE SER SER ASP LEU PRO THR SER LYS ALA          
SEQRES   1 B  442  MET ASN THR ASN LYS ALA THR ALA THR TYR LEU LYS SER          
SEQRES   2 B  442  ILE MET LEU PRO GLU THR GLY PRO ALA SER ILE PRO ASP          
SEQRES   3 B  442  ASP ILE THR GLU ARG HIS ILE LEU LYS GLN GLU THR SER          
SEQRES   4 B  442  SER TYR ASN LEU GLU VAL SER GLU SER GLY SER GLY VAL          
SEQRES   5 B  442  LEU VAL CYS PHE PRO GLY ALA PRO GLY SER ARG ILE GLY          
SEQRES   6 B  442  ALA HIS TYR ARG TRP ASN ALA ASN GLN THR GLY LEU GLU          
SEQRES   7 B  442  PHE ASP GLN TRP LEU GLU THR SER GLN ASP LEU LYS LYS          
SEQRES   8 B  442  ALA PHE ASN TYR GLY ARG LEU ILE SER ARG LYS TYR ASP          
SEQRES   9 B  442  ILE GLN SER SER THR LEU PRO ALA GLY LEU TYR ALA LEU          
SEQRES  10 B  442  ASN GLY THR LEU ASN ALA ALA THR PHE GLU GLY SER LEU          
SEQRES  11 B  442  SER GLU VAL GLU SER LEU THR TYR ASN SER LEU MET SER          
SEQRES  12 B  442  LEU THR THR ASN PRO GLN ASP LYS VAL ASN ASN GLN LEU          
SEQRES  13 B  442  VAL THR LYS GLY VAL THR VAL LEU ASN LEU PRO THR GLY          
SEQRES  14 B  442  PHE ASP LYS PRO TYR VAL ARG LEU GLU ASP GLU THR PRO          
SEQRES  15 B  442  GLN GLY LEU GLN SER MET ASN GLY ALA LYS MET ARG CYS          
SEQRES  16 B  442  THR ALA ALA ILE ALA PRO ARG ARG TYR GLU ILE ASP LEU          
SEQRES  17 B  442  PRO SER GLN ARG LEU PRO PRO VAL PRO ALA THR GLY THR          
SEQRES  18 B  442  LEU THR THR LEU TYR GLU GLY ASN ALA ASP ILE VAL ASN          
SEQRES  19 B  442  SER THR THR VAL THR GLY ASP ILE ASN PHE SER LEU ALA          
SEQRES  20 B  442  GLU GLN PRO ALA ASP GLU THR LYS PHE ASP PHE GLN LEU          
SEQRES  21 B  442  ASP PHE MET GLY LEU ASP ASN ASP VAL PRO VAL VAL THR          
SEQRES  22 B  442  VAL VAL SER SER VAL LEU ALA THR ASN ASP ASN TYR ARG          
SEQRES  23 B  442  GLY VAL SER ALA LYS MET THR GLN SER ILE PRO THR GLU          
SEQRES  24 B  442  ASN ILE THR LYS PRO ILE THR ARG VAL LYS LEU SER TYR          
SEQRES  25 B  442  LYS ILE ASN GLN GLN THR ALA ILE GLY ASN VAL ALA THR          
SEQRES  26 B  442  LEU GLY THR MET GLY PRO ALA SER VAL SER PHE SER SER          
SEQRES  27 B  442  GLY ASN GLY ASN VAL PRO GLY VAL LEU ARG PRO ILE THR          
SEQRES  28 B  442  LEU VAL ALA TYR GLU LYS MET THR PRO LEU SER ILE LEU          
SEQRES  29 B  442  THR VAL ALA GLY VAL SER ASN TYR GLU LEU ILE PRO ASN          
SEQRES  30 B  442  PRO GLU LEU LEU LYS ASN MET VAL THR ARG TYR GLY LYS          
SEQRES  31 B  442  TYR ASP PRO GLU GLY LEU ASN TYR ALA LYS MET ILE LEU          
SEQRES  32 B  442  SER HIS ARG GLU GLU LEU ASP ILE ARG THR VAL TRP ARG          
SEQRES  33 B  442  THR GLU GLU TYR LYS GLU ARG THR ARG VAL PHE ASN GLU          
SEQRES  34 B  442  ILE THR ASP PHE SER SER ASP LEU PRO THR SER LYS ALA          
SEQRES   1 C  442  MET ASN THR ASN LYS ALA THR ALA THR TYR LEU LYS SER          
SEQRES   2 C  442  ILE MET LEU PRO GLU THR GLY PRO ALA SER ILE PRO ASP          
SEQRES   3 C  442  ASP ILE THR GLU ARG HIS ILE LEU LYS GLN GLU THR SER          
SEQRES   4 C  442  SER TYR ASN LEU GLU VAL SER GLU SER GLY SER GLY VAL          
SEQRES   5 C  442  LEU VAL CYS PHE PRO GLY ALA PRO GLY SER ARG ILE GLY          
SEQRES   6 C  442  ALA HIS TYR ARG TRP ASN ALA ASN GLN THR GLY LEU GLU          
SEQRES   7 C  442  PHE ASP GLN TRP LEU GLU THR SER GLN ASP LEU LYS LYS          
SEQRES   8 C  442  ALA PHE ASN TYR GLY ARG LEU ILE SER ARG LYS TYR ASP          
SEQRES   9 C  442  ILE GLN SER SER THR LEU PRO ALA GLY LEU TYR ALA LEU          
SEQRES  10 C  442  ASN GLY THR LEU ASN ALA ALA THR PHE GLU GLY SER LEU          
SEQRES  11 C  442  SER GLU VAL GLU SER LEU THR TYR ASN SER LEU MET SER          
SEQRES  12 C  442  LEU THR THR ASN PRO GLN ASP LYS VAL ASN ASN GLN LEU          
SEQRES  13 C  442  VAL THR LYS GLY VAL THR VAL LEU ASN LEU PRO THR GLY          
SEQRES  14 C  442  PHE ASP LYS PRO TYR VAL ARG LEU GLU ASP GLU THR PRO          
SEQRES  15 C  442  GLN GLY LEU GLN SER MET ASN GLY ALA LYS MET ARG CYS          
SEQRES  16 C  442  THR ALA ALA ILE ALA PRO ARG ARG TYR GLU ILE ASP LEU          
SEQRES  17 C  442  PRO SER GLN ARG LEU PRO PRO VAL PRO ALA THR GLY THR          
SEQRES  18 C  442  LEU THR THR LEU TYR GLU GLY ASN ALA ASP ILE VAL ASN          
SEQRES  19 C  442  SER THR THR VAL THR GLY ASP ILE ASN PHE SER LEU ALA          
SEQRES  20 C  442  GLU GLN PRO ALA ASP GLU THR LYS PHE ASP PHE GLN LEU          
SEQRES  21 C  442  ASP PHE MET GLY LEU ASP ASN ASP VAL PRO VAL VAL THR          
SEQRES  22 C  442  VAL VAL SER SER VAL LEU ALA THR ASN ASP ASN TYR ARG          
SEQRES  23 C  442  GLY VAL SER ALA LYS MET THR GLN SER ILE PRO THR GLU          
SEQRES  24 C  442  ASN ILE THR LYS PRO ILE THR ARG VAL LYS LEU SER TYR          
SEQRES  25 C  442  LYS ILE ASN GLN GLN THR ALA ILE GLY ASN VAL ALA THR          
SEQRES  26 C  442  LEU GLY THR MET GLY PRO ALA SER VAL SER PHE SER SER          
SEQRES  27 C  442  GLY ASN GLY ASN VAL PRO GLY VAL LEU ARG PRO ILE THR          
SEQRES  28 C  442  LEU VAL ALA TYR GLU LYS MET THR PRO LEU SER ILE LEU          
SEQRES  29 C  442  THR VAL ALA GLY VAL SER ASN TYR GLU LEU ILE PRO ASN          
SEQRES  30 C  442  PRO GLU LEU LEU LYS ASN MET VAL THR ARG TYR GLY LYS          
SEQRES  31 C  442  TYR ASP PRO GLU GLY LEU ASN TYR ALA LYS MET ILE LEU          
SEQRES  32 C  442  SER HIS ARG GLU GLU LEU ASP ILE ARG THR VAL TRP ARG          
SEQRES  33 C  442  THR GLU GLU TYR LYS GLU ARG THR ARG VAL PHE ASN GLU          
SEQRES  34 C  442  ILE THR ASP PHE SER SER ASP LEU PRO THR SER LYS ALA          
SEQRES   1 D  442  MET ASN THR ASN LYS ALA THR ALA THR TYR LEU LYS SER          
SEQRES   2 D  442  ILE MET LEU PRO GLU THR GLY PRO ALA SER ILE PRO ASP          
SEQRES   3 D  442  ASP ILE THR GLU ARG HIS ILE LEU LYS GLN GLU THR SER          
SEQRES   4 D  442  SER TYR ASN LEU GLU VAL SER GLU SER GLY SER GLY VAL          
SEQRES   5 D  442  LEU VAL CYS PHE PRO GLY ALA PRO GLY SER ARG ILE GLY          
SEQRES   6 D  442  ALA HIS TYR ARG TRP ASN ALA ASN GLN THR GLY LEU GLU          
SEQRES   7 D  442  PHE ASP GLN TRP LEU GLU THR SER GLN ASP LEU LYS LYS          
SEQRES   8 D  442  ALA PHE ASN TYR GLY ARG LEU ILE SER ARG LYS TYR ASP          
SEQRES   9 D  442  ILE GLN SER SER THR LEU PRO ALA GLY LEU TYR ALA LEU          
SEQRES  10 D  442  ASN GLY THR LEU ASN ALA ALA THR PHE GLU GLY SER LEU          
SEQRES  11 D  442  SER GLU VAL GLU SER LEU THR TYR ASN SER LEU MET SER          
SEQRES  12 D  442  LEU THR THR ASN PRO GLN ASP LYS VAL ASN ASN GLN LEU          
SEQRES  13 D  442  VAL THR LYS GLY VAL THR VAL LEU ASN LEU PRO THR GLY          
SEQRES  14 D  442  PHE ASP LYS PRO TYR VAL ARG LEU GLU ASP GLU THR PRO          
SEQRES  15 D  442  GLN GLY LEU GLN SER MET ASN GLY ALA LYS MET ARG CYS          
SEQRES  16 D  442  THR ALA ALA ILE ALA PRO ARG ARG TYR GLU ILE ASP LEU          
SEQRES  17 D  442  PRO SER GLN ARG LEU PRO PRO VAL PRO ALA THR GLY THR          
SEQRES  18 D  442  LEU THR THR LEU TYR GLU GLY ASN ALA ASP ILE VAL ASN          
SEQRES  19 D  442  SER THR THR VAL THR GLY ASP ILE ASN PHE SER LEU ALA          
SEQRES  20 D  442  GLU GLN PRO ALA ASP GLU THR LYS PHE ASP PHE GLN LEU          
SEQRES  21 D  442  ASP PHE MET GLY LEU ASP ASN ASP VAL PRO VAL VAL THR          
SEQRES  22 D  442  VAL VAL SER SER VAL LEU ALA THR ASN ASP ASN TYR ARG          
SEQRES  23 D  442  GLY VAL SER ALA LYS MET THR GLN SER ILE PRO THR GLU          
SEQRES  24 D  442  ASN ILE THR LYS PRO ILE THR ARG VAL LYS LEU SER TYR          
SEQRES  25 D  442  LYS ILE ASN GLN GLN THR ALA ILE GLY ASN VAL ALA THR          
SEQRES  26 D  442  LEU GLY THR MET GLY PRO ALA SER VAL SER PHE SER SER          
SEQRES  27 D  442  GLY ASN GLY ASN VAL PRO GLY VAL LEU ARG PRO ILE THR          
SEQRES  28 D  442  LEU VAL ALA TYR GLU LYS MET THR PRO LEU SER ILE LEU          
SEQRES  29 D  442  THR VAL ALA GLY VAL SER ASN TYR GLU LEU ILE PRO ASN          
SEQRES  30 D  442  PRO GLU LEU LEU LYS ASN MET VAL THR ARG TYR GLY LYS          
SEQRES  31 D  442  TYR ASP PRO GLU GLY LEU ASN TYR ALA LYS MET ILE LEU          
SEQRES  32 D  442  SER HIS ARG GLU GLU LEU ASP ILE ARG THR VAL TRP ARG          
SEQRES  33 D  442  THR GLU GLU TYR LYS GLU ARG THR ARG VAL PHE ASN GLU          
SEQRES  34 D  442  ILE THR ASP PHE SER SER ASP LEU PRO THR SER LYS ALA          
SEQRES   1 E  442  MET ASN THR ASN LYS ALA THR ALA THR TYR LEU LYS SER          
SEQRES   2 E  442  ILE MET LEU PRO GLU THR GLY PRO ALA SER ILE PRO ASP          
SEQRES   3 E  442  ASP ILE THR GLU ARG HIS ILE LEU LYS GLN GLU THR SER          
SEQRES   4 E  442  SER TYR ASN LEU GLU VAL SER GLU SER GLY SER GLY VAL          
SEQRES   5 E  442  LEU VAL CYS PHE PRO GLY ALA PRO GLY SER ARG ILE GLY          
SEQRES   6 E  442  ALA HIS TYR ARG TRP ASN ALA ASN GLN THR GLY LEU GLU          
SEQRES   7 E  442  PHE ASP GLN TRP LEU GLU THR SER GLN ASP LEU LYS LYS          
SEQRES   8 E  442  ALA PHE ASN TYR GLY ARG LEU ILE SER ARG LYS TYR ASP          
SEQRES   9 E  442  ILE GLN SER SER THR LEU PRO ALA GLY LEU TYR ALA LEU          
SEQRES  10 E  442  ASN GLY THR LEU ASN ALA ALA THR PHE GLU GLY SER LEU          
SEQRES  11 E  442  SER GLU VAL GLU SER LEU THR TYR ASN SER LEU MET SER          
SEQRES  12 E  442  LEU THR THR ASN PRO GLN ASP LYS VAL ASN ASN GLN LEU          
SEQRES  13 E  442  VAL THR LYS GLY VAL THR VAL LEU ASN LEU PRO THR GLY          
SEQRES  14 E  442  PHE ASP LYS PRO TYR VAL ARG LEU GLU ASP GLU THR PRO          
SEQRES  15 E  442  GLN GLY LEU GLN SER MET ASN GLY ALA LYS MET ARG CYS          
SEQRES  16 E  442  THR ALA ALA ILE ALA PRO ARG ARG TYR GLU ILE ASP LEU          
SEQRES  17 E  442  PRO SER GLN ARG LEU PRO PRO VAL PRO ALA THR GLY THR          
SEQRES  18 E  442  LEU THR THR LEU TYR GLU GLY ASN ALA ASP ILE VAL ASN          
SEQRES  19 E  442  SER THR THR VAL THR GLY ASP ILE ASN PHE SER LEU ALA          
SEQRES  20 E  442  GLU GLN PRO ALA ASP GLU THR LYS PHE ASP PHE GLN LEU          
SEQRES  21 E  442  ASP PHE MET GLY LEU ASP ASN ASP VAL PRO VAL VAL THR          
SEQRES  22 E  442  VAL VAL SER SER VAL LEU ALA THR ASN ASP ASN TYR ARG          
SEQRES  23 E  442  GLY VAL SER ALA LYS MET THR GLN SER ILE PRO THR GLU          
SEQRES  24 E  442  ASN ILE THR LYS PRO ILE THR ARG VAL LYS LEU SER TYR          
SEQRES  25 E  442  LYS ILE ASN GLN GLN THR ALA ILE GLY ASN VAL ALA THR          
SEQRES  26 E  442  LEU GLY THR MET GLY PRO ALA SER VAL SER PHE SER SER          
SEQRES  27 E  442  GLY ASN GLY ASN VAL PRO GLY VAL LEU ARG PRO ILE THR          
SEQRES  28 E  442  LEU VAL ALA TYR GLU LYS MET THR PRO LEU SER ILE LEU          
SEQRES  29 E  442  THR VAL ALA GLY VAL SER ASN TYR GLU LEU ILE PRO ASN          
SEQRES  30 E  442  PRO GLU LEU LEU LYS ASN MET VAL THR ARG TYR GLY LYS          
SEQRES  31 E  442  TYR ASP PRO GLU GLY LEU ASN TYR ALA LYS MET ILE LEU          
SEQRES  32 E  442  SER HIS ARG GLU GLU LEU ASP ILE ARG THR VAL TRP ARG          
SEQRES  33 E  442  THR GLU GLU TYR LYS GLU ARG THR ARG VAL PHE ASN GLU          
SEQRES  34 E  442  ILE THR ASP PHE SER SER ASP LEU PRO THR SER LYS ALA          
HET     CO  A 443       1                                                       
HET     CL  A 444       1                                                       
HET     CO  C 443       1                                                       
HET     CL  C 444       1                                                       
HET     CO  E 443       1                                                       
HET     CL  E 444       1                                                       
HETNAM      CO COBALT (II) ION                                                  
HETNAM      CL CHLORIDE ION                                                     
FORMUL   6   CO    3(CO 2+)                                                     
FORMUL   7   CL    3(CL 1-)                                                     
FORMUL  12  HOH   *10(H2 O)                                                     
HELIX    1   1 ALA A    8  LEU A   16  1                                   9    
HELIX    2   2 PRO A   17  GLY A   20  5                                   4    
HELIX    3   3 ASP A   88  LYS A   91  5                                   4    
HELIX    4   4 SER A  129  VAL A  133  5                                   5    
HELIX    5   5 ASN A  139  LEU A  144  5                                   6    
HELIX    6   6 ASN A  147  GLN A  149  5                                   3    
HELIX    7   7 PRO A  297  ILE A  301  5                                   5    
HELIX    8   8 GLN A  316  ILE A  320  5                                   5    
HELIX    9   9 LEU A  326  GLY A  330  5                                   5    
HELIX   10  10 ASN A  377  LYS A  382  1                                   6    
HELIX   11  11 GLU A  394  HIS A  405  1                                  12    
HELIX   12  12 THR A  417  ARG A  423  1                                   7    
HELIX   13  13 THR A  424  ASN A  428  5                                   5    
HELIX   14  14 ALA B    8  LEU B   16  1                                   9    
HELIX   15  15 PRO B   17  GLY B   20  5                                   4    
HELIX   16  16 ASP B   88  LYS B   91  5                                   4    
HELIX   17  17 SER B  129  VAL B  133  5                                   5    
HELIX   18  18 ASN B  139  LEU B  144  5                                   6    
HELIX   19  19 ASN B  147  GLN B  149  5                                   3    
HELIX   20  20 PRO B  297  ILE B  301  5                                   5    
HELIX   21  21 GLN B  316  ILE B  320  5                                   5    
HELIX   22  22 LEU B  326  GLY B  330  5                                   5    
HELIX   23  23 ASN B  377  LYS B  382  1                                   6    
HELIX   24  24 GLU B  394  HIS B  405  1                                  12    
HELIX   25  25 THR B  417  ARG B  423  1                                   7    
HELIX   26  26 THR B  424  ASN B  428  5                                   5    
HELIX   27  27 ALA C    8  LEU C   16  1                                   9    
HELIX   28  28 PRO C   17  GLY C   20  5                                   4    
HELIX   29  29 ASP C   88  LYS C   91  5                                   4    
HELIX   30  30 SER C  129  VAL C  133  5                                   5    
HELIX   31  31 ASN C  139  LEU C  144  5                                   6    
HELIX   32  32 ASN C  147  GLN C  149  5                                   3    
HELIX   33  33 PRO C  297  ILE C  301  5                                   5    
HELIX   34  34 GLN C  316  ILE C  320  5                                   5    
HELIX   35  35 LEU C  326  GLY C  330  5                                   5    
HELIX   36  36 ASN C  377  LYS C  382  1                                   6    
HELIX   37  37 GLU C  394  HIS C  405  1                                  12    
HELIX   38  38 THR C  417  ARG C  423  1                                   7    
HELIX   39  39 THR C  424  ASN C  428  5                                   5    
HELIX   40  40 ALA D    8  LEU D   16  1                                   9    
HELIX   41  41 PRO D   17  GLY D   20  5                                   4    
HELIX   42  42 ASP D   88  LYS D   91  5                                   4    
HELIX   43  43 SER D  129  VAL D  133  5                                   5    
HELIX   44  44 ASN D  139  LEU D  144  5                                   6    
HELIX   45  45 ASN D  147  GLN D  149  5                                   3    
HELIX   46  46 PRO D  297  ILE D  301  5                                   5    
HELIX   47  47 GLN D  316  ILE D  320  5                                   5    
HELIX   48  48 LEU D  326  GLY D  330  5                                   5    
HELIX   49  49 ASN D  377  LYS D  382  1                                   6    
HELIX   50  50 GLU D  394  HIS D  405  1                                  12    
HELIX   51  51 THR D  417  ARG D  423  1                                   7    
HELIX   52  52 THR D  424  ASN D  428  5                                   5    
HELIX   53  53 ALA E    8  LEU E   16  1                                   9    
HELIX   54  54 PRO E   17  GLY E   20  5                                   4    
HELIX   55  55 ASP E   88  LYS E   91  5                                   4    
HELIX   56  56 SER E  129  VAL E  133  5                                   5    
HELIX   57  57 ASN E  139  LEU E  144  5                                   6    
HELIX   58  58 ASN E  147  GLN E  149  5                                   3    
HELIX   59  59 PRO E  297  ILE E  301  5                                   5    
HELIX   60  60 GLN E  316  ILE E  320  5                                   5    
HELIX   61  61 LEU E  326  GLY E  330  5                                   5    
HELIX   62  62 ASN E  377  LYS E  382  1                                   6    
HELIX   63  63 GLU E  394  HIS E  405  1                                  12    
HELIX   64  64 THR E  417  ARG E  423  1                                   7    
HELIX   65  65 THR E  424  ASN E  428  5                                   5    
SHEET    1   A 4 ILE A  33  GLU A  44  0                                        
SHEET    2   A 4 ILE A 363  PRO A 376 -1  O  GLY A 368   N  SER A  39           
SHEET    3   A 4 PHE A  93  SER A 107 -1  N  ILE A  99   O  ASN A 371           
SHEET    4   A 4 VAL A 175  ARG A 176 -1  O  VAL A 175   N  GLY A  96           
SHEET    1   B 5 ILE A  33  GLU A  44  0                                        
SHEET    2   B 5 ILE A 363  PRO A 376 -1  O  GLY A 368   N  SER A  39           
SHEET    3   B 5 PHE A  93  SER A 107 -1  N  ILE A  99   O  ASN A 371           
SHEET    4   B 5 VAL A 161  LEU A 164 -1  O  VAL A 163   N  TYR A 103           
SHEET    5   B 5 VAL A 414  ARG A 416 -1  O  TRP A 415   N  THR A 162           
SHEET    1   C 6 LEU A  77  GLU A  84  0                                        
SHEET    2   C 6 ARG A  63  TRP A  70 -1  N  ARG A  69   O  GLU A  78           
SHEET    3   C 6 GLY A  51  CYS A  55 -1  N  VAL A  54   O  ALA A  66           
SHEET    4   C 6 ILE A 350  GLU A 356 -1  O  VAL A 353   N  LEU A  53           
SHEET    5   C 6 THR A 120  PHE A 126 -1  N  ASN A 122   O  ALA A 354           
SHEET    6   C 6 LYS A 151  LEU A 156 -1  O  VAL A 152   N  ALA A 123           
SHEET    1   D 2 ASP A 179  GLU A 180  0                                        
SHEET    2   D 2 ARG A 194  CYS A 195 -1  O  CYS A 195   N  ASP A 179           
SHEET    1   E 4 ARG A 202  LEU A 208  0                                        
SHEET    2   E 4 ALA A 332  SER A 338 -1  O  VAL A 334   N  ILE A 206           
SHEET    3   E 4 THR A 236  LEU A 246 -1  N  THR A 239   O  SER A 335           
SHEET    4   E 4 SER A 295  ILE A 296 -1  O  ILE A 296   N  THR A 236           
SHEET    1   F 3 VAL A 288  MET A 292  0                                        
SHEET    2   F 3 THR A 236  LEU A 246 -1  N  PHE A 244   O  VAL A 288           
SHEET    3   F 3 ALA A 324  THR A 325 -1  O  THR A 325   N  SER A 245           
SHEET    1   G 4 THR A 223  ILE A 232  0                                        
SHEET    2   G 4 ILE A 305  LYS A 313 -1  O  LEU A 310   N  LEU A 225           
SHEET    3   G 4 THR A 254  MET A 263 -1  N  ASP A 261   O  LYS A 309           
SHEET    4   G 4 VAL A 272  ALA A 280 -1  O  VAL A 274   N  LEU A 260           
SHEET    1   H 4 ILE B  33  GLU B  44  0                                        
SHEET    2   H 4 ILE B 363  PRO B 376 -1  O  GLY B 368   N  SER B  39           
SHEET    3   H 4 PHE B  93  SER B 107 -1  N  ILE B  99   O  ASN B 371           
SHEET    4   H 4 VAL B 175  ARG B 176 -1  O  VAL B 175   N  GLY B  96           
SHEET    1   I 5 ILE B  33  GLU B  44  0                                        
SHEET    2   I 5 ILE B 363  PRO B 376 -1  O  GLY B 368   N  SER B  39           
SHEET    3   I 5 PHE B  93  SER B 107 -1  N  ILE B  99   O  ASN B 371           
SHEET    4   I 5 VAL B 161  LEU B 164 -1  O  VAL B 163   N  TYR B 103           
SHEET    5   I 5 VAL B 414  ARG B 416 -1  O  TRP B 415   N  THR B 162           
SHEET    1   J 6 LEU B  77  GLU B  84  0                                        
SHEET    2   J 6 ARG B  63  TRP B  70 -1  N  ARG B  69   O  GLU B  78           
SHEET    3   J 6 GLY B  51  CYS B  55 -1  N  VAL B  54   O  ALA B  66           
SHEET    4   J 6 ILE B 350  GLU B 356 -1  O  VAL B 353   N  LEU B  53           
SHEET    5   J 6 THR B 120  PHE B 126 -1  N  ASN B 122   O  ALA B 354           
SHEET    6   J 6 LYS B 151  LEU B 156 -1  O  VAL B 152   N  ALA B 123           
SHEET    1   K 2 ASP B 179  GLU B 180  0                                        
SHEET    2   K 2 ARG B 194  CYS B 195 -1  O  CYS B 195   N  ASP B 179           
SHEET    1   L 4 ARG B 202  LEU B 208  0                                        
SHEET    2   L 4 ALA B 332  SER B 338 -1  O  VAL B 334   N  ILE B 206           
SHEET    3   L 4 THR B 236  LEU B 246 -1  N  THR B 239   O  SER B 335           
SHEET    4   L 4 SER B 295  ILE B 296 -1  O  ILE B 296   N  THR B 236           
SHEET    1   M 3 VAL B 288  MET B 292  0                                        
SHEET    2   M 3 THR B 236  LEU B 246 -1  N  PHE B 244   O  VAL B 288           
SHEET    3   M 3 ALA B 324  THR B 325 -1  O  THR B 325   N  SER B 245           
SHEET    1   N 4 THR B 223  ILE B 232  0                                        
SHEET    2   N 4 ILE B 305  LYS B 313 -1  O  LEU B 310   N  LEU B 225           
SHEET    3   N 4 THR B 254  MET B 263 -1  N  ASP B 261   O  LYS B 309           
SHEET    4   N 4 VAL B 272  ALA B 280 -1  O  VAL B 274   N  LEU B 260           
SHEET    1   O 4 ILE C  33  GLU C  44  0                                        
SHEET    2   O 4 ILE C 363  PRO C 376 -1  O  GLY C 368   N  SER C  39           
SHEET    3   O 4 PHE C  93  SER C 107 -1  N  ILE C  99   O  ASN C 371           
SHEET    4   O 4 VAL C 175  ARG C 176 -1  O  VAL C 175   N  GLY C  96           
SHEET    1   P 5 ILE C  33  GLU C  44  0                                        
SHEET    2   P 5 ILE C 363  PRO C 376 -1  O  GLY C 368   N  SER C  39           
SHEET    3   P 5 PHE C  93  SER C 107 -1  N  ILE C  99   O  ASN C 371           
SHEET    4   P 5 VAL C 161  LEU C 164 -1  O  VAL C 163   N  TYR C 103           
SHEET    5   P 5 VAL C 414  ARG C 416 -1  O  TRP C 415   N  THR C 162           
SHEET    1   Q 6 LEU C  77  GLU C  84  0                                        
SHEET    2   Q 6 ARG C  63  TRP C  70 -1  N  ARG C  69   O  GLU C  78           
SHEET    3   Q 6 GLY C  51  CYS C  55 -1  N  VAL C  54   O  ALA C  66           
SHEET    4   Q 6 ILE C 350  GLU C 356 -1  O  THR C 351   N  CYS C  55           
SHEET    5   Q 6 THR C 120  PHE C 126 -1  N  ASN C 122   O  ALA C 354           
SHEET    6   Q 6 LYS C 151  LEU C 156 -1  O  VAL C 152   N  ALA C 123           
SHEET    1   R 2 ASP C 179  GLU C 180  0                                        
SHEET    2   R 2 ARG C 194  CYS C 195 -1  O  CYS C 195   N  ASP C 179           
SHEET    1   S 4 ARG C 202  LEU C 208  0                                        
SHEET    2   S 4 ALA C 332  SER C 338 -1  O  VAL C 334   N  ILE C 206           
SHEET    3   S 4 THR C 236  LEU C 246 -1  N  THR C 239   O  SER C 335           
SHEET    4   S 4 SER C 295  ILE C 296 -1  O  ILE C 296   N  THR C 236           
SHEET    1   T 3 VAL C 288  MET C 292  0                                        
SHEET    2   T 3 THR C 236  LEU C 246 -1  N  PHE C 244   O  VAL C 288           
SHEET    3   T 3 ALA C 324  THR C 325 -1  O  THR C 325   N  SER C 245           
SHEET    1   U 4 THR C 223  ILE C 232  0                                        
SHEET    2   U 4 ILE C 305  LYS C 313 -1  O  LEU C 310   N  LEU C 225           
SHEET    3   U 4 THR C 254  MET C 263 -1  N  ASP C 261   O  LYS C 309           
SHEET    4   U 4 VAL C 272  ALA C 280 -1  O  VAL C 274   N  LEU C 260           
SHEET    1   V 4 ILE D  33  GLU D  44  0                                        
SHEET    2   V 4 ILE D 363  PRO D 376 -1  O  GLY D 368   N  SER D  39           
SHEET    3   V 4 PHE D  93  SER D 107 -1  N  ILE D  99   O  ASN D 371           
SHEET    4   V 4 VAL D 175  ARG D 176 -1  O  VAL D 175   N  GLY D  96           
SHEET    1   W 5 ILE D  33  GLU D  44  0                                        
SHEET    2   W 5 ILE D 363  PRO D 376 -1  O  GLY D 368   N  SER D  39           
SHEET    3   W 5 PHE D  93  SER D 107 -1  N  ILE D  99   O  ASN D 371           
SHEET    4   W 5 VAL D 161  LEU D 164 -1  O  VAL D 163   N  TYR D 103           
SHEET    5   W 5 VAL D 414  ARG D 416 -1  O  TRP D 415   N  THR D 162           
SHEET    1   X 6 LEU D  77  GLU D  84  0                                        
SHEET    2   X 6 ARG D  63  TRP D  70 -1  N  ARG D  69   O  GLU D  78           
SHEET    3   X 6 GLY D  51  CYS D  55 -1  N  VAL D  54   O  ALA D  66           
SHEET    4   X 6 ILE D 350  GLU D 356 -1  O  VAL D 353   N  LEU D  53           
SHEET    5   X 6 THR D 120  PHE D 126 -1  N  ASN D 122   O  ALA D 354           
SHEET    6   X 6 LYS D 151  LEU D 156 -1  O  VAL D 152   N  ALA D 123           
SHEET    1   Y 2 ASP D 179  GLU D 180  0                                        
SHEET    2   Y 2 ARG D 194  CYS D 195 -1  O  CYS D 195   N  ASP D 179           
SHEET    1   Z 4 ARG D 202  LEU D 208  0                                        
SHEET    2   Z 4 ALA D 332  SER D 338 -1  O  VAL D 334   N  ILE D 206           
SHEET    3   Z 4 THR D 236  LEU D 246 -1  N  THR D 239   O  SER D 335           
SHEET    4   Z 4 SER D 295  ILE D 296 -1  O  ILE D 296   N  THR D 236           
SHEET    1  AA 3 VAL D 288  MET D 292  0                                        
SHEET    2  AA 3 THR D 236  LEU D 246 -1  N  PHE D 244   O  VAL D 288           
SHEET    3  AA 3 ALA D 324  THR D 325 -1  O  THR D 325   N  SER D 245           
SHEET    1  AB 4 THR D 223  ILE D 232  0                                        
SHEET    2  AB 4 ILE D 305  LYS D 313 -1  O  LEU D 310   N  LEU D 225           
SHEET    3  AB 4 THR D 254  MET D 263 -1  N  ASP D 261   O  LYS D 309           
SHEET    4  AB 4 VAL D 272  ALA D 280 -1  O  VAL D 274   N  LEU D 260           
SHEET    1  AC 4 ILE E  33  GLU E  44  0                                        
SHEET    2  AC 4 ILE E 363  PRO E 376 -1  O  GLY E 368   N  SER E  39           
SHEET    3  AC 4 PHE E  93  SER E 107 -1  N  ILE E  99   O  ASN E 371           
SHEET    4  AC 4 VAL E 175  ARG E 176 -1  O  VAL E 175   N  GLY E  96           
SHEET    1  AD 5 ILE E  33  GLU E  44  0                                        
SHEET    2  AD 5 ILE E 363  PRO E 376 -1  O  GLY E 368   N  SER E  39           
SHEET    3  AD 5 PHE E  93  SER E 107 -1  N  ILE E  99   O  ASN E 371           
SHEET    4  AD 5 VAL E 161  LEU E 164 -1  O  VAL E 163   N  TYR E 103           
SHEET    5  AD 5 VAL E 414  ARG E 416 -1  O  TRP E 415   N  THR E 162           
SHEET    1  AE 6 LEU E  77  GLU E  84  0                                        
SHEET    2  AE 6 ARG E  63  TRP E  70 -1  N  ARG E  69   O  GLU E  78           
SHEET    3  AE 6 GLY E  51  CYS E  55 -1  N  VAL E  54   O  ALA E  66           
SHEET    4  AE 6 ILE E 350  GLU E 356 -1  O  VAL E 353   N  LEU E  53           
SHEET    5  AE 6 THR E 120  PHE E 126 -1  N  ASN E 122   O  ALA E 354           
SHEET    6  AE 6 LYS E 151  LEU E 156 -1  O  VAL E 152   N  ALA E 123           
SHEET    1  AF 2 ASP E 179  GLU E 180  0                                        
SHEET    2  AF 2 ARG E 194  CYS E 195 -1  O  CYS E 195   N  ASP E 179           
SHEET    1  AG 4 ARG E 202  LEU E 208  0                                        
SHEET    2  AG 4 ALA E 332  SER E 338 -1  O  VAL E 334   N  ILE E 206           
SHEET    3  AG 4 THR E 236  LEU E 246 -1  N  THR E 239   O  SER E 335           
SHEET    4  AG 4 SER E 295  ILE E 296 -1  O  ILE E 296   N  THR E 236           
SHEET    1  AH 3 VAL E 288  MET E 292  0                                        
SHEET    2  AH 3 THR E 236  LEU E 246 -1  N  PHE E 244   O  VAL E 288           
SHEET    3  AH 3 ALA E 324  THR E 325 -1  O  THR E 325   N  SER E 245           
SHEET    1  AI 4 THR E 223  ILE E 232  0                                        
SHEET    2  AI 4 ILE E 305  LYS E 313 -1  O  LEU E 310   N  LEU E 225           
SHEET    3  AI 4 THR E 254  MET E 263 -1  N  ASP E 261   O  LYS E 309           
SHEET    4  AI 4 VAL E 272  ALA E 280 -1  O  VAL E 274   N  LEU E 260           
LINK         OD2 ASP A  27                CO    CO A 443     1555   1555  2.15  
LINK         OD2 ASP B  27                CO    CO A 443     1555   4566  2.11  
LINK         OD2 ASP C  27                CO    CO C 443     1555   1555  2.12  
LINK         OD2 ASP D  27                CO    CO A 443     1555   5555  2.11  
LINK         OD2 ASP E  27                CO    CO E 443     1555   1555  2.16  
CISPEP   1 ARG A  348    PRO A  349          0        -1.52                     
CISPEP   2 ARG B  348    PRO B  349          0        -1.67                     
CISPEP   3 ARG C  348    PRO C  349          0        -0.46                     
CISPEP   4 ARG D  348    PRO D  349          0        -0.96                     
CISPEP   5 ARG E  348    PRO E  349          0        -0.87                     
SITE     1 AC1  3 ASP A  27  ASP B  27  ASP D  27                               
SITE     1 AC2  3 ALA A 200  ALA B 200  ALA D 200                               
SITE     1 AC3  1 ASP C  27                                                     
SITE     1 AC4  1 ALA C 200                                                     
SITE     1 AC5  1 ASP E  27                                                     
SITE     1 AC6  1 ALA E 200                                                     
CRYST1  303.431  303.431  303.431  90.00  90.00  90.00 I 2 3       120          
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      0.003296  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.003296  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003296        0.00000                         
MTRIX1   1  0.810781  0.303649 -0.500432       58.60710    1                    
MTRIX2   1  0.308983  0.504104  0.806479      -94.00760    1                    
MTRIX3   1  0.497156 -0.808503  0.314896      150.99100    1                    
MTRIX1   2  0.501223  0.806866 -0.312639        0.36153    1                    
MTRIX2   2  0.812262 -0.314144  0.491471        1.83655    1                    
MTRIX3   2  0.298337 -0.500282 -0.812843      305.24799    1                    
MTRIX1   3  0.491694  0.814407  0.308185      -93.07320    1                    
MTRIX2   3  0.813667 -0.303659 -0.495719      149.92799    1                    
MTRIX3   3 -0.310134  0.494502 -0.811963      246.52100    1                    
MTRIX1   4  0.805853  0.312112  0.503177      -94.39900    1                    
MTRIX2   4  0.307898  0.504986 -0.806342      150.97200    1                    
MTRIX3   4 -0.505767  0.804720  0.310846       58.79010    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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