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Database: PDB
Entry: 3MMP
LinkDB: 3MMP
Original site: 3MMP 
HEADER    TRANSFERASE                             20-APR-10   3MMP              
TITLE     STRUCTURE OF THE QB REPLICASE, AN RNA-DEPENDENT RNA POLYMERASE        
TITLE    2 CONSISTING OF VIRAL AND HOST PROTEINS                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELONGATION FACTOR TU 2, ELONGATION FACTOR TS;              
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: EF-TU 2, P-43, EF-TS;                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: RNA-DIRECTED RNA POLYMERASE BETA CHAIN;                    
COMPND   8 CHAIN: G, F;                                                         
COMPND   9 SYNONYM: RNA REPLICASE BETA CHAIN;                                   
COMPND  10 EC: 2.7.7.48;                                                        
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: TUFB, B3980, JW3943, TSF, B0170, JW0165;                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PBAD33;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE QBETA;                     
SOURCE  13 ORGANISM_COMMON: BACTERIOPHAGE Q-BETA;                               
SOURCE  14 ORGANISM_TAXID: 39803;                                               
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PBAD33                                    
KEYWDS    RDRP,HOST-FACTOR COMPLEX, TRANSLATION, TRANSFERASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.T.KIDMOSE,N.N.VASILIEV,A.B.CHETVERIN,C.R.KNUDSEN,G.R.ANDERSEN       
REVDAT   3   30-JUN-10 3MMP    1       JRNL                                     
REVDAT   2   23-JUN-10 3MMP    1       JRNL                                     
REVDAT   1   09-JUN-10 3MMP    0                                                
JRNL        AUTH   R.T.KIDMOSE,N.N.VASILIEV,A.B.CHETVERIN,G.R.ANDERSEN,         
JRNL        AUTH 2 C.R.KNUDSEN                                                  
JRNL        TITL   STRUCTURE OF THE QBETA REPLICASE, AN RNA-DEPENDENT RNA       
JRNL        TITL 2 POLYMERASE CONSISTING OF VIRAL AND HOST PROTEINS.            
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 107 10884 2010              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   20534494                                                     
JRNL        DOI    10.1073/PNAS.1003015107                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6_289)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.28                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 122547                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.630                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1993                            
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 47.2917 -  6.0215    0.99     8684   151  0.1717 0.1819        
REMARK   3     2  6.0215 -  4.7809    1.00     8677   147  0.1754 0.2049        
REMARK   3     3  4.7809 -  4.1770    1.00     8632   148  0.1663 0.1780        
REMARK   3     4  4.1770 -  3.7953    1.00     8641   128  0.1888 0.2049        
REMARK   3     5  3.7953 -  3.5233    1.00     8591   135  0.2022 0.2335        
REMARK   3     6  3.5233 -  3.3157    1.00     8630   142  0.2147 0.2300        
REMARK   3     7  3.3157 -  3.1497    1.00     8611   149  0.2337 0.2198        
REMARK   3     8  3.1497 -  3.0126    1.00     8592   136  0.2355 0.2752        
REMARK   3     9  3.0126 -  2.8966    1.00     8598   140  0.2487 0.2757        
REMARK   3    10  2.8966 -  2.7967    1.00     8588   139  0.2515 0.2946        
REMARK   3    11  2.7967 -  2.7092    1.00     8639   143  0.2594 0.3210        
REMARK   3    12  2.7092 -  2.6318    1.00     8540   149  0.2557 0.2976        
REMARK   3    13  2.6318 -  2.5625    1.00     8601   145  0.2661 0.2943        
REMARK   3    14  2.5625 -  2.5000    1.00     8530   141  0.2729 0.3353        
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              : 0.33                                          
REMARK   3   B_SOL              : 46.62                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.950           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 11.95000                                             
REMARK   3    B22 (A**2) : -5.98520                                             
REMARK   3    B33 (A**2) : -5.96480                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.22040                                             
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      :  0.008          18828                                  
REMARK   3   ANGLE     :  1.053          25452                                  
REMARK   3   CHIRALITY :  0.075           2888                                  
REMARK   3   PLANARITY :  0.004           3298                                  
REMARK   3   DIHEDRAL  : 16.709           6978                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 3                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN G AND (RESSEQ 7:113 OR RESSEQ 119:    
REMARK   3                          519 OR RESSEQ 533:573 )                     
REMARK   3     SELECTION          : CHAIN F AND (RESSEQ 7:113 OR RESSEQ 119:    
REMARK   3                          519 OR RESSEQ 533:573 )                     
REMARK   3     ATOM PAIRS NUMBER  : 4318                                        
REMARK   3     RMSD               : 0.040                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 1009:1041 OR RESSEQ     
REMARK   3                          1064:1392 )                                 
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 1009:1041 OR RESSEQ     
REMARK   3                          1064:1392 )                                 
REMARK   3     ATOM PAIRS NUMBER  : 2790                                        
REMARK   3     RMSD               : 0.054                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 3:282 )                 
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 3:282 )                 
REMARK   3     ATOM PAIRS NUMBER  : 2108                                        
REMARK   3     RMSD               : 0.023                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3MMP COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB058737.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 122568                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.11200                            
REMARK 200  R SYM                      (I) : 0.06900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.2900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.57100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.870                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1EFU                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M KCL, 0.05M HEPES PH 7.5, 27%-30%    
REMARK 280  V/V PENTAERYTHRITOL PROPOXYLATE (5/4 PO/OH), VAPOR DIFFUSION,       
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      127.35500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       69.70000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      127.35500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       69.70000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 51620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 51420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13880 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 100910 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G, C, F                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     HIS A   999                                                      
REMARK 465     MET A  1000                                                      
REMARK 465     SER A  1001                                                      
REMARK 465     LYS A  1002                                                      
REMARK 465     GLU A  1003                                                      
REMARK 465     LYS A  1004                                                      
REMARK 465     PHE A  1005                                                      
REMARK 465     GLU A  1006                                                      
REMARK 465     ARG A  1007                                                      
REMARK 465     THR A  1008                                                      
REMARK 465     ALA A  1042                                                      
REMARK 465     ALA A  1043                                                      
REMARK 465     ARG A  1044                                                      
REMARK 465     ALA A  1045                                                      
REMARK 465     PHE A  1046                                                      
REMARK 465     ASP A  1047                                                      
REMARK 465     GLN A  1048                                                      
REMARK 465     ILE A  1049                                                      
REMARK 465     ASP A  1050                                                      
REMARK 465     ASN A  1051                                                      
REMARK 465     ALA A  1052                                                      
REMARK 465     PRO A  1053                                                      
REMARK 465     GLU A  1054                                                      
REMARK 465     GLU A  1055                                                      
REMARK 465     LYS A  1056                                                      
REMARK 465     ALA A  1057                                                      
REMARK 465     ARG A  1058                                                      
REMARK 465     GLY A  1059                                                      
REMARK 465     ILE A  1060                                                      
REMARK 465     THR A  1061                                                      
REMARK 465     ILE A  1062                                                      
REMARK 465     ASN A  1063                                                      
REMARK 465     MET G     1                                                      
REMARK 465     SER G     2                                                      
REMARK 465     LYS G     3                                                      
REMARK 465     THR G     4                                                      
REMARK 465     ALA G     5                                                      
REMARK 465     SER G     6                                                      
REMARK 465     ASP G   114                                                      
REMARK 465     TYR G   115                                                      
REMARK 465     SER G   116                                                      
REMARK 465     GLU G   117                                                      
REMARK 465     ASP G   118                                                      
REMARK 465     GLU G   520                                                      
REMARK 465     SER G   521                                                      
REMARK 465     ASN G   522                                                      
REMARK 465     ASP G   523                                                      
REMARK 465     GLY G   524                                                      
REMARK 465     LEU G   525                                                      
REMARK 465     PRO G   526                                                      
REMARK 465     LEU G   527                                                      
REMARK 465     ARG G   528                                                      
REMARK 465     GLY G   529                                                      
REMARK 465     PRO G   530                                                      
REMARK 465     SER G   531                                                      
REMARK 465     GLY G   532                                                      
REMARK 465     PRO G   574                                                      
REMARK 465     TYR G   575                                                      
REMARK 465     GLY G   576                                                      
REMARK 465     VAL G   577                                                      
REMARK 465     PHE G   578                                                      
REMARK 465     GLN G   579                                                      
REMARK 465     GLY G   580                                                      
REMARK 465     THR G   581                                                      
REMARK 465     LYS G   582                                                      
REMARK 465     VAL G   583                                                      
REMARK 465     ALA G   584                                                      
REMARK 465     SER G   585                                                      
REMARK 465     LEU G   586                                                      
REMARK 465     HIS G   587                                                      
REMARK 465     GLU G   588                                                      
REMARK 465     ALA G   589                                                      
REMARK 465     MET C     0                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     HIS C   999                                                      
REMARK 465     MET C  1000                                                      
REMARK 465     SER C  1001                                                      
REMARK 465     LYS C  1002                                                      
REMARK 465     GLU C  1003                                                      
REMARK 465     LYS C  1004                                                      
REMARK 465     PHE C  1005                                                      
REMARK 465     GLU C  1006                                                      
REMARK 465     ARG C  1007                                                      
REMARK 465     THR C  1008                                                      
REMARK 465     ALA C  1042                                                      
REMARK 465     ALA C  1043                                                      
REMARK 465     ARG C  1044                                                      
REMARK 465     ALA C  1045                                                      
REMARK 465     PHE C  1046                                                      
REMARK 465     ASP C  1047                                                      
REMARK 465     GLN C  1048                                                      
REMARK 465     ILE C  1049                                                      
REMARK 465     ASP C  1050                                                      
REMARK 465     ASN C  1051                                                      
REMARK 465     ALA C  1052                                                      
REMARK 465     PRO C  1053                                                      
REMARK 465     GLU C  1054                                                      
REMARK 465     GLU C  1055                                                      
REMARK 465     LYS C  1056                                                      
REMARK 465     ALA C  1057                                                      
REMARK 465     ARG C  1058                                                      
REMARK 465     GLY C  1059                                                      
REMARK 465     ILE C  1060                                                      
REMARK 465     THR C  1061                                                      
REMARK 465     ILE C  1062                                                      
REMARK 465     ASN C  1063                                                      
REMARK 465     MET F     1                                                      
REMARK 465     SER F     2                                                      
REMARK 465     LYS F     3                                                      
REMARK 465     THR F     4                                                      
REMARK 465     ALA F     5                                                      
REMARK 465     SER F     6                                                      
REMARK 465     ASP F   114                                                      
REMARK 465     TYR F   115                                                      
REMARK 465     SER F   116                                                      
REMARK 465     GLU F   117                                                      
REMARK 465     ASP F   118                                                      
REMARK 465     GLU F   520                                                      
REMARK 465     SER F   521                                                      
REMARK 465     ASN F   522                                                      
REMARK 465     ASP F   523                                                      
REMARK 465     GLY F   524                                                      
REMARK 465     LEU F   525                                                      
REMARK 465     PRO F   526                                                      
REMARK 465     LEU F   527                                                      
REMARK 465     ARG F   528                                                      
REMARK 465     GLY F   529                                                      
REMARK 465     PRO F   530                                                      
REMARK 465     SER F   531                                                      
REMARK 465     GLY F   532                                                      
REMARK 465     PRO F   574                                                      
REMARK 465     TYR F   575                                                      
REMARK 465     GLY F   576                                                      
REMARK 465     VAL F   577                                                      
REMARK 465     PHE F   578                                                      
REMARK 465     GLN F   579                                                      
REMARK 465     GLY F   580                                                      
REMARK 465     THR F   581                                                      
REMARK 465     LYS F   582                                                      
REMARK 465     VAL F   583                                                      
REMARK 465     ALA F   584                                                      
REMARK 465     SER F   585                                                      
REMARK 465     LEU F   586                                                      
REMARK 465     HIS F   587                                                      
REMARK 465     GLU F   588                                                      
REMARK 465     ALA F   589                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A1318   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG A1318   NE  -  CZ  -  NH2 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG C1318   CD  -  NE  -  CZ  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ARG C1318   NE  -  CZ  -  NH1 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ARG C1318   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  30     -169.29     53.93                                   
REMARK 500    LYS A 103       45.59     34.56                                   
REMARK 500    ARG A 132      -66.02    -97.41                                   
REMARK 500    SER A 186       94.72    -43.03                                   
REMARK 500    PRO A 207      149.39    -37.41                                   
REMARK 500    GLU A 236       74.40   -167.01                                   
REMARK 500    GLU A 262      122.44    -37.15                                   
REMARK 500    GLU A 265      -80.26     25.28                                   
REMARK 500    LYS A 266       51.55     88.42                                   
REMARK 500    GLN A1097       99.82   -170.33                                   
REMARK 500    PRO A1163       67.39    -69.68                                   
REMARK 500    ARG A1223      -48.79   -134.62                                   
REMARK 500    ILE A1247      -58.66     63.07                                   
REMARK 500    PHE A1323     -159.26   -139.01                                   
REMARK 500    ARG A1333      -61.43     69.42                                   
REMARK 500    LEU A1392      -87.76   -122.89                                   
REMARK 500    ARG G   8       78.97   -151.84                                   
REMARK 500    SER G  83       65.42   -113.75                                   
REMARK 500    LYS G 214      -66.48   -135.82                                   
REMARK 500    SER G 276       81.00    -51.43                                   
REMARK 500    ALA G 277       46.82     39.15                                   
REMARK 500    ASN C  30     -168.66     53.37                                   
REMARK 500    LYS C 103       44.74     36.39                                   
REMARK 500    ARG C 132      -66.94    -96.22                                   
REMARK 500    SER C 186       94.22    -42.67                                   
REMARK 500    PRO C 207      149.35    -36.68                                   
REMARK 500    GLU C 236       74.11   -168.08                                   
REMARK 500    GLU C 262      122.83    -36.24                                   
REMARK 500    GLU C 265      -80.46     25.14                                   
REMARK 500    LYS C 266       51.20     88.75                                   
REMARK 500    GLN C1097      100.19   -170.43                                   
REMARK 500    PRO C1163       65.64    -68.28                                   
REMARK 500    ARG C1223      -49.02   -133.46                                   
REMARK 500    ILE C1247      -56.44     61.43                                   
REMARK 500    ARG C1333      -61.16     67.98                                   
REMARK 500    ARG F   8       78.54   -151.88                                   
REMARK 500    SER F  83       66.74   -114.19                                   
REMARK 500    LYS F 214      -65.68   -134.26                                   
REMARK 500    ASN F 268       14.62     58.82                                   
REMARK 500    SER F 276       80.53    -50.98                                   
REMARK 500    ALA F 277       47.59     39.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU A 1392     SER A 1393                 -143.07                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 667        DISTANCE =  5.82 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PXN A 1394                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PXN C 1394                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 CHAINS A AND C ARE A CHIMERA OF UNP ENTRIES P0A6P1 AND P0CE48 WITH   
REMARK 999 A SINGLE HIS AS LINKER                                               
DBREF  3MMP A    0   282  UNP    P0A6P1   EFTS_ECOLI       1    283             
DBREF  3MMP A 1000  1393  UNP    P0CE48   EFTU2_ECOLI      1    394             
DBREF  3MMP G    1   589  UNP    P14647   RDRP_BPQBE       1    589             
DBREF  3MMP C    0   282  UNP    P0A6P1   EFTS_ECOLI       1    283             
DBREF  3MMP C 1000  1393  UNP    P0CE48   EFTU2_ECOLI      1    394             
DBREF  3MMP F    1   589  UNP    P14647   RDRP_BPQBE       1    589             
SEQADV 3MMP HIS A  999  UNP  P0A6P1              LINKER                         
SEQADV 3MMP HIS C  999  UNP  P0A6P1              LINKER                         
SEQRES   1 A  678  MET ALA GLU ILE THR ALA SER LEU VAL LYS GLU LEU ARG          
SEQRES   2 A  678  GLU ARG THR GLY ALA GLY MET MET ASP CYS LYS LYS ALA          
SEQRES   3 A  678  LEU THR GLU ALA ASN GLY ASP ILE GLU LEU ALA ILE GLU          
SEQRES   4 A  678  ASN MET ARG LYS SER GLY ALA ILE LYS ALA ALA LYS LYS          
SEQRES   5 A  678  ALA GLY ASN VAL ALA ALA ASP GLY VAL ILE LYS THR LYS          
SEQRES   6 A  678  ILE ASP GLY ASN TYR GLY ILE ILE LEU GLU VAL ASN CYS          
SEQRES   7 A  678  GLN THR ASP PHE VAL ALA LYS ASP ALA GLY PHE GLN ALA          
SEQRES   8 A  678  PHE ALA ASP LYS VAL LEU ASP ALA ALA VAL ALA GLY LYS          
SEQRES   9 A  678  ILE THR ASP VAL GLU VAL LEU LYS ALA GLN PHE GLU GLU          
SEQRES  10 A  678  GLU ARG VAL ALA LEU VAL ALA LYS ILE GLY GLU ASN ILE          
SEQRES  11 A  678  ASN ILE ARG ARG VAL ALA ALA LEU GLU GLY ASP VAL LEU          
SEQRES  12 A  678  GLY SER TYR GLN HIS GLY ALA ARG ILE GLY VAL LEU VAL          
SEQRES  13 A  678  ALA ALA LYS GLY ALA ASP GLU GLU LEU VAL LYS HIS ILE          
SEQRES  14 A  678  ALA MET HIS VAL ALA ALA SER LYS PRO GLU PHE ILE LYS          
SEQRES  15 A  678  PRO GLU ASP VAL SER ALA GLU VAL VAL GLU LYS GLU TYR          
SEQRES  16 A  678  GLN VAL GLN LEU ASP ILE ALA MET GLN SER GLY LYS PRO          
SEQRES  17 A  678  LYS GLU ILE ALA GLU LYS MET VAL GLU GLY ARG MET LYS          
SEQRES  18 A  678  LYS PHE THR GLY GLU VAL SER LEU THR GLY GLN PRO PHE          
SEQRES  19 A  678  VAL MET GLU PRO SER LYS THR VAL GLY GLN LEU LEU LYS          
SEQRES  20 A  678  GLU HIS ASN ALA GLU VAL THR GLY PHE ILE ARG PHE GLU          
SEQRES  21 A  678  VAL GLY GLU GLY ILE GLU LYS VAL GLU THR ASP PHE ALA          
SEQRES  22 A  678  ALA GLU VAL ALA ALA MET SER LYS GLN SER HIS MET SER          
SEQRES  23 A  678  LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL ASN VAL          
SEQRES  24 A  678  GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR LEU          
SEQRES  25 A  678  THR ALA ALA ILE THR THR VAL LEU ALA LYS THR TYR GLY          
SEQRES  26 A  678  GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN ALA PRO          
SEQRES  27 A  678  GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR SER HIS          
SEQRES  28 A  678  VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA HIS VAL          
SEQRES  29 A  678  ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN MET ILE          
SEQRES  30 A  678  THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU VAL VAL          
SEQRES  31 A  678  ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG GLU HIS          
SEQRES  32 A  678  ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR ILE ILE          
SEQRES  33 A  678  VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP GLU GLU          
SEQRES  34 A  678  LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU LEU LEU          
SEQRES  35 A  678  SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO ILE VAL          
SEQRES  36 A  678  ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP ALA GLU          
SEQRES  37 A  678  TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE LEU ASP          
SEQRES  38 A  678  SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP LYS PRO          
SEQRES  39 A  678  PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE SER GLY          
SEQRES  40 A  678  ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG GLY ILE          
SEQRES  41 A  678  ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY ILE LYS          
SEQRES  42 A  678  GLU THR GLN LYS SER THR CYS THR GLY VAL GLU MET PHE          
SEQRES  43 A  678  ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU ASN VAL          
SEQRES  44 A  678  GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU ILE GLU          
SEQRES  45 A  678  ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE LYS PRO          
SEQRES  46 A  678  HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU SER LYS          
SEQRES  47 A  678  ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS GLY TYR          
SEQRES  48 A  678  ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR GLY          
SEQRES  49 A  678  THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL MET PRO          
SEQRES  50 A  678  GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE HIS PRO          
SEQRES  51 A  678  ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE ARG GLU          
SEQRES  52 A  678  GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA LYS VAL          
SEQRES  53 A  678  LEU SER                                                      
SEQRES   1 G  589  MET SER LYS THR ALA SER SER ARG ASN SER LEU SER ALA          
SEQRES   2 G  589  GLN LEU ARG ARG ALA ALA ASN THR ARG ILE GLU VAL GLU          
SEQRES   3 G  589  GLY ASN LEU ALA LEU SER ILE ALA ASN ASP LEU LEU LEU          
SEQRES   4 G  589  ALA TYR GLY GLN SER PRO PHE ASN SER GLU ALA GLU CYS          
SEQRES   5 G  589  ILE SER PHE SER PRO ARG PHE ASP GLY THR PRO ASP ASP          
SEQRES   6 G  589  PHE ARG ILE ASN TYR LEU LYS ALA GLU ILE MET SER LYS          
SEQRES   7 G  589  TYR ASP ASP PHE SER LEU GLY ILE ASP THR GLU ALA VAL          
SEQRES   8 G  589  ALA TRP GLU LYS PHE LEU ALA ALA GLU ALA GLU CYS ALA          
SEQRES   9 G  589  LEU THR ASN ALA ARG LEU TYR ARG PRO ASP TYR SER GLU          
SEQRES  10 G  589  ASP PHE ASN PHE SER LEU GLY GLU SER CYS ILE HIS MET          
SEQRES  11 G  589  ALA ARG ARG LYS ILE ALA LYS LEU ILE GLY ASP VAL PRO          
SEQRES  12 G  589  SER VAL GLU GLY MET LEU ARG HIS CYS ARG PHE SER GLY          
SEQRES  13 G  589  GLY ALA THR THR THR ASN ASN ARG SER TYR GLY HIS PRO          
SEQRES  14 G  589  SER PHE LYS PHE ALA LEU PRO GLN ALA CYS THR PRO ARG          
SEQRES  15 G  589  ALA LEU LYS TYR VAL LEU ALA LEU ARG ALA SER THR HIS          
SEQRES  16 G  589  PHE ASP THR ARG ILE SER ASP ILE SER PRO PHE ASN LYS          
SEQRES  17 G  589  ALA VAL THR VAL PRO LYS ASN SER LYS THR ASP ARG CYS          
SEQRES  18 G  589  ILE ALA ILE GLU PRO GLY TRP ASN MET PHE PHE GLN LEU          
SEQRES  19 G  589  GLY ILE GLY GLY ILE LEU ARG ASP ARG LEU ARG CYS TRP          
SEQRES  20 G  589  GLY ILE ASP LEU ASN ASP GLN THR ILE ASN GLN ARG ARG          
SEQRES  21 G  589  ALA HIS GLU GLY SER VAL THR ASN ASN LEU ALA THR VAL          
SEQRES  22 G  589  ASP LEU SER ALA ALA SER ASP SER ILE SER LEU ALA LEU          
SEQRES  23 G  589  CYS GLU LEU LEU LEU PRO PRO GLY TRP PHE GLU VAL LEU          
SEQRES  24 G  589  MET ASP LEU ARG SER PRO LYS GLY ARG LEU PRO ASP GLY          
SEQRES  25 G  589  SER VAL VAL THR TYR GLU LYS ILE SER SER MET GLY ASN          
SEQRES  26 G  589  GLY TYR THR PHE GLU LEU GLU SER LEU ILE PHE ALA SER          
SEQRES  27 G  589  LEU ALA ARG SER VAL CYS GLU ILE LEU ASP LEU ASP SER          
SEQRES  28 G  589  SER GLU VAL THR VAL TYR GLY ASP ASP ILE ILE LEU PRO          
SEQRES  29 G  589  SER CYS ALA VAL PRO ALA LEU ARG GLU VAL PHE LYS TYR          
SEQRES  30 G  589  VAL GLY PHE THR THR ASN THR LYS LYS THR PHE SER GLU          
SEQRES  31 G  589  GLY PRO PHE ARG GLU SER CYS GLY LYS HIS TYR TYR SER          
SEQRES  32 G  589  GLY VAL ASP VAL THR PRO PHE TYR ILE ARG HIS ARG ILE          
SEQRES  33 G  589  VAL SER PRO ALA ASP LEU ILE LEU VAL LEU ASN ASN LEU          
SEQRES  34 G  589  TYR ARG TRP ALA THR ILE ASP GLY VAL TRP ASP PRO ARG          
SEQRES  35 G  589  ALA HIS SER VAL TYR LEU LYS TYR ARG LYS LEU LEU PRO          
SEQRES  36 G  589  LYS GLN LEU GLN ARG ASN THR ILE PRO ASP GLY TYR GLY          
SEQRES  37 G  589  ASP GLY ALA LEU VAL GLY SER VAL LEU ILE ASN PRO PHE          
SEQRES  38 G  589  ALA LYS ASN ARG GLY TRP ILE ARG TYR VAL PRO VAL ILE          
SEQRES  39 G  589  THR ASP HIS THR ARG ASP ARG GLU ARG ALA GLU LEU GLY          
SEQRES  40 G  589  SER TYR LEU TYR ASP LEU PHE SER ARG CYS LEU SER GLU          
SEQRES  41 G  589  SER ASN ASP GLY LEU PRO LEU ARG GLY PRO SER GLY CYS          
SEQRES  42 G  589  ASP SER ALA ASP LEU PHE ALA ILE ASP GLN LEU ILE CYS          
SEQRES  43 G  589  ARG SER ASN PRO THR LYS ILE SER ARG SER THR GLY LYS          
SEQRES  44 G  589  PHE ASP ILE GLN TYR ILE ALA CYS SER SER ARG VAL LEU          
SEQRES  45 G  589  ALA PRO TYR GLY VAL PHE GLN GLY THR LYS VAL ALA SER          
SEQRES  46 G  589  LEU HIS GLU ALA                                              
SEQRES   1 C  678  MET ALA GLU ILE THR ALA SER LEU VAL LYS GLU LEU ARG          
SEQRES   2 C  678  GLU ARG THR GLY ALA GLY MET MET ASP CYS LYS LYS ALA          
SEQRES   3 C  678  LEU THR GLU ALA ASN GLY ASP ILE GLU LEU ALA ILE GLU          
SEQRES   4 C  678  ASN MET ARG LYS SER GLY ALA ILE LYS ALA ALA LYS LYS          
SEQRES   5 C  678  ALA GLY ASN VAL ALA ALA ASP GLY VAL ILE LYS THR LYS          
SEQRES   6 C  678  ILE ASP GLY ASN TYR GLY ILE ILE LEU GLU VAL ASN CYS          
SEQRES   7 C  678  GLN THR ASP PHE VAL ALA LYS ASP ALA GLY PHE GLN ALA          
SEQRES   8 C  678  PHE ALA ASP LYS VAL LEU ASP ALA ALA VAL ALA GLY LYS          
SEQRES   9 C  678  ILE THR ASP VAL GLU VAL LEU LYS ALA GLN PHE GLU GLU          
SEQRES  10 C  678  GLU ARG VAL ALA LEU VAL ALA LYS ILE GLY GLU ASN ILE          
SEQRES  11 C  678  ASN ILE ARG ARG VAL ALA ALA LEU GLU GLY ASP VAL LEU          
SEQRES  12 C  678  GLY SER TYR GLN HIS GLY ALA ARG ILE GLY VAL LEU VAL          
SEQRES  13 C  678  ALA ALA LYS GLY ALA ASP GLU GLU LEU VAL LYS HIS ILE          
SEQRES  14 C  678  ALA MET HIS VAL ALA ALA SER LYS PRO GLU PHE ILE LYS          
SEQRES  15 C  678  PRO GLU ASP VAL SER ALA GLU VAL VAL GLU LYS GLU TYR          
SEQRES  16 C  678  GLN VAL GLN LEU ASP ILE ALA MET GLN SER GLY LYS PRO          
SEQRES  17 C  678  LYS GLU ILE ALA GLU LYS MET VAL GLU GLY ARG MET LYS          
SEQRES  18 C  678  LYS PHE THR GLY GLU VAL SER LEU THR GLY GLN PRO PHE          
SEQRES  19 C  678  VAL MET GLU PRO SER LYS THR VAL GLY GLN LEU LEU LYS          
SEQRES  20 C  678  GLU HIS ASN ALA GLU VAL THR GLY PHE ILE ARG PHE GLU          
SEQRES  21 C  678  VAL GLY GLU GLY ILE GLU LYS VAL GLU THR ASP PHE ALA          
SEQRES  22 C  678  ALA GLU VAL ALA ALA MET SER LYS GLN SER HIS MET SER          
SEQRES  23 C  678  LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL ASN VAL          
SEQRES  24 C  678  GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR LEU          
SEQRES  25 C  678  THR ALA ALA ILE THR THR VAL LEU ALA LYS THR TYR GLY          
SEQRES  26 C  678  GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN ALA PRO          
SEQRES  27 C  678  GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR SER HIS          
SEQRES  28 C  678  VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA HIS VAL          
SEQRES  29 C  678  ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN MET ILE          
SEQRES  30 C  678  THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU VAL VAL          
SEQRES  31 C  678  ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG GLU HIS          
SEQRES  32 C  678  ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR ILE ILE          
SEQRES  33 C  678  VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP GLU GLU          
SEQRES  34 C  678  LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU LEU LEU          
SEQRES  35 C  678  SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO ILE VAL          
SEQRES  36 C  678  ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP ALA GLU          
SEQRES  37 C  678  TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE LEU ASP          
SEQRES  38 C  678  SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP LYS PRO          
SEQRES  39 C  678  PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE SER GLY          
SEQRES  40 C  678  ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG GLY ILE          
SEQRES  41 C  678  ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY ILE LYS          
SEQRES  42 C  678  GLU THR GLN LYS SER THR CYS THR GLY VAL GLU MET PHE          
SEQRES  43 C  678  ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU ASN VAL          
SEQRES  44 C  678  GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU ILE GLU          
SEQRES  45 C  678  ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE LYS PRO          
SEQRES  46 C  678  HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU SER LYS          
SEQRES  47 C  678  ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS GLY TYR          
SEQRES  48 C  678  ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR GLY          
SEQRES  49 C  678  THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL MET PRO          
SEQRES  50 C  678  GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE HIS PRO          
SEQRES  51 C  678  ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE ARG GLU          
SEQRES  52 C  678  GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA LYS VAL          
SEQRES  53 C  678  LEU SER                                                      
SEQRES   1 F  589  MET SER LYS THR ALA SER SER ARG ASN SER LEU SER ALA          
SEQRES   2 F  589  GLN LEU ARG ARG ALA ALA ASN THR ARG ILE GLU VAL GLU          
SEQRES   3 F  589  GLY ASN LEU ALA LEU SER ILE ALA ASN ASP LEU LEU LEU          
SEQRES   4 F  589  ALA TYR GLY GLN SER PRO PHE ASN SER GLU ALA GLU CYS          
SEQRES   5 F  589  ILE SER PHE SER PRO ARG PHE ASP GLY THR PRO ASP ASP          
SEQRES   6 F  589  PHE ARG ILE ASN TYR LEU LYS ALA GLU ILE MET SER LYS          
SEQRES   7 F  589  TYR ASP ASP PHE SER LEU GLY ILE ASP THR GLU ALA VAL          
SEQRES   8 F  589  ALA TRP GLU LYS PHE LEU ALA ALA GLU ALA GLU CYS ALA          
SEQRES   9 F  589  LEU THR ASN ALA ARG LEU TYR ARG PRO ASP TYR SER GLU          
SEQRES  10 F  589  ASP PHE ASN PHE SER LEU GLY GLU SER CYS ILE HIS MET          
SEQRES  11 F  589  ALA ARG ARG LYS ILE ALA LYS LEU ILE GLY ASP VAL PRO          
SEQRES  12 F  589  SER VAL GLU GLY MET LEU ARG HIS CYS ARG PHE SER GLY          
SEQRES  13 F  589  GLY ALA THR THR THR ASN ASN ARG SER TYR GLY HIS PRO          
SEQRES  14 F  589  SER PHE LYS PHE ALA LEU PRO GLN ALA CYS THR PRO ARG          
SEQRES  15 F  589  ALA LEU LYS TYR VAL LEU ALA LEU ARG ALA SER THR HIS          
SEQRES  16 F  589  PHE ASP THR ARG ILE SER ASP ILE SER PRO PHE ASN LYS          
SEQRES  17 F  589  ALA VAL THR VAL PRO LYS ASN SER LYS THR ASP ARG CYS          
SEQRES  18 F  589  ILE ALA ILE GLU PRO GLY TRP ASN MET PHE PHE GLN LEU          
SEQRES  19 F  589  GLY ILE GLY GLY ILE LEU ARG ASP ARG LEU ARG CYS TRP          
SEQRES  20 F  589  GLY ILE ASP LEU ASN ASP GLN THR ILE ASN GLN ARG ARG          
SEQRES  21 F  589  ALA HIS GLU GLY SER VAL THR ASN ASN LEU ALA THR VAL          
SEQRES  22 F  589  ASP LEU SER ALA ALA SER ASP SER ILE SER LEU ALA LEU          
SEQRES  23 F  589  CYS GLU LEU LEU LEU PRO PRO GLY TRP PHE GLU VAL LEU          
SEQRES  24 F  589  MET ASP LEU ARG SER PRO LYS GLY ARG LEU PRO ASP GLY          
SEQRES  25 F  589  SER VAL VAL THR TYR GLU LYS ILE SER SER MET GLY ASN          
SEQRES  26 F  589  GLY TYR THR PHE GLU LEU GLU SER LEU ILE PHE ALA SER          
SEQRES  27 F  589  LEU ALA ARG SER VAL CYS GLU ILE LEU ASP LEU ASP SER          
SEQRES  28 F  589  SER GLU VAL THR VAL TYR GLY ASP ASP ILE ILE LEU PRO          
SEQRES  29 F  589  SER CYS ALA VAL PRO ALA LEU ARG GLU VAL PHE LYS TYR          
SEQRES  30 F  589  VAL GLY PHE THR THR ASN THR LYS LYS THR PHE SER GLU          
SEQRES  31 F  589  GLY PRO PHE ARG GLU SER CYS GLY LYS HIS TYR TYR SER          
SEQRES  32 F  589  GLY VAL ASP VAL THR PRO PHE TYR ILE ARG HIS ARG ILE          
SEQRES  33 F  589  VAL SER PRO ALA ASP LEU ILE LEU VAL LEU ASN ASN LEU          
SEQRES  34 F  589  TYR ARG TRP ALA THR ILE ASP GLY VAL TRP ASP PRO ARG          
SEQRES  35 F  589  ALA HIS SER VAL TYR LEU LYS TYR ARG LYS LEU LEU PRO          
SEQRES  36 F  589  LYS GLN LEU GLN ARG ASN THR ILE PRO ASP GLY TYR GLY          
SEQRES  37 F  589  ASP GLY ALA LEU VAL GLY SER VAL LEU ILE ASN PRO PHE          
SEQRES  38 F  589  ALA LYS ASN ARG GLY TRP ILE ARG TYR VAL PRO VAL ILE          
SEQRES  39 F  589  THR ASP HIS THR ARG ASP ARG GLU ARG ALA GLU LEU GLY          
SEQRES  40 F  589  SER TYR LEU TYR ASP LEU PHE SER ARG CYS LEU SER GLU          
SEQRES  41 F  589  SER ASN ASP GLY LEU PRO LEU ARG GLY PRO SER GLY CYS          
SEQRES  42 F  589  ASP SER ALA ASP LEU PHE ALA ILE ASP GLN LEU ILE CYS          
SEQRES  43 F  589  ARG SER ASN PRO THR LYS ILE SER ARG SER THR GLY LYS          
SEQRES  44 F  589  PHE ASP ILE GLN TYR ILE ALA CYS SER SER ARG VAL LEU          
SEQRES  45 F  589  ALA PRO TYR GLY VAL PHE GLN GLY THR LYS VAL ALA SER          
SEQRES  46 F  589  LEU HIS GLU ALA                                              
HET    PXN  A1394      25                                                       
HET    PXN  C1394      25                                                       
HETNAM     PXN (2S)-1-[3-{[(2R)-2-HYDROXYPROPYL]OXY}-2,2-BIS({[(2R)-2-          
HETNAM   2 PXN  HYDROXYPROPYL]OXY}METHYL)PROPOXY]PROPAN-2-OL                    
HETSYN     PXN PENTAERYTHRITOL PROPOXYLATE (5/4 PO/OH)                          
FORMUL   5  PXN    2(C17 H36 O8)                                                
FORMUL   7  HOH   *925(H2 O)                                                    
HELIX    1   1 THR A    4  GLY A   16  1                                  13    
HELIX    2   2 GLY A   18  LEU A   26  1                                   9    
HELIX    3   3 ASP A   32  ALA A   52  1                                  21    
HELIX    4   4 THR A   79  ASP A   85  1                                   7    
HELIX    5   5 ASP A   85  GLY A  102  1                                  18    
HELIX    6   6 ASP A  106  GLY A  126  1                                  21    
HELIX    7   7 ASP A  161  LYS A  176  1                                  16    
HELIX    8   8 LYS A  181  VAL A  185  5                                   5    
HELIX    9   9 LYS A  192  MET A  202  1                                  11    
HELIX   10  10 PRO A  207  VAL A  226  1                                  20    
HELIX   11  11 SER A  227  GLY A  230  5                                   4    
HELIX   12  12 VAL A  241  HIS A  248  1                                   8    
HELIX   13  13 ASP A  270  SER A  282  1                                  13    
HELIX   14  14 GLY A 1023  GLY A 1040  1                                  18    
HELIX   15  15 GLY A 1083  THR A 1093  1                                  11    
HELIX   16  16 GLN A 1114  VAL A 1125  1                                  12    
HELIX   17  17 LYS A 1136  VAL A 1140  5                                   5    
HELIX   18  18 ASP A 1142  TYR A 1160  1                                  19    
HELIX   19  19 PRO A 1163  THR A 1167  5                                   5    
HELIX   20  20 SER A 1173  GLY A 1180  1                                   8    
HELIX   21  21 ASP A 1181  ILE A 1199  1                                  19    
HELIX   22  22 ARG A 1204  LYS A 1208  5                                   5    
HELIX   23  23 LYS A 1282  ILE A 1286  5                                   5    
HELIX   24  24 SER G   10  ASN G   20  1                                  11    
HELIX   25  25 ASN G   28  TYR G   41  1                                  14    
HELIX   26  26 SER G   48  SER G   54  1                                   7    
HELIX   27  27 THR G   62  MET G   76  1                                  15    
HELIX   28  28 ASP G   87  TYR G  111  1                                  25    
HELIX   29  29 SER G  122  GLY G  140  1                                  19    
HELIX   30  30 SER G  144  CYS G  152  1                                   9    
HELIX   31  31 ASN G  163  GLY G  167  5                                   5    
HELIX   32  32 HIS G  168  LEU G  175  1                                   8    
HELIX   33  33 THR G  180  ARG G  182  5                                   3    
HELIX   34  34 ALA G  183  SER G  193  1                                  11    
HELIX   35  35 PRO G  226  ARG G  245  1                                  20    
HELIX   36  36 CYS G  246  GLY G  248  5                                   3    
HELIX   37  37 GLN G  254  ASN G  268  1                                  15    
HELIX   38  38 ALA G  277  SER G  281  5                                   5    
HELIX   39  39 SER G  283  LEU G  291  1                                   9    
HELIX   40  40 PRO G  292  ARG G  303  1                                  12    
HELIX   41  41 TYR G  327  ASP G  348  1                                  22    
HELIX   42  42 ASP G  350  VAL G  354  5                                   5    
HELIX   43  43 ALA G  367  VAL G  378  1                                  12    
HELIX   44  44 ASN G  383  THR G  387  5                                   5    
HELIX   45  45 SER G  418  ALA G  433  1                                  16    
HELIX   46  46 ASP G  440  LYS G  452  1                                  13    
HELIX   47  47 PRO G  455  ASN G  461  1                                   7    
HELIX   48  48 SER G  475  ASN G  479  5                                   5    
HELIX   49  49 ALA G  504  LEU G  518  1                                  15    
HELIX   50  50 SER G  535  GLN G  543  1                                   9    
HELIX   51  51 THR C    4  GLY C   16  1                                  13    
HELIX   52  52 GLY C   18  LEU C   26  1                                   9    
HELIX   53  53 ASP C   32  ALA C   52  1                                  21    
HELIX   54  54 THR C   79  ASP C   85  1                                   7    
HELIX   55  55 ASP C   85  GLY C  102  1                                  18    
HELIX   56  56 ASP C  106  GLY C  126  1                                  21    
HELIX   57  57 ASP C  161  LYS C  176  1                                  16    
HELIX   58  58 LYS C  181  VAL C  185  5                                   5    
HELIX   59  59 LYS C  192  MET C  202  1                                  11    
HELIX   60  60 PRO C  207  VAL C  226  1                                  20    
HELIX   61  61 VAL C  241  HIS C  248  1                                   8    
HELIX   62  62 ASP C  270  SER C  282  1                                  13    
HELIX   63  63 GLY C 1023  GLY C 1040  1                                  18    
HELIX   64  64 GLY C 1083  THR C 1093  1                                  11    
HELIX   65  65 GLN C 1114  VAL C 1125  1                                  12    
HELIX   66  66 LYS C 1136  VAL C 1140  5                                   5    
HELIX   67  67 ASP C 1142  TYR C 1160  1                                  19    
HELIX   68  68 PRO C 1163  THR C 1167  5                                   5    
HELIX   69  69 SER C 1173  GLY C 1180  1                                   8    
HELIX   70  70 ASP C 1181  ILE C 1199  1                                  19    
HELIX   71  71 ARG C 1204  LYS C 1208  5                                   5    
HELIX   72  72 LYS C 1282  ILE C 1286  5                                   5    
HELIX   73  73 SER F   10  ASN F   20  1                                  11    
HELIX   74  74 ASN F   28  TYR F   41  1                                  14    
HELIX   75  75 SER F   48  SER F   54  1                                   7    
HELIX   76  76 THR F   62  ILE F   75  1                                  14    
HELIX   77  77 ASP F   87  TYR F  111  1                                  25    
HELIX   78  78 SER F  122  GLY F  140  1                                  19    
HELIX   79  79 SER F  144  CYS F  152  1                                   9    
HELIX   80  80 ASN F  163  GLY F  167  5                                   5    
HELIX   81  81 HIS F  168  LEU F  175  1                                   8    
HELIX   82  82 ALA F  183  SER F  193  1                                  11    
HELIX   83  83 PRO F  226  ARG F  245  1                                  20    
HELIX   84  84 CYS F  246  GLY F  248  5                                   3    
HELIX   85  85 GLN F  254  ASN F  268  1                                  15    
HELIX   86  86 ALA F  277  SER F  281  5                                   5    
HELIX   87  87 SER F  283  LEU F  291  1                                   9    
HELIX   88  88 PRO F  292  ARG F  303  1                                  12    
HELIX   89  89 TYR F  327  ASP F  348  1                                  22    
HELIX   90  90 ASP F  350  VAL F  354  5                                   5    
HELIX   91  91 ALA F  367  VAL F  378  1                                  12    
HELIX   92  92 ASN F  383  THR F  387  5                                   5    
HELIX   93  93 SER F  418  ALA F  433  1                                  16    
HELIX   94  94 ASP F  440  LYS F  452  1                                  13    
HELIX   95  95 PRO F  455  ASN F  461  1                                   7    
HELIX   96  96 SER F  475  ASN F  479  5                                   5    
HELIX   97  97 ALA F  504  LEU F  518  1                                  15    
HELIX   98  98 SER F  535  GLN F  543  1                                   9    
SHEET    1   A 3 ASP A  58  ASP A  66  0                                        
SHEET    2   A 3 TYR A  69  CYS A  77 -1  O  LEU A  73   N  LYS A  62           
SHEET    3   A 3 ASN A 130  GLU A 138 -1  O  ASN A 130   N  ASN A  76           
SHEET    1   B 3 VAL A 141  HIS A 147  0                                        
SHEET    2   B 3 ILE A 151  LYS A 158 -1  O  ILE A 151   N  HIS A 147           
SHEET    3   B 3 GLU A 251  GLU A 259 -1  O  PHE A 258   N  GLY A 152           
SHEET    1   C 2 PRO A 232  PHE A 233  0                                        
SHEET    2   C 2 GLU A 236  THR A 240 -1  O  LYS A 239   N  PHE A 233           
SHEET    1   D 6 VAL A1067  ASP A1070  0                                        
SHEET    2   D 6 HIS A1075  ASP A1080 -1  O  HIS A1078   N  VAL A1067           
SHEET    3   D 6 HIS A1011  GLY A1018  1  N  VAL A1014   O  ALA A1077           
SHEET    4   D 6 GLY A1100  ALA A1106  1  O  ILE A1102   N  GLY A1015           
SHEET    5   D 6 ILE A1130  ASN A1135  1  O  ILE A1131   N  ALA A1101           
SHEET    6   D 6 ILE A1169  ARG A1171  1  O  VAL A1170   N  LEU A1134           
SHEET    1   E 7 LEU A1211  PRO A1213  0                                        
SHEET    2   E 7 VAL A1291  ALA A1293 -1  O  LEU A1292   N  LEU A1212           
SHEET    3   E 7 GLU A1241  VAL A1245 -1  N  GLU A1243   O  ALA A1293           
SHEET    4   E 7 GLN A1251  GLU A1259 -1  O  GLN A1251   N  ILE A1244           
SHEET    5   E 7 ASN A1273  LEU A1278 -1  O  GLY A1275   N  GLU A1259           
SHEET    6   E 7 GLY A1224  ARG A1230 -1  N  VAL A1227   O  VAL A1276           
SHEET    7   E 7 ASP A1216  ILE A1220 -1  N  ILE A1220   O  GLY A1224           
SHEET    1   F 5 LEU A1211  PRO A1213  0                                        
SHEET    2   F 5 VAL A1291  ALA A1293 -1  O  LEU A1292   N  LEU A1212           
SHEET    3   F 5 GLU A1241  VAL A1245 -1  N  GLU A1243   O  ALA A1293           
SHEET    4   F 5 GLN A1251  GLU A1259 -1  O  GLN A1251   N  ILE A1244           
SHEET    5   F 5 LEU A1264  LEU A1265 -1  O  LEU A1265   N  VAL A1258           
SHEET    1   G 2 ILE A1235  LYS A1237  0                                        
SHEET    2   G 2 GLU A1267  ARG A1269 -1  O  GLY A1268   N  ILE A1236           
SHEET    1   H 7 PRO A1300  ILE A1310  0                                        
SHEET    2   H 7 ASN A1355  ALA A1367 -1  O  LEU A1362   N  THR A1302           
SHEET    3   H 7 THR A1335  GLU A1342 -1  N  THR A1338   O  ILE A1363           
SHEET    4   H 7 GLN A1329  PHE A1332 -1  N  PHE A1330   O  VAL A1337           
SHEET    5   H 7 ARG A1373  GLU A1378 -1  O  ARG A1377   N  GLN A1329           
SHEET    6   H 7 ARG A1381  VAL A1391 -1  O  GLY A1386   N  PHE A1374           
SHEET    7   H 7 PRO A1300  ILE A1310 -1  N  GLU A1305   O  LYS A1390           
SHEET    1   I 2 GLN G 177  CYS G 179  0                                        
SHEET    2   I 2 ILE G 200  ILE G 203  1  O  ASP G 202   N  CYS G 179           
SHEET    1   J 4 ARG G 220  ILE G 224  0                                        
SHEET    2   J 4 PHE G 206  VAL G 212 -1  N  VAL G 212   O  ARG G 220           
SHEET    3   J 4 LYS G 306  ARG G 308  1  O  ARG G 308   N  ALA G 209           
SHEET    4   J 4 VAL G 314  THR G 316 -1  O  VAL G 315   N  GLY G 307           
SHEET    1   K 3 LEU G 270  ASP G 274  0                                        
SHEET    2   K 3 ASP G 360  PRO G 364 -1  O  LEU G 363   N  ALA G 271           
SHEET    3   K 3 THR G 355  TYR G 357 -1  N  THR G 355   O  ILE G 362           
SHEET    1   L 3 PHE G 393  SER G 396  0                                        
SHEET    2   L 3 LYS G 399  TYR G 402 -1  O  TYR G 401   N  ARG G 394           
SHEET    3   L 3 VAL G 405  ASP G 406 -1  O  VAL G 405   N  TYR G 402           
SHEET    1   M 2 THR G 434  ILE G 435  0                                        
SHEET    2   M 2 VAL G 438  TRP G 439 -1  O  VAL G 438   N  ILE G 435           
SHEET    1   N 2 THR G 462  ILE G 463  0                                        
SHEET    2   N 2 LEU G 472  VAL G 473  1  O  LEU G 472   N  ILE G 463           
SHEET    1   O 3 LYS G 483  ARG G 485  0                                        
SHEET    2   O 3 ILE G 488  ARG G 501 -1  O  ILE G 488   N  ARG G 485           
SHEET    3   O 3 ILE G 553  CYS G 567 -1  O  ASP G 561   N  THR G 495           
SHEET    1   P 3 ASP C  58  ASP C  66  0                                        
SHEET    2   P 3 TYR C  69  CYS C  77 -1  O  LEU C  73   N  LYS C  62           
SHEET    3   P 3 ASN C 130  GLU C 138 -1  O  ASN C 130   N  ASN C  76           
SHEET    1   Q 3 VAL C 141  HIS C 147  0                                        
SHEET    2   Q 3 ILE C 151  LYS C 158 -1  O  VAL C 155   N  GLY C 143           
SHEET    3   Q 3 GLU C 251  GLU C 259 -1  O  PHE C 258   N  GLY C 152           
SHEET    1   R 2 PRO C 232  PHE C 233  0                                        
SHEET    2   R 2 GLU C 236  THR C 240 -1  O  LYS C 239   N  PHE C 233           
SHEET    1   S 6 VAL C1067  ASP C1070  0                                        
SHEET    2   S 6 HIS C1075  ASP C1080 -1  O  HIS C1078   N  VAL C1067           
SHEET    3   S 6 HIS C1011  GLY C1018  1  N  VAL C1014   O  ALA C1077           
SHEET    4   S 6 GLY C1100  ALA C1106  1  O  ILE C1102   N  GLY C1015           
SHEET    5   S 6 ILE C1130  ASN C1135  1  O  ILE C1131   N  ALA C1101           
SHEET    6   S 6 ILE C1169  ARG C1171  1  O  VAL C1170   N  LEU C1134           
SHEET    1   T 7 LEU C1211  PRO C1213  0                                        
SHEET    2   T 7 VAL C1291  ALA C1293 -1  O  LEU C1292   N  LEU C1212           
SHEET    3   T 7 GLU C1241  VAL C1245 -1  N  GLU C1243   O  ALA C1293           
SHEET    4   T 7 GLN C1251  GLU C1259 -1  O  GLN C1251   N  ILE C1244           
SHEET    5   T 7 ASN C1273  LEU C1278 -1  O  GLY C1275   N  GLU C1259           
SHEET    6   T 7 GLY C1224  ARG C1230 -1  N  VAL C1227   O  VAL C1276           
SHEET    7   T 7 ASP C1216  ILE C1220 -1  N  ILE C1220   O  GLY C1224           
SHEET    1   U 5 LEU C1211  PRO C1213  0                                        
SHEET    2   U 5 VAL C1291  ALA C1293 -1  O  LEU C1292   N  LEU C1212           
SHEET    3   U 5 GLU C1241  VAL C1245 -1  N  GLU C1243   O  ALA C1293           
SHEET    4   U 5 GLN C1251  GLU C1259 -1  O  GLN C1251   N  ILE C1244           
SHEET    5   U 5 LEU C1264  LEU C1265 -1  O  LEU C1265   N  VAL C1258           
SHEET    1   V 2 ILE C1235  LYS C1237  0                                        
SHEET    2   V 2 GLU C1267  ARG C1269 -1  O  GLY C1268   N  ILE C1236           
SHEET    1   W 7 PRO C1300  ILE C1310  0                                        
SHEET    2   W 7 ASN C1355  ALA C1367 -1  O  LEU C1362   N  THR C1302           
SHEET    3   W 7 THR C1335  GLU C1342 -1  N  THR C1338   O  ILE C1363           
SHEET    4   W 7 GLN C1329  PHE C1332 -1  N  PHE C1330   O  VAL C1337           
SHEET    5   W 7 ARG C1373  GLU C1378 -1  O  ARG C1377   N  GLN C1329           
SHEET    6   W 7 ARG C1381  VAL C1391 -1  O  GLY C1386   N  PHE C1374           
SHEET    7   W 7 PRO C1300  ILE C1310 -1  N  TYR C1309   O  ALA C1385           
SHEET    1   X 2 GLN F 177  CYS F 179  0                                        
SHEET    2   X 2 ILE F 200  ILE F 203  1  O  SER F 201   N  GLN F 177           
SHEET    1   Y 4 ARG F 220  ILE F 224  0                                        
SHEET    2   Y 4 PHE F 206  VAL F 212 -1  N  VAL F 212   O  ARG F 220           
SHEET    3   Y 4 LYS F 306  ARG F 308  1  O  ARG F 308   N  ALA F 209           
SHEET    4   Y 4 VAL F 314  THR F 316 -1  O  VAL F 315   N  GLY F 307           
SHEET    1   Z 3 LEU F 270  ASP F 274  0                                        
SHEET    2   Z 3 ASP F 360  PRO F 364 -1  O  LEU F 363   N  ALA F 271           
SHEET    3   Z 3 THR F 355  TYR F 357 -1  N  THR F 355   O  ILE F 362           
SHEET    1  AA 3 PHE F 393  SER F 396  0                                        
SHEET    2  AA 3 LYS F 399  TYR F 402 -1  O  TYR F 401   N  ARG F 394           
SHEET    3  AA 3 VAL F 405  ASP F 406 -1  O  VAL F 405   N  TYR F 402           
SHEET    1  AB 2 THR F 434  ILE F 435  0                                        
SHEET    2  AB 2 VAL F 438  TRP F 439 -1  O  VAL F 438   N  ILE F 435           
SHEET    1  AC 2 THR F 462  ILE F 463  0                                        
SHEET    2  AC 2 LEU F 472  VAL F 473  1  O  LEU F 472   N  ILE F 463           
SHEET    1  AD 3 LYS F 483  ARG F 485  0                                        
SHEET    2  AD 3 ILE F 488  ARG F 501 -1  O  ILE F 488   N  ARG F 485           
SHEET    3  AD 3 ILE F 553  CYS F 567 -1  O  ASP F 561   N  THR F 495           
SITE     1 AC1  7 HOH A 741  HOH A 887  ARG A1262  PRO G 143                    
SITE     2 AC1  7 MET G 148  TYR G 186  ALA G 189                               
SITE     1 AC2  4 ARG C1262  PRO F 143  MET F 148  TYR F 186                    
CRYST1  254.710  139.400  101.870  90.00  92.06  90.00 C 1 2 1       8          
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      0.003926  0.000000  0.000141        0.00000                         
SCALE2      0.000000  0.007174  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009823        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system