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Entry: 1GEH
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HEADER    LYASE                                   13-NOV-00   1GEH              
TITLE     CRYSTAL STRUCTURE OF ARCHAEAL RUBISCO (RIBULOSE 1,5-BISPHOSPHATE      
TITLE    2 CARBOXYLASE/OXYGENASE)                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE;           
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 EC: 4.1.1.39;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOCOCCUS KODAKARENSIS;                      
SOURCE   3 ORGANISM_TAXID: 69014;                                               
SOURCE   4 STRAIN: KOD1;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PENTAGONAL TOROID DECAMER, RUBISCO, LYASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.KITANO,N.MAEDA,T.FUKUI,H.ATOMI,T.IMANAKA,K.MIKI                     
REVDAT   4   13-JUL-11 1GEH    1       VERSN                                    
REVDAT   3   24-FEB-09 1GEH    1       VERSN                                    
REVDAT   2   21-JAN-03 1GEH    1       REMARK                                   
REVDAT   1   19-DEC-01 1GEH    0                                                
JRNL        AUTH   K.KITANO,N.MAEDA,T.FUKUI,H.ATOMI,T.IMANAKA,K.MIKI            
JRNL        TITL   CRYSTAL STRUCTURE OF A NOVEL-TYPE ARCHAEAL RUBISCO WITH      
JRNL        TITL 2 PENTAGONAL SYMMETRY                                          
JRNL        REF    STRUCTURE                     V.   9   473 2001              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   11435112                                                     
JRNL        DOI    10.1016/S0969-2126(01)00608-6                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   N.MAEDA,K.KITANO,T.FUKUI,S.EZAKI,H.ATOMI,K.MIKI,T.IMANAKA    
REMARK   1  TITL   RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE FROM             
REMARK   1  TITL 2 HYPERTHERMOPHILIC ARCHAEON PYROCOCCUS KODAKARAENSIS KOD1 IS  
REMARK   1  TITL 3 COMPOSED SOLELY OF LARGE SUBUNITS AND FORMS A PENTAGONAL     
REMARK   1  TITL 4 STRUCTURE                                                    
REMARK   1  REF    J.MOL.BIOL.                   V. 293    57 1999              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  DOI    10.1006/JMBI.1999.3145                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 11437229.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 64453                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 6530                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7222                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.10                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 16890                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.87                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 10.050; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 15.580; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 13.930; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 19.710; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1GEH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-NOV-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB005076.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL; NULL                         
REMARK 200  TEMPERATURE           (KELVIN) : 293.0; 293.0                       
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 5                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY; PHOTON FACTORY     
REMARK 200  BEAMLINE                       : BL-6A; BL-6B                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0; 1.0                           
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE; IMAGE PLATE           
REMARK 200  DETECTOR MANUFACTURER          : FUJI; FUJI                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64453                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.5                               
REMARK 200  DATA REDUNDANCY                : 12.100                             
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 65.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL                        
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMOINUM SULFATE, PH 9.0, VAPOR          
REMARK 280  DIFFUSION, TEMPERATURE 293K                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       31.08667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       62.17333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       62.17333            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       31.08667            
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 BIOLOGICAL ASSEMBLY IS A DECAMER GENERATED FROM THE      
REMARK 300 PENTAMER IN THE ASYMMETRIC UNIT BY THE OPERATIONS: Y, X, -Z.         
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: DECAMERIC                         
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 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     PHE A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     ILE A     8                                                      
REMARK 465     TYR A     9                                                      
REMARK 465     ASP A    10                                                      
REMARK 465     TYR A    11                                                      
REMARK 465     GLY A   319                                                      
REMARK 465     ALA A   320                                                      
REMARK 465     GLY A   321                                                      
REMARK 465     LYS A   322                                                      
REMARK 465     LEU A   323                                                      
REMARK 465     VAL A   444                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     LYS B     4                                                      
REMARK 465     PHE B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     ILE B     8                                                      
REMARK 465     TYR B     9                                                      
REMARK 465     ASP B    10                                                      
REMARK 465     TYR B    11                                                      
REMARK 465     GLY B   319                                                      
REMARK 465     ALA B   320                                                      
REMARK 465     GLY B   321                                                      
REMARK 465     LYS B   322                                                      
REMARK 465     LEU B   323                                                      
REMARK 465     VAL B   444                                                      
REMARK 465     MET C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     GLU C     3                                                      
REMARK 465     LYS C     4                                                      
REMARK 465     PHE C     5                                                      
REMARK 465     ASP C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     ILE C     8                                                      
REMARK 465     TYR C     9                                                      
REMARK 465     ASP C    10                                                      
REMARK 465     TYR C    11                                                      
REMARK 465     GLY C   319                                                      
REMARK 465     ALA C   320                                                      
REMARK 465     GLY C   321                                                      
REMARK 465     LYS C   322                                                      
REMARK 465     LEU C   323                                                      
REMARK 465     VAL C   444                                                      
REMARK 465     MET D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     GLU D     3                                                      
REMARK 465     LYS D     4                                                      
REMARK 465     PHE D     5                                                      
REMARK 465     ASP D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     ILE D     8                                                      
REMARK 465     TYR D     9                                                      
REMARK 465     ASP D    10                                                      
REMARK 465     TYR D    11                                                      
REMARK 465     GLY D   319                                                      
REMARK 465     ALA D   320                                                      
REMARK 465     GLY D   321                                                      
REMARK 465     LYS D   322                                                      
REMARK 465     LEU D   323                                                      
REMARK 465     VAL D   444                                                      
REMARK 465     MET E     1                                                      
REMARK 465     VAL E     2                                                      
REMARK 465     GLU E     3                                                      
REMARK 465     LYS E     4                                                      
REMARK 465     PHE E     5                                                      
REMARK 465     ASP E     6                                                      
REMARK 465     THR E     7                                                      
REMARK 465     ILE E     8                                                      
REMARK 465     TYR E     9                                                      
REMARK 465     ASP E    10                                                      
REMARK 465     TYR E    11                                                      
REMARK 465     GLY E   319                                                      
REMARK 465     ALA E   320                                                      
REMARK 465     GLY E   321                                                      
REMARK 465     LYS E   322                                                      
REMARK 465     LEU E   323                                                      
REMARK 465     VAL E   444                                                      
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    GLY A  16   N   -  CA  -  C   ANGL. DEV. = -18.1 DEGREES          
REMARK 500    GLY B  16   N   -  CA  -  C   ANGL. DEV. = -17.5 DEGREES          
REMARK 500    GLY C  16   N   -  CA  -  C   ANGL. DEV. = -17.9 DEGREES          
REMARK 500    GLY D  16   N   -  CA  -  C   ANGL. DEV. = -17.4 DEGREES          
REMARK 500    GLY E  16   N   -  CA  -  C   ANGL. DEV. = -17.9 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    LYS A  15     -142.77   -141.68                                   
REMARK 500    TYR A  17      154.66    -44.64                                   
REMARK 500    LYS A  21        6.07    -62.55                                   
REMARK 500    ALA A  34     -155.41    -77.30                                   
REMARK 500    GLU A  35      -92.88    -69.77                                   
REMARK 500    ALA A  42      -70.89    -77.13                                   
REMARK 500    SER A  51     -130.45   -155.13                                   
REMARK 500    THR A  52     -171.01    -64.07                                   
REMARK 500    THR A  56      104.26   -164.53                                   
REMARK 500    LEU A  58       49.27    -75.05                                   
REMARK 500    TYR A  59      111.84    158.74                                   
REMARK 500    ALA A  72     -167.24    -78.81                                   
REMARK 500    LYS A  73      124.52   -178.62                                   
REMARK 500    ALA A  99       57.69     39.36                                   
REMARK 500    SER A 107      -60.79    -97.80                                   
REMARK 500    ALA A 109       34.17   -157.41                                   
REMARK 500    ARG A 117        3.26    -53.89                                   
REMARK 500    LYS A 165      -35.87     50.86                                   
REMARK 500    THR A 195     -106.70    -93.69                                   
REMARK 500    ASN A 200       83.50   -168.06                                   
REMARK 500    ALA A 232     -176.02    165.42                                   
REMARK 500    LEU A 249     -177.69    -66.97                                   
REMARK 500    MET A 284      -14.97     94.09                                   
REMARK 500    ALA A 286      -13.57    -49.63                                   
REMARK 500    PRO A 344     -175.89    -59.87                                   
REMARK 500    TYR A 357     -121.92     54.29                                   
REMARK 500    GLN A 376      -70.40    -22.03                                   
REMARK 500    ILE A 379       12.53    -63.87                                   
REMARK 500    ILE A 415       -9.29    -54.36                                   
REMARK 500    ILE A 419      137.11    -24.12                                   
REMARK 500    THR A 427       -4.09     72.02                                   
REMARK 500    LYS A 437     -128.20    -79.00                                   
REMARK 500    TRP A 438       21.08    -70.53                                   
REMARK 500    VAL A 441      153.28    -38.46                                   
REMARK 500    LYS B  15     -141.65   -141.44                                   
REMARK 500    TYR B  17      154.62    -44.54                                   
REMARK 500    LYS B  21        6.64    -62.34                                   
REMARK 500    ALA B  34     -155.08    -77.12                                   
REMARK 500    GLU B  35      -92.44    -69.76                                   
REMARK 500    ALA B  42      -70.76    -77.74                                   
REMARK 500    SER B  51     -131.75   -156.62                                   
REMARK 500    THR B  52     -170.85    -63.04                                   
REMARK 500    THR B  56      104.41   -165.31                                   
REMARK 500    LEU B  58       49.45    -74.84                                   
REMARK 500    TYR B  59      112.09    159.05                                   
REMARK 500    ALA B  72     -166.54    -77.39                                   
REMARK 500    LYS B  73      123.84   -179.07                                   
REMARK 500    ALA B  99       57.07     39.13                                   
REMARK 500    SER B 107      -60.71    -97.79                                   
REMARK 500    ALA B 109       33.20   -156.46                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     170 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 445                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 446                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1445                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1446                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2445                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2446                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3445                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3446                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 4445                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 4446                
DBREF  1GEH A    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  1GEH B    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  1GEH C    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  1GEH D    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  1GEH E    1   444  UNP    O93627   RBL_PYRKO        1    444             
SEQRES   1 A  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 A  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 A  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 A  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 A  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 A  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 A  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 A  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 A  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 A  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 A  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 A  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 A  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 A  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 A  444  ASN GLY ALA ASP TYR MET LYS ASP ASP GLU ASN LEU THR          
SEQRES  16 A  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 A  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 A  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 A  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 A  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 A  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 A  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 A  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 A  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 A  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 A  444  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG          
SEQRES  27 A  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 A  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 A  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 A  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 A  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 A  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 A  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 A  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 A  444  PRO VAL                                                      
SEQRES   1 B  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 B  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 B  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 B  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 B  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 B  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 B  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 B  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 B  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 B  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 B  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 B  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 B  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 B  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 B  444  ASN GLY ALA ASP TYR MET LYS ASP ASP GLU ASN LEU THR          
SEQRES  16 B  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 B  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 B  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 B  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 B  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 B  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 B  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 B  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 B  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 B  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 B  444  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG          
SEQRES  27 B  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 B  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 B  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 B  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 B  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 B  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 B  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 B  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 B  444  PRO VAL                                                      
SEQRES   1 C  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 C  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 C  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 C  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 C  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 C  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 C  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 C  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 C  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 C  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 C  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 C  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 C  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 C  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 C  444  ASN GLY ALA ASP TYR MET LYS ASP ASP GLU ASN LEU THR          
SEQRES  16 C  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 C  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 C  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 C  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 C  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 C  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 C  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 C  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 C  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 C  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 C  444  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG          
SEQRES  27 C  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 C  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 C  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 C  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 C  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 C  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 C  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 C  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 C  444  PRO VAL                                                      
SEQRES   1 D  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 D  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 D  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 D  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 D  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 D  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 D  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 D  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 D  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 D  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 D  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 D  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 D  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 D  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 D  444  ASN GLY ALA ASP TYR MET LYS ASP ASP GLU ASN LEU THR          
SEQRES  16 D  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 D  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 D  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 D  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 D  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 D  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 D  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 D  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 D  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 D  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 D  444  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG          
SEQRES  27 D  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 D  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 D  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 D  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 D  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 D  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 D  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 D  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 D  444  PRO VAL                                                      
SEQRES   1 E  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 E  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 E  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 E  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 E  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 E  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 E  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 E  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 E  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 E  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 E  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 E  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 E  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 E  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 E  444  ASN GLY ALA ASP TYR MET LYS ASP ASP GLU ASN LEU THR          
SEQRES  16 E  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 E  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 E  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 E  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 E  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 E  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 E  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 E  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 E  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 E  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 E  444  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG          
SEQRES  27 E  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 E  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 E  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 E  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 E  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 E  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 E  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 E  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 E  444  PRO VAL                                                      
HET    SO4  A 445       5                                                       
HET    SO4  A 446       5                                                       
HET    SO4  B1445       5                                                       
HET    SO4  B1446       5                                                       
HET    SO4  C2445       5                                                       
HET    SO4  C2446       5                                                       
HET    SO4  D3445       5                                                       
HET    SO4  D3446       5                                                       
HET    SO4  E4445       5                                                       
HET    SO4  E4446       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   6  SO4    10(O4 S 2-)                                                  
HELIX    1   1 THR A   38  SER A   50  1                                  13    
HELIX    2   2 GLU A   63  SER A   71  1                                   9    
HELIX    3   3 HIS A   94  PHE A   96  5                                   3    
HELIX    4   4 ASN A  100  ALA A  109  1                                  10    
HELIX    5   5 GLY A  110  MET A  115  5                                   6    
HELIX    6   6 PRO A  129  ARG A  134  1                                   6    
HELIX    7   7 PHE A  141  GLU A  151  1                                  11    
HELIX    8   8 SER A  169  ASN A  183  1                                  15    
HELIX    9   9 ARG A  201  THR A  220  1                                  20    
HELIX   10  10 ASP A  233  GLY A  248  1                                  16    
HELIX   11  11 VAL A  256  TYR A  274  1                                  19    
HELIX   12  12 MET A  284  PHE A  288  5                                   5    
HELIX   13  13 SER A  297  GLY A  309  1                                  13    
HELIX   14  14 GLY A  325  GLU A  339  1                                  15    
HELIX   15  15 ASN A  374  LEU A  382  1                                   9    
HELIX   16  16 GLY A  391  GLY A  396  1                                   6    
HELIX   17  17 GLY A  400  MET A  416  1                                  17    
HELIX   18  18 PRO A  420  LYS A  426  1                                   7    
HELIX   19  19 HIS A  428  LYS A  437  1                                  10    
HELIX   20  20 THR B   38  SER B   50  1                                  13    
HELIX   21  21 GLU B   63  SER B   71  1                                   9    
HELIX   22  22 HIS B   94  PHE B   96  5                                   3    
HELIX   23  23 ASN B  100  ALA B  109  1                                  10    
HELIX   24  24 GLY B  110  MET B  115  5                                   6    
HELIX   25  25 PRO B  129  ARG B  134  1                                   6    
HELIX   26  26 PHE B  141  GLU B  151  1                                  11    
HELIX   27  27 SER B  169  ASN B  183  1                                  15    
HELIX   28  28 ARG B  201  THR B  220  1                                  20    
HELIX   29  29 ASP B  233  GLY B  248  1                                  16    
HELIX   30  30 VAL B  256  TYR B  274  1                                  19    
HELIX   31  31 MET B  284  PHE B  288  5                                   5    
HELIX   32  32 SER B  297  GLY B  309  1                                  13    
HELIX   33  33 GLY B  325  GLU B  339  1                                  15    
HELIX   34  34 ASN B  374  LEU B  382  1                                   9    
HELIX   35  35 GLY B  391  GLY B  396  1                                   6    
HELIX   36  36 GLY B  400  MET B  416  1                                  17    
HELIX   37  37 PRO B  420  LYS B  426  1                                   7    
HELIX   38  38 HIS B  428  LYS B  437  1                                  10    
HELIX   39  39 THR C   38  SER C   50  1                                  13    
HELIX   40  40 GLU C   63  SER C   71  1                                   9    
HELIX   41  41 HIS C   94  PHE C   96  5                                   3    
HELIX   42  42 ASN C  100  ALA C  109  1                                  10    
HELIX   43  43 GLY C  110  MET C  115  5                                   6    
HELIX   44  44 PRO C  129  ARG C  134  1                                   6    
HELIX   45  45 PHE C  141  GLU C  151  1                                  11    
HELIX   46  46 SER C  169  ASN C  183  1                                  15    
HELIX   47  47 ARG C  201  THR C  220  1                                  20    
HELIX   48  48 ASP C  233  GLY C  248  1                                  16    
HELIX   49  49 VAL C  256  TYR C  274  1                                  19    
HELIX   50  50 MET C  284  PHE C  288  5                                   5    
HELIX   51  51 SER C  297  GLY C  309  1                                  13    
HELIX   52  52 GLY C  325  GLU C  339  1                                  15    
HELIX   53  53 ASN C  374  LEU C  382  1                                   9    
HELIX   54  54 GLY C  391  GLY C  396  1                                   6    
HELIX   55  55 GLY C  400  MET C  416  1                                  17    
HELIX   56  56 PRO C  420  LYS C  426  1                                   7    
HELIX   57  57 HIS C  428  LYS C  437  1                                  10    
HELIX   58  58 THR D   38  SER D   50  1                                  13    
HELIX   59  59 GLU D   63  SER D   71  1                                   9    
HELIX   60  60 HIS D   94  PHE D   96  5                                   3    
HELIX   61  61 ASN D  100  ALA D  109  1                                  10    
HELIX   62  62 GLY D  110  MET D  115  5                                   6    
HELIX   63  63 PRO D  129  ARG D  134  1                                   6    
HELIX   64  64 PHE D  141  GLU D  151  1                                  11    
HELIX   65  65 SER D  169  ASN D  183  1                                  15    
HELIX   66  66 ARG D  201  THR D  220  1                                  20    
HELIX   67  67 ASP D  233  GLY D  248  1                                  16    
HELIX   68  68 VAL D  256  TYR D  274  1                                  19    
HELIX   69  69 HIS D  285  ARG D  290  1                                   6    
HELIX   70  70 SER D  297  GLY D  309  1                                  13    
HELIX   71  71 GLY D  325  GLU D  339  1                                  15    
HELIX   72  72 ASN D  374  LEU D  382  1                                   9    
HELIX   73  73 GLY D  391  GLY D  396  1                                   6    
HELIX   74  74 GLY D  400  MET D  416  1                                  17    
HELIX   75  75 PRO D  420  LYS D  426  1                                   7    
HELIX   76  76 HIS D  428  LYS D  437  1                                  10    
HELIX   77  77 THR E   38  SER E   50  1                                  13    
HELIX   78  78 GLU E   63  SER E   71  1                                   9    
HELIX   79  79 HIS E   94  PHE E   96  5                                   3    
HELIX   80  80 ASN E  100  ALA E  109  1                                  10    
HELIX   81  81 GLY E  110  MET E  115  5                                   6    
HELIX   82  82 PRO E  129  ARG E  134  1                                   6    
HELIX   83  83 PHE E  141  GLU E  151  1                                  11    
HELIX   84  84 SER E  169  ASN E  183  1                                  15    
HELIX   85  85 ARG E  201  THR E  220  1                                  20    
HELIX   86  86 ASP E  233  GLY E  248  1                                  16    
HELIX   87  87 VAL E  256  TYR E  274  1                                  19    
HELIX   88  88 HIS E  285  ARG E  290  1                                   6    
HELIX   89  89 SER E  297  GLY E  309  1                                  13    
HELIX   90  90 GLY E  325  GLU E  339  1                                  15    
HELIX   91  91 ASN E  374  LEU E  382  1                                   9    
HELIX   92  92 GLY E  391  GLY E  396  1                                   6    
HELIX   93  93 GLY E  400  MET E  416  1                                  17    
HELIX   94  94 PRO E  420  LYS E  426  1                                   7    
HELIX   95  95 HIS E  428  LYS E  437  1                                  10    
SHEET    1   A 4 LYS A  73  ASP A  76  0                                        
SHEET    2   A 4 TRP A  85  PRO A  92 -1  O  ARG A  88   N  TYR A  75           
SHEET    3   A 4 ASP A  24  PRO A  33 -1  N  ILE A  25   O  TYR A  91           
SHEET    4   A 4 VAL A 118  GLY A 120 -1  N  LYS A 119   O  THR A  32           
SHEET    1   B 5 LYS A  73  ASP A  76  0                                        
SHEET    2   B 5 TRP A  85  PRO A  92 -1  O  ARG A  88   N  TYR A  75           
SHEET    3   B 5 ASP A  24  PRO A  33 -1  N  ILE A  25   O  TYR A  91           
SHEET    4   B 5 ARG A 122  TYR A 127 -1  O  ARG A 122   N  ARG A  30           
SHEET    5   B 5 GLY A 295  ILE A 296  1  O  GLY A 295   N  LEU A 123           
SHEET    1   C 8 THR A 225  PHE A 227  0                                        
SHEET    2   C 8 TYR A 187  LYS A 189  1  O  MET A 188   N  PHE A 227           
SHEET    3   C 8 ILE A 157  VAL A 160  1  O  TYR A 158   N  TYR A 187           
SHEET    4   C 8 VAL A 387  GLN A 389  1  N  LEU A 388   O  ILE A 157           
SHEET    5   C 8 PHE A 363  SER A 367  1  O  PRO A 364   N  VAL A 387           
SHEET    6   C 8 GLN A 312  HIS A 314  1  O  LEU A 313   N  THR A 365           
SHEET    7   C 8 ALA A 277  HIS A 281  1  O  ILE A 278   N  GLN A 312           
SHEET    8   C 8 HIS A 251  ASP A 255  1  O  ALA A 252   N  HIS A 279           
SHEET    1   D 2 HIS A 341  TYR A 342  0                                        
SHEET    2   D 2 GLN A 354  LYS A 355 -1  O  GLN A 354   N  TYR A 342           
SHEET    1   E 4 LYS B  73  ASP B  76  0                                        
SHEET    2   E 4 TRP B  85  PRO B  92 -1  O  ARG B  88   N  TYR B  75           
SHEET    3   E 4 ASP B  24  PRO B  33 -1  N  ILE B  25   O  TYR B  91           
SHEET    4   E 4 VAL B 118  GLY B 120 -1  N  LYS B 119   O  THR B  32           
SHEET    1   F 5 LYS B  73  ASP B  76  0                                        
SHEET    2   F 5 TRP B  85  PRO B  92 -1  O  ARG B  88   N  TYR B  75           
SHEET    3   F 5 ASP B  24  PRO B  33 -1  N  ILE B  25   O  TYR B  91           
SHEET    4   F 5 ARG B 122  TYR B 127 -1  O  ARG B 122   N  ARG B  30           
SHEET    5   F 5 GLY B 295  ILE B 296  1  O  GLY B 295   N  LEU B 123           
SHEET    1   G 8 THR B 225  PHE B 227  0                                        
SHEET    2   G 8 TYR B 187  LYS B 189  1  O  MET B 188   N  PHE B 227           
SHEET    3   G 8 ILE B 157  VAL B 160  1  O  TYR B 158   N  TYR B 187           
SHEET    4   G 8 VAL B 387  GLN B 389  1  N  LEU B 388   O  ILE B 157           
SHEET    5   G 8 PHE B 363  SER B 367  1  O  PRO B 364   N  VAL B 387           
SHEET    6   G 8 GLN B 312  HIS B 314  1  O  LEU B 313   N  THR B 365           
SHEET    7   G 8 ALA B 277  HIS B 281  1  O  ILE B 278   N  GLN B 312           
SHEET    8   G 8 HIS B 251  ASP B 255  1  O  ALA B 252   N  HIS B 279           
SHEET    1   H 2 HIS B 341  TYR B 342  0                                        
SHEET    2   H 2 GLN B 354  LYS B 355 -1  O  GLN B 354   N  TYR B 342           
SHEET    1   I 4 LYS C  73  ASP C  76  0                                        
SHEET    2   I 4 TRP C  85  PRO C  92 -1  O  ARG C  88   N  TYR C  75           
SHEET    3   I 4 ASP C  24  PRO C  33 -1  N  ILE C  25   O  TYR C  91           
SHEET    4   I 4 VAL C 118  GLY C 120 -1  N  LYS C 119   O  THR C  32           
SHEET    1   J 5 LYS C  73  ASP C  76  0                                        
SHEET    2   J 5 TRP C  85  PRO C  92 -1  O  ARG C  88   N  TYR C  75           
SHEET    3   J 5 ASP C  24  PRO C  33 -1  N  ILE C  25   O  TYR C  91           
SHEET    4   J 5 ARG C 122  TYR C 127 -1  O  ARG C 122   N  ARG C  30           
SHEET    5   J 5 GLY C 295  ILE C 296  1  O  GLY C 295   N  LEU C 123           
SHEET    1   K 8 THR C 225  PHE C 227  0                                        
SHEET    2   K 8 TYR C 187  LYS C 189  1  O  MET C 188   N  PHE C 227           
SHEET    3   K 8 ILE C 157  VAL C 160  1  O  TYR C 158   N  TYR C 187           
SHEET    4   K 8 VAL C 387  GLN C 389  1  N  LEU C 388   O  ILE C 157           
SHEET    5   K 8 PHE C 363  SER C 367  1  O  PRO C 364   N  VAL C 387           
SHEET    6   K 8 GLN C 312  HIS C 314  1  O  LEU C 313   N  THR C 365           
SHEET    7   K 8 ALA C 277  HIS C 281  1  O  ILE C 278   N  GLN C 312           
SHEET    8   K 8 HIS C 251  ASP C 255  1  O  ALA C 252   N  HIS C 279           
SHEET    1   L 2 HIS C 341  TYR C 342  0                                        
SHEET    2   L 2 GLN C 354  LYS C 355 -1  O  GLN C 354   N  TYR C 342           
SHEET    1   M 4 LYS D  73  ASP D  76  0                                        
SHEET    2   M 4 TRP D  85  PRO D  92 -1  O  ARG D  88   N  TYR D  75           
SHEET    3   M 4 ASP D  24  PRO D  33 -1  N  ILE D  25   O  TYR D  91           
SHEET    4   M 4 VAL D 118  GLY D 120 -1  N  LYS D 119   O  THR D  32           
SHEET    1   N 5 LYS D  73  ASP D  76  0                                        
SHEET    2   N 5 TRP D  85  PRO D  92 -1  O  ARG D  88   N  TYR D  75           
SHEET    3   N 5 ASP D  24  PRO D  33 -1  N  ILE D  25   O  TYR D  91           
SHEET    4   N 5 ARG D 122  TYR D 127 -1  O  ARG D 122   N  ARG D  30           
SHEET    5   N 5 GLY D 295  ILE D 296  1  O  GLY D 295   N  LEU D 123           
SHEET    1   O 8 THR D 225  PHE D 227  0                                        
SHEET    2   O 8 TYR D 187  LYS D 189  1  O  MET D 188   N  PHE D 227           
SHEET    3   O 8 ILE D 157  VAL D 160  1  O  TYR D 158   N  TYR D 187           
SHEET    4   O 8 VAL D 387  GLN D 389  1  N  LEU D 388   O  ILE D 157           
SHEET    5   O 8 PHE D 363  SER D 367  1  O  PRO D 364   N  VAL D 387           
SHEET    6   O 8 GLN D 312  HIS D 314  1  O  LEU D 313   N  THR D 365           
SHEET    7   O 8 ALA D 277  HIS D 281  1  O  ILE D 278   N  GLN D 312           
SHEET    8   O 8 HIS D 251  ASP D 255  1  O  ALA D 252   N  HIS D 279           
SHEET    1   P 2 HIS D 341  TYR D 342  0                                        
SHEET    2   P 2 GLN D 354  LYS D 355 -1  O  GLN D 354   N  TYR D 342           
SHEET    1   Q 4 LYS E  73  ASP E  76  0                                        
SHEET    2   Q 4 TRP E  85  PRO E  92 -1  O  ARG E  88   N  TYR E  75           
SHEET    3   Q 4 ASP E  24  PRO E  33 -1  N  ILE E  25   O  TYR E  91           
SHEET    4   Q 4 VAL E 118  GLY E 120 -1  N  LYS E 119   O  THR E  32           
SHEET    1   R 5 LYS E  73  ASP E  76  0                                        
SHEET    2   R 5 TRP E  85  PRO E  92 -1  O  ARG E  88   N  TYR E  75           
SHEET    3   R 5 ASP E  24  PRO E  33 -1  N  ILE E  25   O  TYR E  91           
SHEET    4   R 5 ARG E 122  TYR E 127 -1  O  ARG E 122   N  ARG E  30           
SHEET    5   R 5 GLY E 295  ILE E 296  1  O  GLY E 295   N  LEU E 123           
SHEET    1   S 8 THR E 225  PHE E 227  0                                        
SHEET    2   S 8 TYR E 187  LYS E 189  1  O  MET E 188   N  PHE E 227           
SHEET    3   S 8 ILE E 157  VAL E 160  1  O  TYR E 158   N  TYR E 187           
SHEET    4   S 8 VAL E 387  GLN E 389  1  N  LEU E 388   O  ILE E 157           
SHEET    5   S 8 PHE E 363  SER E 367  1  O  PRO E 364   N  VAL E 387           
SHEET    6   S 8 GLN E 312  HIS E 314  1  O  LEU E 313   N  THR E 365           
SHEET    7   S 8 ALA E 277  HIS E 281  1  O  ILE E 278   N  GLN E 312           
SHEET    8   S 8 HIS E 251  ASP E 255  1  O  ALA E 252   N  HIS E 279           
SHEET    1   T 2 HIS E 341  TYR E 342  0                                        
SHEET    2   T 2 GLN E 354  LYS E 355 -1  O  GLN E 354   N  TYR E 342           
SITE     1 AC1  5 LYS A 163  GLY A 369  GLN A 389  GLY A 391                    
SITE     2 AC1  5 GLY A 392                                                     
SITE     1 AC2  2 ARG A 282  HIS A 314                                          
SITE     1 AC3  5 LYS B 163  GLY B 369  GLN B 389  GLY B 391                    
SITE     2 AC3  5 GLY B 392                                                     
SITE     1 AC4  2 ARG B 282  HIS B 314                                          
SITE     1 AC5  5 LYS C 163  GLY C 369  GLN C 389  GLY C 391                    
SITE     2 AC5  5 GLY C 392                                                     
SITE     1 AC6  2 ARG C 282  HIS C 314                                          
SITE     1 AC7  5 LYS D 163  GLY D 369  GLN D 389  GLY D 391                    
SITE     2 AC7  5 GLY D 392                                                     
SITE     1 AC8  2 ARG D 282  HIS D 314                                          
SITE     1 AC9  5 LYS E 163  GLY E 369  GLN E 389  GLY E 391                    
SITE     2 AC9  5 GLY E 392                                                     
SITE     1 BC1  2 ARG E 282  HIS E 314                                          
CRYST1  233.750  233.750   93.260  90.00  90.00 120.00 P 31 2 1     30          
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      0.004278  0.002470  0.000000        0.00000                         
SCALE2      0.000000  0.004940  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010723        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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