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Database: PDB
Entry: 1GK8
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Original site: 1GK8 
HEADER    LYASE                                   09-AUG-01   1GK8              
TITLE     RUBISCO FROM CHLAMYDOMONAS REINHARDTII                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE-1,5 BISPHOSPHATE CARBOXYLASE LARGE                
COMPND   3  CHAIN;                                                              
COMPND   4 CHAIN: A, C, E, G;                                                   
COMPND   5 SYNONYM: RUBISCO LARGE SUBUNIT;                                      
COMPND   6 EC: 4.1.1.39;                                                        
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1;           
COMPND   9 CHAIN: I, K, M, O;                                                   
COMPND  10 SYNONYM: RUBISCO SMALL SUBUNIT 1;                                    
COMPND  11 EC: 4.1.1.39                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;                      
SOURCE   3 ORGANISM_TAXID: 3055;                                                
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;                      
SOURCE   6 ORGANISM_TAXID: 3055                                                 
KEYWDS    LYASE, RUBISCO, PHOTOSYNTHESIS                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.C.TAYLOR,R.J.SPREITZER,I.ANDERSSON                                  
REVDAT   4   24-FEB-09 1GK8    1       VERSN                                    
REVDAT   3   05-APR-05 1GK8    1       JRNL                                     
REVDAT   2   01-AUG-03 1GK8    1       COMPND SOURCE MODRES CRYST1              
REVDAT   1   24-OCT-01 1GK8    0                                                
JRNL        AUTH   T.C.TAYLOR,A.BACKLUND,K.BJORHALL,                            
JRNL        AUTH 2 R.J.SPREITZERI.ANDERSSON                                     
JRNL        TITL   FIRST CRYSTAL STRUCTURE OF RUBISCO FROM A GREEN              
JRNL        TITL 2 ALGA, CHLAMYDOMONAS REINHARDTII                              
JRNL        REF    J.BIOL.CHEM.                  V. 276 48159 2001              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   11641402                                                     
JRNL        DOI    10.1074/JBC.M107765200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.4  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.4                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20                             
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97                             
REMARK   3   NUMBER OF REFLECTIONS             : 467822                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.149                           
REMARK   3   R VALUE            (WORKING SET) : 0.149                           
REMARK   3   FREE R VALUE                     : 0.162                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 23546                           
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18662                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 424                                     
REMARK   3   SOLVENT ATOMS            : 2556                                    
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) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.05          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.38          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.7           
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: CONTRIBUTION FOR RIDING HYDROGENS         
REMARK   3  ADDED DURING LAST CYCLE. THE SMALL SUBUNIT C TERMINUS IS            
REMARK   3  DISORDERED BEYOND RESIDUE 126. THE LARGE SUBUNIT N-TERMINI ARE      
REMARK   3  DISORDERED.                                                         
REMARK   4                                                                      
REMARK   4 1GK8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-OCT-01.                  
REMARK 100 THE PDBE ID CODE IS EBI-8442.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.931                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 469880                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 8RUC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): NULL                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM HEPES PH 7.5, 8-12% PEG 4000,      
REMARK 280  50 MM NAHCO3, 5 MM MGCL2, 50 UM 2-CABP, 18 DEG C, 10-15 MG/ML       
REMARK 280  PROTEIN                                                             
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       85.68750            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       71.31900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       85.68750            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       71.31900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: HEXADECAMERIC                     
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC              
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, G, I, O, E, K, M                
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  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     PRO A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     MET C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     PRO C     3                                                      
REMARK 465     GLN C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     GLU C     6                                                      
REMARK 465     MET E     1                                                      
REMARK 465     VAL E     2                                                      
REMARK 465     PRO E     3                                                      
REMARK 465     GLN E     4                                                      
REMARK 465     THR E     5                                                      
REMARK 465     GLU E     6                                                      
REMARK 465     THR E     7                                                      
REMARK 465     LYS E     8                                                      
REMARK 465     ALA E     9                                                      
REMARK 465     GLY E    10                                                      
REMARK 465     MET G     1                                                      
REMARK 465     VAL G     2                                                      
REMARK 465     PRO G     3                                                      
REMARK 465     GLN G     4                                                      
REMARK 465     THR G     5                                                      
REMARK 465     GLU G     6                                                      
REMARK 465     THR G     7                                                      
REMARK 465     LYS G     8                                                      
REMARK 465     LYS I   127                                                      
REMARK 465     THR I   128                                                      
REMARK 465     ALA I   129                                                      
REMARK 465     ARG I   130                                                      
REMARK 465     ASP I   131                                                      
REMARK 465     PHE I   132                                                      
REMARK 465     GLN I   133                                                      
REMARK 465     PRO I   134                                                      
REMARK 465     ALA I   135                                                      
REMARK 465     ASN I   136                                                      
REMARK 465     LYS I   137                                                      
REMARK 465     ARG I   138                                                      
REMARK 465     SER I   139                                                      
REMARK 465     VAL I   140                                                      
REMARK 465     LYS K   127                                                      
REMARK 465     THR K   128                                                      
REMARK 465     ALA K   129                                                      
REMARK 465     ARG K   130                                                      
REMARK 465     ASP K   131                                                      
REMARK 465     PHE K   132                                                      
REMARK 465     GLN K   133                                                      
REMARK 465     PRO K   134                                                      
REMARK 465     ALA K   135                                                      
REMARK 465     ASN K   136                                                      
REMARK 465     LYS K   137                                                      
REMARK 465     ARG K   138                                                      
REMARK 465     SER K   139                                                      
REMARK 465     VAL K   140                                                      
REMARK 465     LYS M   127                                                      
REMARK 465     THR M   128                                                      
REMARK 465     ALA M   129                                                      
REMARK 465     ARG M   130                                                      
REMARK 465     ASP M   131                                                      
REMARK 465     PHE M   132                                                      
REMARK 465     GLN M   133                                                      
REMARK 465     PRO M   134                                                      
REMARK 465     ALA M   135                                                      
REMARK 465     ASN M   136                                                      
REMARK 465     LYS M   137                                                      
REMARK 465     ARG M   138                                                      
REMARK 465     SER M   139                                                      
REMARK 465     VAL M   140                                                      
REMARK 465     LYS O   127                                                      
REMARK 465     THR O   128                                                      
REMARK 465     ALA O   129                                                      
REMARK 465     ARG O   130                                                      
REMARK 465     ASP O   131                                                      
REMARK 465     PHE O   132                                                      
REMARK 465     GLN O   133                                                      
REMARK 465     PRO O   134                                                      
REMARK 465     ALA O   135                                                      
REMARK 465     ASN O   136                                                      
REMARK 465     LYS O   137                                                      
REMARK 465     ARG O   138                                                      
REMARK 465     SER O   139                                                      
REMARK 465     VAL O   140                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH G  2084  -  O    HOH G  2087              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500                                                                      
REMARK 500   CD1  LEU E    22     O    HOH G  2087     4455      1.90           
REMARK 500   O    HOH G  2087     CD1  LEU E    22     4445      1.90           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 217   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    TYR A 239   CB  -  CG  -  CD1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    TYR A 239   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG A 303   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    LYS C 175   CA  -  C   -  O   ANGL. DEV. = -15.4 DEGREES          
REMARK 500    ARG C 187   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    TYR C 239   CB  -  CG  -  CD1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    TYR C 239   CB  -  CG  -  CD2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG C 339   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    CYS C 449   CA  -  CB  -  SG  ANGL. DEV. =   6.7 DEGREES          
REMARK 500    LEU E  22   CB  -  CG  -  CD1 ANGL. DEV. = -11.2 DEGREES          
REMARK 500    ARG E 134   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    LYS E 175   CA  -  C   -  O   ANGL. DEV. = -12.8 DEGREES          
REMARK 500    ARG E 187   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG E 217   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    TYR E 239   CB  -  CG  -  CD1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    TYR E 239   CB  -  CG  -  CD2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG E 350   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG E 435   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    MET G  42   CA  -  CB  -  CG  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    LYS G 175   CA  -  C   -  O   ANGL. DEV. = -14.7 DEGREES          
REMARK 500    ARG G 187   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG G 217   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG G 303   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    CYS G 449   CA  -  CB  -  SG  ANGL. DEV. =   7.1 DEGREES          
REMARK 500    GLU K  55   CA  -  CB  -  CG  ANGL. DEV. =  13.2 DEGREES          
REMARK 500    ARG K  71   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    GLU O  55   CA  -  CB  -  CG  ANGL. DEV. =  22.4 DEGREES          
REMARK 500    ARG O  91   CD  -  NE  -  CZ  ANGL. DEV. =  11.4 DEGREES          
REMARK 500    ARG O  91   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG O  91   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG O 125   CD  -  NE  -  CZ  ANGL. DEV. =  13.3 DEGREES          
REMARK 500    ARG O 125   NE  -  CZ  -  NH1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG O 125   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 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 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    SER A  62      -80.83   -141.52                                   
REMARK 500    THR A  65     -163.95   -129.71                                   
REMARK 500    THR A  75     -165.86   -124.36                                   
REMARK 500    CYS A 172      126.66   -175.67                                   
REMARK 500    PRO A 176      144.66    -27.55                                   
REMARK 500    ASN A 207      -92.44   -123.57                                   
REMARK 500    MET A 212      109.07   -167.38                                   
REMARK 500    MET A 297       -7.10     86.26                                   
REMARK 500    VAL A 331      -49.93     76.14                                   
REMARK 500    ASP A 357       92.23   -161.33                                   
REMARK 500    SER C  62      -81.02   -142.02                                   
REMARK 500    THR C  65     -165.08   -128.98                                   
REMARK 500    THR C  75     -168.83   -122.80                                   
REMARK 500    CYS C 172      122.74   -178.17                                   
REMARK 500    PRO C 176      143.52    -16.75                                   
REMARK 500    ASN C 207      -91.98   -121.95                                   
REMARK 500    MET C 212      110.74   -165.55                                   
REMARK 500    MET C 297       -9.05     87.75                                   
REMARK 500    VAL C 331      -50.25     73.42                                   
REMARK 500    ASP C 357       95.40   -162.86                                   
REMARK 500    SER E  62      -81.67   -143.06                                   
REMARK 500    THR E  75     -168.44   -123.63                                   
REMARK 500    CYS E 172      123.87   -176.50                                   
REMARK 500    PRO E 176      144.62    -21.34                                   
REMARK 500    ASN E 207      -92.68   -123.51                                   
REMARK 500    MET E 212      107.18   -166.99                                   
REMARK 500    MET E 297       -9.11     84.57                                   
REMARK 500    VAL E 331      -52.54     75.28                                   
REMARK 500    ASP E 357       92.58   -160.73                                   
REMARK 500    SER G  62      -79.52   -141.04                                   
REMARK 500    THR G  65     -164.50   -124.20                                   
REMARK 500    CYS G 172      122.51   -177.94                                   
REMARK 500    PRO G 176      141.91    -17.05                                   
REMARK 500    ASN G 207      -91.83   -122.63                                   
REMARK 500    MET G 212      108.58   -164.56                                   
REMARK 500    MET G 297       -9.12     87.82                                   
REMARK 500    VAL G 331      -50.79     73.57                                   
REMARK 500    ASP G 357       93.88   -161.22                                   
REMARK 500    GLU I  13     -141.43     63.57                                   
REMARK 500    PHE I  15        8.60     82.27                                   
REMARK 500    SER I  62       53.65    -91.96                                   
REMARK 500    LYS I  77     -123.39     55.83                                   
REMARK 500    GLU K  13     -141.07     66.58                                   
REMARK 500    PHE K  15        7.89     84.32                                   
REMARK 500    LYS K  77     -126.03     54.44                                   
REMARK 500    GLU M  13     -140.87     63.57                                   
REMARK 500    PHE M  15        7.60     83.14                                   
REMARK 500    SER M  62       52.67    -91.45                                   
REMARK 500    LYS M  77     -126.71     55.04                                   
REMARK 500    GLU O  13     -141.99     66.20                                   
REMARK 500    PHE O  15        8.68     83.51                                   
REMARK 500    LYS O  77     -125.84     56.14                                   
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 LYS A  175     PRO A  176                  -40.34                    
REMARK 500 LYS C  175     PRO C  176                  -58.70                    
REMARK 500 LYS E  175     PRO E  176                  -47.70                    
REMARK 500 LYS G  175     PRO G  176                  -56.62                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    LYS A 175        -13.11                                           
REMARK 500    LYS C 175        -22.08                                           
REMARK 500    LYS E 175        -13.01                                           
REMARK 500    LYS G 175        -21.39                                           
REMARK 500    ARG I 125         13.98                                           
REMARK 500    ARG M 125         12.33                                           
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 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 203   OD1                                                    
REMARK 620 2 GLU A 204   OE1  93.8                                              
REMARK 620 3 CAP A1477   O2  104.3 160.8                                        
REMARK 620 4 CAP A1477   O3  173.2  89.6  73.0                                  
REMARK 620 5 CAP A1477   O6   97.6  98.7  73.2  87.7                            
REMARK 620 6 KCX A 201   OQ2  88.6  93.2  93.3  85.3 166.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX C 201   OQ2                                                    
REMARK 620 2 ASP C 203   OD1  87.5                                              
REMARK 620 3 GLU C 204   OE1  93.2  93.1                                        
REMARK 620 4 CAP C1477   O2   93.7 104.5 161.3                                  
REMARK 620 5 CAP C1477   O3   86.5 173.4  89.8  73.3                            
REMARK 620 6 CAP C1477   O6  165.5  98.5  99.5  72.1  86.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX E 201   OQ2                                                    
REMARK 620 2 GLU E 204   OE1  92.3                                              
REMARK 620 3 CAP E1477   O3   86.6  89.4                                        
REMARK 620 4 ASP E 203   OD1  88.5  93.8 174.2                                  
REMARK 620 5 CAP E1477   O6  167.2  98.9  87.5  96.7                            
REMARK 620 6 CAP E1477   O2   94.5 160.5  72.9 104.6  72.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP G1477   O6                                                     
REMARK 620 2 KCX G 201   OQ2 167.5                                              
REMARK 620 3 ASP G 203   OD1  97.0  88.5                                        
REMARK 620 4 GLU G 204   OE1  99.1  91.7  93.4                                  
REMARK 620 5 CAP G1477   O2   73.6  94.2 104.2 161.6                            
REMARK 620 6 CAP G1477   O3   87.8  86.1 174.1  89.1  73.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG C1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG E1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG G1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1484                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1484                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I1127                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I1128                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1127                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1128                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1127                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1128                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1127                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1128                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AA1   RELATED DB: PDB                                   
REMARK 900  ACTIVATED SPINACH RUBISCO IN COMPLEX WITH                           
REMARK 900  THE PRODUCT 3-PHOSPHOGLYCERATE                                      
REMARK 900 RELATED ID: 1AUS   RELATED DB: PDB                                   
REMARK 900  ACTIVATED UNLIGANDED SPINACH RUBISCO                                
REMARK 900 RELATED ID: 1BWV   RELATED DB: PDB                                   
REMARK 900  ACTIVATED RIBULOSE 1,5-BISPHOSPHATE                                 
REMARK 900  CARBOXYLASE/OXYGENASE (RUBISCO) COMPLEXED WITH                      
REMARK 900  THE REACTION INTERMEDIATE ANALOGUE 2-                               
REMARK 900  CARBOXYARABINITOL 1,5-BISPHOSPHATE                                  
REMARK 900 RELATED ID: 1BXN   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF RUBISCO FROM                               
REMARK 900  ALCALIGENES EUTROPHUS TO 2.7 ANGSTROMS.                             
REMARK 900 RELATED ID: 1EJ7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF UNACTIVATED TOBACCO                            
REMARK 900  RUBISCO WITH BOUND PHOSPHATE IONS                                   
REMARK 900 RELATED ID: 1GK8   RELATED DB: PDB                                   
REMARK 900  RUBISCO FROM CHLAMYDOMONAS REINHARDTII                              
REMARK 900 RELATED ID: 1RBA   RELATED DB: PDB                                   
REMARK 900  RUBISCO (RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE                      
REMARK 900  /OXYGENASE) MUTANT WITH ASP 193 REPLACED BY                         
REMARK 900   ASN (D193N)                                                        
REMARK 900 RELATED ID: 1RBL   RELATED DB: PDB                                   
REMARK 900  RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/                              
REMARK 900  OXYGENASE (RUBISCO)                                                 
REMARK 900 RELATED ID: 1RBO   RELATED DB: PDB                                   
REMARK 900  SPINACH RUBISCO IN COMPLEX WITH THE                                 
REMARK 900  INHIBITOR 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE                       
REMARK 900 RELATED ID: 1RCO   RELATED DB: PDB                                   
REMARK 900  SPINACH RUBISCO IN COMPLEX WITH THE                                 
REMARK 900  INHIBITOR D-XYLULOSE-2,2-DIOL-1,5-                                  
REMARK 900  BISPHOSPHATE                                                        
REMARK 900 RELATED ID: 1RCX   RELATED DB: PDB                                   
REMARK 900  NON-ACTIVATED SPINACH RUBISCO IN COMPLEX                            
REMARK 900  WITH ITS SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE                        
REMARK 900 RELATED ID: 1RLC   RELATED DB: PDB                                   
REMARK 900  RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/                              
REMARK 900  OXYGENASE (RUBISCO) COMPLEX WITH 2-CARBOXY-D                        
REMARK 900  -ARABINITOL-1,5-BISPHOSPHATE(CABP)                                  
REMARK 900 RELATED ID: 1RLD   RELATED DB: PDB                                   
REMARK 900  RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/                              
REMARK 900  OXYGENASE (RUBISCO)                                                 
REMARK 900 RELATED ID: 1RSC   RELATED DB: PDB                                   
REMARK 900  RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/                              
REMARK 900  OXYGENASE (RUBISCO)                                                 
REMARK 900 RELATED ID: 1RUS   RELATED DB: PDB                                   
REMARK 900  RUBISCO (RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE                      
REMARK 900  (SLASH)OXYGENASE) COMPLEX WITH 3-                                   
REMARK 900  PHOSPHOGLYCERATE                                                    
REMARK 900 RELATED ID: 1RXO   RELATED DB: PDB                                   
REMARK 900  ACTIVATED SPINACH RUBISCO IN COMPLEX WITH                           
REMARK 900  ITS SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE AND                         
REMARK 900   CALCIUM                                                            
REMARK 900 RELATED ID: 2RUS   RELATED DB: PDB                                   
REMARK 900  RUBISCO (RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE                      
REMARK 900  (SLASH)OXYGENASE) COMPLEX WITH CO2 AND MG+                          
REMARK 900 RELATED ID: 5RUB   RELATED DB: PDB                                   
REMARK 900  RUBISCO (RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE                      
REMARK 900  (SLASH)OXYGENASE)                                                   
REMARK 900 RELATED ID: 8RUC   RELATED DB: PDB                                   
REMARK 900  ACTIVATED SPINACH RUBISCO COMPLEXED WITH 2-                         
REMARK 900  CARBOXYARABINITOL BISPHOSPHATE                                      
REMARK 900 RELATED ID: 9RUB   RELATED DB: PDB                                   
REMARK 900  RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE(SLASH)                        
REMARK 900  OXYGLUCOSE (RUBISCO) COMPLEXED WITH CO=2=,                          
REMARK 900  MG==++==, AND SUBSTRATE RIBULOSE-1,5-                               
REMARK 900  BISPHOSPHATE                                                        
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999  RESIDUE 46 IN THE LARGE SUBUNITS (CHAIN A C E G) WAS                
REMARK 999  FOUND TO BE PRO AFTER INSPECTION OF THE ELECTRON DENSITY MAPS.      
DBREF  1GK8 A    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1GK8 C    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1GK8 E    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1GK8 G    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1GK8 I    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  1GK8 K    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  1GK8 M    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  1GK8 O    1   140  UNP    P00873   RBS1_CHLRE      46    185             
SEQADV 1GK8 PRO A   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1GK8 PRO C   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1GK8 PRO E   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1GK8 PRO G   46  UNP  P00877    LEU    46 CONFLICT                       
SEQRES   1 A  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 A  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 A  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 A  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 A  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 A  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 A  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 A  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 A  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 A  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 A  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 A  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 A  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 A  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 A  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 A  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 A  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 A  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 A  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 A  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 A  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 A  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 A  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 A  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 A  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 A  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 A  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 A  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 A  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 A  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 A  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 A  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 A  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 A  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 A  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 A  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 A  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 C  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 C  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 C  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 C  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 C  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 C  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 C  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 C  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 C  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 C  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 C  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 C  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 C  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 C  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 C  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 C  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 C  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 C  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 C  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 C  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 C  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 C  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 C  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 C  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 C  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 C  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 C  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 C  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 C  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 C  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 C  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 C  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 C  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 C  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 C  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 C  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 C  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 E  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 E  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 E  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 E  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 E  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 E  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 E  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 E  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 E  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 E  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 E  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 E  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 E  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 E  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 E  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 E  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 E  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 E  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 E  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 E  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 E  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 E  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 E  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 E  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 E  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 E  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 E  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 E  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 E  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 E  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 E  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 E  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 E  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 E  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 E  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 E  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 E  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 G  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 G  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 G  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 G  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 G  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 G  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 G  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 G  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 G  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 G  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 G  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 G  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 G  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 G  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 G  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 G  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 G  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 G  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 G  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 G  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 G  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 G  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 G  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 G  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 G  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 G  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 G  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 G  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 G  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 G  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 G  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 G  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 G  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 G  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 G  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 G  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 G  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 I  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 I  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 I  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 I  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 I  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 I  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 I  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 I  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 I  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 I  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 I  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 K  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 K  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 K  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 K  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 K  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 K  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 K  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 K  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 K  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 K  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 K  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 M  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 M  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 M  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 M  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 M  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 M  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 M  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 M  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 M  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 M  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 M  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 O  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 O  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 O  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 O  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 O  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 O  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 O  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 O  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 O  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 O  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 O  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
MODRES 1GK8 HYP A  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1GK8 HYP A  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1GK8 KCX A  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1GK8 SMC A  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1GK8 SMC A  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1GK8 HYP C  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1GK8 HYP C  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1GK8 KCX C  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1GK8 SMC C  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1GK8 SMC C  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1GK8 HYP E  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1GK8 HYP E  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1GK8 KCX E  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1GK8 SMC E  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1GK8 SMC E  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1GK8 HYP G  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1GK8 HYP G  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1GK8 KCX G  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1GK8 SMC G  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1GK8 SMC G  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1GK8 MME I    1  MET  N-METHYL METHIONINE                                
MODRES 1GK8 MME K    1  MET  N-METHYL METHIONINE                                
MODRES 1GK8 MME M    1  MET  N-METHYL METHIONINE                                
MODRES 1GK8 MME O    1  MET  N-METHYL METHIONINE                                
HET    HYP  A 104       8                                                       
HET    HYP  A 151       8                                                       
HET    KCX  A 201      12                                                       
HET    SMC  A 256       7                                                       
HET    SMC  A 369       7                                                       
HET    HYP  C 104       8                                                       
HET    HYP  C 151       8                                                       
HET    KCX  C 201      12                                                       
HET    SMC  C 256       7                                                       
HET    SMC  C 369       7                                                       
HET    HYP  E 104       8                                                       
HET    HYP  E 151       8                                                       
HET    KCX  E 201      12                                                       
HET    SMC  E 256       7                                                       
HET    SMC  E 369       7                                                       
HET    HYP  G 104       8                                                       
HET    HYP  G 151       8                                                       
HET    KCX  G 201      12                                                       
HET    SMC  G 256       7                                                       
HET    SMC  G 369       7                                                       
HET    MME  I   1       9                                                       
HET    MME  K   1       9                                                       
HET    MME  M   1       9                                                       
HET    MME  O   1       9                                                       
HET     MG  A1476       1                                                       
HET     MG  C1476       1                                                       
HET     MG  E1476       1                                                       
HET     MG  G1476       1                                                       
HET    CAP  A1477      21                                                       
HET    EDO  A1478       4                                                       
HET    EDO  A1479       4                                                       
HET    EDO  A1480       4                                                       
HET    EDO  A1481       4                                                       
HET    EDO  A1482       4                                                       
HET    EDO  A1483       4                                                       
HET    EDO  A1484       4                                                       
HET    CAP  C1477      21                                                       
HET    EDO  C1478       4                                                       
HET    EDO  C1479       4                                                       
HET    EDO  C1480       4                                                       
HET    EDO  C1481       4                                                       
HET    EDO  C1482       4                                                       
HET    CAP  E1477      21                                                       
HET    EDO  E1478       4                                                       
HET    EDO  E1479       4                                                       
HET    EDO  E1480       4                                                       
HET    EDO  E1481       4                                                       
HET    EDO  E1482       4                                                       
HET    EDO  E1483       4                                                       
HET    EDO  E1484       4                                                       
HET    CAP  G1477      21                                                       
HET    EDO  G1478       4                                                       
HET    EDO  G1479       4                                                       
HET    EDO  G1480       4                                                       
HET    EDO  G1481       4                                                       
HET    EDO  G1482       4                                                       
HET    EDO  G1483       4                                                       
HET    EDO  I1127       4                                                       
HET    EDO  I1128       4                                                       
HET    EDO  K1127       4                                                       
HET    EDO  K1128       4                                                       
HET    EDO  M1127       4                                                       
HET    EDO  M1128       4                                                       
HET    EDO  O1127       4                                                       
HET    EDO  O1128       4                                                       
HETNAM     HYP 4-HYDROXYPROLINE                                                 
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM     SMC S-METHYLCYSTEINE                                                 
HETNAM     MME N-METHYL METHIONINE                                              
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE                              
HETNAM     EDO 1,2-ETHANEDIOL                                                   
FORMUL   1  HYP    8(C5 H9 N O3)                                                
FORMUL   1  KCX    4(C7 H14 N2 O4)                                              
FORMUL   1  SMC    8(C4 H9 N O2 S)                                              
FORMUL   5  MME    4(C6 H13 N O2 S)                                             
FORMUL   9   MG    4(MG 2+)                                                     
FORMUL  13  CAP    4(C6 H14 O13 P2)                                             
FORMUL  14  EDO    33(C2 H6 O2)                                                 
FORMUL  50  HOH   *2556(H2 O1)                                                  
HELIX    1   1 TYR A   20  TYR A   25  1                                   6    
HELIX    2   2 PRO A   49  SER A   61  1                                  13    
HELIX    3   3 VAL A   69  THR A   75  5                                   7    
HELIX    4   4 SER A   76  LYS A   81  1                                   6    
HELIX    5   5 HYP A  104  PHE A  108  5                                   5    
HELIX    6   6 SER A  112  GLY A  122  1                                  11    
HELIX    7   7 ASN A  123  PHE A  127  5                                   5    
HELIX    8   8 PRO A  141  LYS A  146  1                                   6    
HELIX    9   9 GLY A  154  ASN A  163  1                                  10    
HELIX   10  10 SER A  181  GLY A  195  1                                  15    
HELIX   11  11 ARG A  213  GLY A  233  1                                  21    
HELIX   12  12 THR A  246  GLY A  261  1                                  16    
HELIX   13  13 TYR A  269  GLY A  288  1                                  20    
HELIX   14  14 MET A  297  ARG A  303  1                                   7    
HELIX   15  15 HIS A  310  GLY A  322  1                                  13    
HELIX   16  16 GLU A  338  ASP A  351  1                                  14    
HELIX   17  17 ARG A  358  GLY A  361  5                                   4    
HELIX   18  18 HIS A  383  TRP A  385  5                                   3    
HELIX   19  19 HIS A  386  GLY A  395  1                                  10    
HELIX   20  20 GLY A  403  GLY A  408  1                                   6    
HELIX   21  21 GLY A  412  GLU A  433  1                                  22    
HELIX   22  22 ASP A  436  LYS A  463  1                                  28    
HELIX   23  23 TYR C   20  TYR C   25  1                                   6    
HELIX   24  24 PRO C   49  SER C   61  1                                  13    
HELIX   25  25 VAL C   69  THR C   75  5                                   7    
HELIX   26  26 SER C   76  LYS C   81  1                                   6    
HELIX   27  27 HYP C  104  PHE C  108  5                                   5    
HELIX   28  28 SER C  112  GLY C  122  1                                  11    
HELIX   29  29 ASN C  123  PHE C  127  5                                   5    
HELIX   30  30 PRO C  141  LYS C  146  1                                   6    
HELIX   31  31 GLY C  154  ASN C  163  1                                  10    
HELIX   32  32 SER C  181  GLY C  195  1                                  15    
HELIX   33  33 ARG C  213  GLY C  233  1                                  21    
HELIX   34  34 THR C  246  GLY C  261  1                                  16    
HELIX   35  35 TYR C  269  GLY C  288  1                                  20    
HELIX   36  36 MET C  297  ARG C  303  1                                   7    
HELIX   37  37 HIS C  310  GLY C  322  1                                  13    
HELIX   38  38 GLU C  338  ASP C  351  1                                  14    
HELIX   39  39 ARG C  358  GLY C  361  5                                   4    
HELIX   40  40 HIS C  383  TRP C  385  5                                   3    
HELIX   41  41 HIS C  386  GLY C  395  1                                  10    
HELIX   42  42 GLY C  403  GLY C  408  1                                   6    
HELIX   43  43 GLY C  412  GLU C  433  1                                  22    
HELIX   44  44 ASP C  436  LYS C  463  1                                  28    
HELIX   45  45 TYR E   20  TYR E   25  1                                   6    
HELIX   46  46 PRO E   49  SER E   61  1                                  13    
HELIX   47  47 VAL E   69  THR E   75  5                                   7    
HELIX   48  48 SER E   76  LYS E   81  1                                   6    
HELIX   49  49 HYP E  104  PHE E  108  5                                   5    
HELIX   50  50 SER E  112  GLY E  122  1                                  11    
HELIX   51  51 ASN E  123  PHE E  127  5                                   5    
HELIX   52  52 PRO E  141  LYS E  146  1                                   6    
HELIX   53  53 GLY E  154  ASN E  163  1                                  10    
HELIX   54  54 SER E  181  GLY E  195  1                                  15    
HELIX   55  55 ARG E  213  GLY E  233  1                                  21    
HELIX   56  56 THR E  246  GLY E  261  1                                  16    
HELIX   57  57 TYR E  269  GLY E  288  1                                  20    
HELIX   58  58 MET E  297  ARG E  303  1                                   7    
HELIX   59  59 HIS E  310  GLY E  322  1                                  13    
HELIX   60  60 GLU E  338  ASP E  351  1                                  14    
HELIX   61  61 ARG E  358  GLY E  361  5                                   4    
HELIX   62  62 HIS E  383  TRP E  385  5                                   3    
HELIX   63  63 HIS E  386  GLY E  395  1                                  10    
HELIX   64  64 GLY E  403  GLY E  408  1                                   6    
HELIX   65  65 GLY E  412  GLU E  433  1                                  22    
HELIX   66  66 ASP E  436  LYS E  463  1                                  28    
HELIX   67  67 TYR G   20  TYR G   25  1                                   6    
HELIX   68  68 PRO G   49  SER G   61  1                                  13    
HELIX   69  69 VAL G   69  THR G   75  5                                   7    
HELIX   70  70 SER G   76  LYS G   81  1                                   6    
HELIX   71  71 HYP G  104  PHE G  108  5                                   5    
HELIX   72  72 SER G  112  GLY G  122  1                                  11    
HELIX   73  73 ASN G  123  PHE G  127  5                                   5    
HELIX   74  74 PRO G  141  LYS G  146  1                                   6    
HELIX   75  75 GLY G  154  ASN G  163  1                                  10    
HELIX   76  76 SER G  181  GLY G  195  1                                  15    
HELIX   77  77 ARG G  213  GLY G  233  1                                  21    
HELIX   78  78 THR G  246  GLY G  261  1                                  16    
HELIX   79  79 TYR G  269  GLY G  288  1                                  20    
HELIX   80  80 MET G  297  ARG G  303  1                                   7    
HELIX   81  81 HIS G  310  GLY G  322  1                                  13    
HELIX   82  82 GLU G  338  ASP G  351  1                                  14    
HELIX   83  83 ARG G  358  GLY G  361  5                                   4    
HELIX   84  84 HIS G  383  TRP G  385  5                                   3    
HELIX   85  85 HIS G  386  GLY G  395  1                                  10    
HELIX   86  86 GLY G  403  GLY G  408  1                                   6    
HELIX   87  87 GLY G  412  GLU G  433  1                                  22    
HELIX   88  88 ASP G  436  LYS G  463  1                                  28    
HELIX   89  89 THR I   22  ASN I   36  1                                  15    
HELIX   90  90 GLU I   46  ALA I   50  5                                   5    
HELIX   91  91 ASN I   54  PHE I   60  5                                   7    
HELIX   92  92 ASP I   85  PHE I  100  1                                  16    
HELIX   93  93 THR K   22  ASN K   36  1                                  15    
HELIX   94  94 GLU K   46  ALA K   50  5                                   5    
HELIX   95  95 ASN K   54  PHE K   60  5                                   7    
HELIX   96  96 ASP K   85  PHE K  100  1                                  16    
HELIX   97  97 THR M   22  ASN M   36  1                                  15    
HELIX   98  98 GLU M   46  ALA M   50  5                                   5    
HELIX   99  99 ASN M   54  PHE M   60  5                                   7    
HELIX  100 100 ASP M   85  PHE M  100  1                                  16    
HELIX  101 101 THR O   22  ASN O   36  1                                  15    
HELIX  102 102 GLU O   46  ALA O   50  5                                   5    
HELIX  103 103 ASN O   54  PHE O   60  5                                   7    
HELIX  104 104 ASP O   85  PHE O  100  1                                  16    
SHEET    1  AA 5 ARG A  83  PRO A  89  0                                        
SHEET    2  AA 5 TYR A  97  TYR A 103 -1  O  ILE A  98   N  GLU A  88           
SHEET    3  AA 5 ILE A  36  PRO A  44 -1  O  ILE A  36   N  TYR A 103           
SHEET    4  AA 5 LEU A 130  ARG A 139 -1  N  ARG A 131   O  THR A  43           
SHEET    5  AA 5 GLY A 308  ILE A 309  1  O  GLY A 308   N  LEU A 135           
SHEET    1  AB 8 LEU A 169  GLY A 171  0                                        
SHEET    2  AB 8 CYS A 399  GLN A 401  1  O  LEU A 400   N  GLY A 171           
SHEET    3  AB 8 MET A 375  SER A 379  1  O  PRO A 376   N  CYS A 399           
SHEET    4  AB 8 HIS A 325  HIS A 327  1  O  LEU A 326   N  VAL A 377           
SHEET    5  AB 8 LEU A 290  HIS A 294  1  O  ILE A 293   N  HIS A 327           
SHEET    6  AB 8 ILE A 264  ASP A 268  1  O  ILE A 265   N  HIS A 292           
SHEET    7  AB 8 GLY A 237  ASN A 241  1  O  LEU A 240   N  MET A 266           
SHEET    8  AB 8 PHE A 199  KCX A 201  1  O  THR A 200   N  TYR A 239           
SHEET    1  AC 2 TYR A 353  VAL A 354  0                                        
SHEET    2  AC 2 GLN A 366  ASP A 367 -1  O  GLN A 366   N  VAL A 354           
SHEET    1  CA 5 ARG C  83  PRO C  89  0                                        
SHEET    2  CA 5 TYR C  97  TYR C 103 -1  O  ILE C  98   N  GLU C  88           
SHEET    3  CA 5 ILE C  36  PRO C  44 -1  O  ILE C  36   N  TYR C 103           
SHEET    4  CA 5 LEU C 130  ARG C 139 -1  N  ARG C 131   O  THR C  43           
SHEET    5  CA 5 GLY C 308  ILE C 309  1  O  GLY C 308   N  LEU C 135           
SHEET    1  CB 8 LEU C 169  GLY C 171  0                                        
SHEET    2  CB 8 CYS C 399  GLN C 401  1  O  LEU C 400   N  GLY C 171           
SHEET    3  CB 8 MET C 375  SER C 379  1  O  PRO C 376   N  CYS C 399           
SHEET    4  CB 8 HIS C 325  HIS C 327  1  O  LEU C 326   N  VAL C 377           
SHEET    5  CB 8 LEU C 290  HIS C 294  1  O  ILE C 293   N  HIS C 327           
SHEET    6  CB 8 ILE C 264  ASP C 268  1  O  ILE C 265   N  HIS C 292           
SHEET    7  CB 8 GLY C 237  ASN C 241  1  O  LEU C 240   N  MET C 266           
SHEET    8  CB 8 PHE C 199  KCX C 201  1  O  THR C 200   N  TYR C 239           
SHEET    1  CC 2 TYR C 353  VAL C 354  0                                        
SHEET    2  CC 2 GLN C 366  ASP C 367 -1  O  GLN C 366   N  VAL C 354           
SHEET    1  EA 5 ARG E  83  PRO E  89  0                                        
SHEET    2  EA 5 TYR E  97  TYR E 103 -1  O  ILE E  98   N  GLU E  88           
SHEET    3  EA 5 ILE E  36  PRO E  44 -1  O  ILE E  36   N  TYR E 103           
SHEET    4  EA 5 LEU E 130  ARG E 139 -1  N  ARG E 131   O  THR E  43           
SHEET    5  EA 5 GLY E 308  ILE E 309  1  O  GLY E 308   N  LEU E 135           
SHEET    1  EB 8 LEU E 169  GLY E 171  0                                        
SHEET    2  EB 8 CYS E 399  GLN E 401  1  O  LEU E 400   N  GLY E 171           
SHEET    3  EB 8 MET E 375  SER E 379  1  O  PRO E 376   N  CYS E 399           
SHEET    4  EB 8 HIS E 325  HIS E 327  1  O  LEU E 326   N  VAL E 377           
SHEET    5  EB 8 LEU E 290  HIS E 294  1  O  ILE E 293   N  HIS E 327           
SHEET    6  EB 8 ILE E 264  ASP E 268  1  O  ILE E 265   N  HIS E 292           
SHEET    7  EB 8 GLY E 237  ASN E 241  1  O  LEU E 240   N  MET E 266           
SHEET    8  EB 8 PHE E 199  KCX E 201  1  O  THR E 200   N  TYR E 239           
SHEET    1  EC 2 TYR E 353  VAL E 354  0                                        
SHEET    2  EC 2 GLN E 366  ASP E 367 -1  O  GLN E 366   N  VAL E 354           
SHEET    1  GA 5 ARG G  83  PRO G  89  0                                        
SHEET    2  GA 5 TYR G  97  TYR G 103 -1  O  ILE G  98   N  GLU G  88           
SHEET    3  GA 5 ILE G  36  PRO G  44 -1  O  ILE G  36   N  TYR G 103           
SHEET    4  GA 5 LEU G 130  ARG G 139 -1  N  ARG G 131   O  THR G  43           
SHEET    5  GA 5 GLY G 308  ILE G 309  1  O  GLY G 308   N  LEU G 135           
SHEET    1  GB 8 LEU G 169  GLY G 171  0                                        
SHEET    2  GB 8 CYS G 399  GLN G 401  1  O  LEU G 400   N  GLY G 171           
SHEET    3  GB 8 MET G 375  SER G 379  1  O  PRO G 376   N  CYS G 399           
SHEET    4  GB 8 HIS G 325  HIS G 327  1  O  LEU G 326   N  VAL G 377           
SHEET    5  GB 8 LEU G 290  HIS G 294  1  O  ILE G 293   N  HIS G 327           
SHEET    6  GB 8 ILE G 264  ASP G 268  1  O  ILE G 265   N  HIS G 292           
SHEET    7  GB 8 GLY G 237  ASN G 241  1  O  LEU G 240   N  MET G 266           
SHEET    8  GB 8 PHE G 199  KCX G 201  1  O  THR G 200   N  TYR G 239           
SHEET    1  GC 2 TYR G 353  VAL G 354  0                                        
SHEET    2  GC 2 GLN G 366  ASP G 367 -1  O  GLN G 366   N  VAL G 354           
SHEET    1  IA 4 THR I  74  TRP I  76  0                                        
SHEET    2  IA 4 ILE I  39  ALA I  45 -1  O  LEU I  42   N  TRP I  76           
SHEET    3  IA 4 TYR I 104  ASP I 111 -1  O  TYR I 104   N  ALA I  45           
SHEET    4  IA 4 VAL I 116  GLN I 124 -1  O  VAL I 116   N  ASP I 111           
SHEET    1  KA 4 THR K  74  TRP K  76  0                                        
SHEET    2  KA 4 ILE K  39  ALA K  45 -1  O  LEU K  42   N  TRP K  76           
SHEET    3  KA 4 TYR K 104  ASP K 111 -1  O  TYR K 104   N  ALA K  45           
SHEET    4  KA 4 VAL K 116  GLN K 124 -1  O  VAL K 116   N  ASP K 111           
SHEET    1  MA 4 THR M  74  TRP M  76  0                                        
SHEET    2  MA 4 ILE M  39  ALA M  45 -1  O  LEU M  42   N  TRP M  76           
SHEET    3  MA 4 TYR M 104  ASP M 111 -1  O  TYR M 104   N  ALA M  45           
SHEET    4  MA 4 VAL M 116  GLN M 124 -1  O  VAL M 116   N  ASP M 111           
SHEET    1  OA 4 THR O  74  TRP O  76  0                                        
SHEET    2  OA 4 ILE O  39  ALA O  45 -1  O  LEU O  42   N  TRP O  76           
SHEET    3  OA 4 TYR O 104  ASP O 111 -1  O  TYR O 104   N  ALA O  45           
SHEET    4  OA 4 VAL O 116  GLN O 124 -1  O  VAL O 116   N  ASP O 111           
SSBOND   1 CYS A  449    CYS A  459                          1555   1555  2.02  
SSBOND   2 CYS C  247    CYS G  247                          1555   2555  2.41  
SSBOND   3 CYS C  449    CYS C  459                          1555   1555  2.01  
SSBOND   4 CYS E  449    CYS E  459                          1555   1555  2.58  
SSBOND   5 CYS G  449    CYS G  459                          1555   1555  2.01  
LINK         C   TYR A 103                 N   HYP A 104     1555   1555  1.43  
LINK         C   HYP A 104                 N   ILE A 105     1555   1555  1.34  
LINK         C   GLY A 150                 N   HYP A 151     1555   1555  1.44  
LINK         C   HYP A 151                 N   PRO A 152     1555   1555  1.33  
LINK         C   THR A 200                 N   KCX A 201     1555   1555  1.33  
LINK         C   KCX A 201                 N   ASP A 202     1555   1555  1.33  
LINK         OQ2 KCX A 201                MG    MG A1476     1555   1555  2.02  
LINK         C   VAL A 255                 N   SMC A 256     1555   1555  1.33  
LINK         C   SMC A 256                 N   ALA A 257     1555   1555  1.33  
LINK         C   TRP A 368                 N   SMC A 369     1555   1555  1.33  
LINK         C   SMC A 369                 N   SER A 370     1555   1555  1.33  
LINK        MG    MG A1476                 OD1 ASP A 203     1555   1555  1.98  
LINK        MG    MG A1476                 OE1 GLU A 204     1555   1555  2.00  
LINK        MG    MG A1476                 O2  CAP A1477     1555   1555  2.24  
LINK        MG    MG A1476                 O3  CAP A1477     1555   1555  2.18  
LINK        MG    MG A1476                 O6  CAP A1477     1555   1555  2.10  
LINK         C   TYR C 103                 N   HYP C 104     1555   1555  1.43  
LINK         C   HYP C 104                 N   ILE C 105     1555   1555  1.33  
LINK         C   GLY C 150                 N   HYP C 151     1555   1555  1.44  
LINK         C   HYP C 151                 N   PRO C 152     1555   1555  1.32  
LINK         C   THR C 200                 N   KCX C 201     1555   1555  1.33  
LINK         C   KCX C 201                 N   ASP C 202     1555   1555  1.33  
LINK         OQ2 KCX C 201                MG    MG C1476     1555   1555  2.00  
LINK         C   VAL C 255                 N   SMC C 256     1555   1555  1.33  
LINK         C   SMC C 256                 N   ALA C 257     1555   1555  1.33  
LINK         C   TRP C 368                 N   SMC C 369     1555   1555  1.33  
LINK         C   SMC C 369                 N   SER C 370     1555   1555  1.33  
LINK        MG    MG C1476                 OD1 ASP C 203     1555   1555  1.94  
LINK        MG    MG C1476                 O2  CAP C1477     1555   1555  2.34  
LINK        MG    MG C1476                 OE1 GLU C 204     1555   1555  2.00  
LINK        MG    MG C1476                 O6  CAP C1477     1555   1555  2.08  
LINK        MG    MG C1476                 O3  CAP C1477     1555   1555  2.19  
LINK         C   TYR E 103                 N   HYP E 104     1555   1555  1.43  
LINK         C   HYP E 104                 N   ILE E 105     1555   1555  1.34  
LINK         C   GLY E 150                 N   HYP E 151     1555   1555  1.43  
LINK         C   HYP E 151                 N   PRO E 152     1555   1555  1.33  
LINK         C   THR E 200                 N   KCX E 201     1555   1555  1.33  
LINK         C   KCX E 201                 N   ASP E 202     1555   1555  1.34  
LINK         OQ2 KCX E 201                MG    MG E1476     1555   1555  2.01  
LINK         C   VAL E 255                 N   SMC E 256     1555   1555  1.33  
LINK         C   SMC E 256                 N   ALA E 257     1555   1555  1.32  
LINK         C   TRP E 368                 N   SMC E 369     1555   1555  1.33  
LINK         C   SMC E 369                 N   SER E 370     1555   1555  1.33  
LINK        MG    MG E1476                 OD1 ASP E 203     1555   1555  1.96  
LINK        MG    MG E1476                 O3  CAP E1477     1555   1555  2.19  
LINK        MG    MG E1476                 O6  CAP E1477     1555   1555  2.08  
LINK        MG    MG E1476                 O2  CAP E1477     1555   1555  2.21  
LINK        MG    MG E1476                 OE1 GLU E 204     1555   1555  2.02  
LINK         C   TYR G 103                 N   HYP G 104     1555   1555  1.43  
LINK         C   HYP G 104                 N   ILE G 105     1555   1555  1.33  
LINK         C   GLY G 150                 N   HYP G 151     1555   1555  1.44  
LINK         C   HYP G 151                 N   PRO G 152     1555   1555  1.33  
LINK         C   THR G 200                 N   KCX G 201     1555   1555  1.33  
LINK         OQ2 KCX G 201                MG    MG G1476     1555   1555  2.03  
LINK         C   KCX G 201                 N   ASP G 202     1555   1555  1.34  
LINK         C   VAL G 255                 N   SMC G 256     1555   1555  1.33  
LINK         C   SMC G 256                 N   ALA G 257     1555   1555  1.33  
LINK         C   TRP G 368                 N   SMC G 369     1555   1555  1.32  
LINK         C   SMC G 369                 N   SER G 370     1555   1555  1.33  
LINK        MG    MG G1476                 O3  CAP G1477     1555   1555  2.19  
LINK        MG    MG G1476                 O2  CAP G1477     1555   1555  2.21  
LINK        MG    MG G1476                 OE1 GLU G 204     1555   1555  2.02  
LINK        MG    MG G1476                 O6  CAP G1477     1555   1555  2.09  
LINK        MG    MG G1476                 OD1 ASP G 203     1555   1555  1.95  
LINK         C   MME I   1                 N   MET I   2     1555   1555  1.32  
LINK         C   MME K   1                 N   MET K   2     1555   1555  1.32  
LINK         C   MME M   1                 N   MET M   2     1555   1555  1.32  
LINK         C   MME O   1                 N   MET O   2     1555   1555  1.33  
SITE     1 AC1  5 LYS A 177  KCX A 201  ASP A 203  GLU A 204                    
SITE     2 AC1  5 CAP A1477                                                     
SITE     1 AC2  5 LYS C 177  KCX C 201  ASP C 203  GLU C 204                    
SITE     2 AC2  5 CAP C1477                                                     
SITE     1 AC3  5 LYS E 177  KCX E 201  ASP E 203  GLU E 204                    
SITE     2 AC3  5 CAP E1477                                                     
SITE     1 AC4  4 KCX G 201  ASP G 203  GLU G 204  CAP G1477                    
SITE     1 AC5 28 GLU A  60  THR A  65  TRP A  66  ASN A 123                    
SITE     2 AC5 28 THR A 173  LYS A 175  LYS A 177  KCX A 201                    
SITE     3 AC5 28 ASP A 203  GLU A 204  HIS A 294  ARG A 295                    
SITE     4 AC5 28 HIS A 327  LYS A 334  LEU A 335  SER A 379                    
SITE     5 AC5 28 GLY A 380  GLY A 381  GLY A 403  GLY A 404                    
SITE     6 AC5 28  MG A1476  HOH A2153  HOH A2443  HOH A2444                    
SITE     7 AC5 28 HOH A2445  HOH A2446  HOH A2447  HOH A2448                    
SITE     1 AC6  9 TYR A  24  GLY A  64  THR A  68  VAL A  69                    
SITE     2 AC6  9 ASP A  72  LEU A  77  HOH A2449  HOH A2450                    
SITE     3 AC6  9 HOH A2451                                                     
SITE     1 AC7  8 VAL A  17  LYS A  18  THR A  65  TRP A  66                    
SITE     2 AC7  8 THR A  67  THR A  68  HOH A2451  HOH A2452                    
SITE     1 AC8  4 GLU A  52  HOH A2453  HOH A2454  HOH A2455                    
SITE     1 AC9  8 GLY A  47  VAL A  48  PRO A  49  GLU A  52                    
SITE     2 AC9  8 HOH A2022  HOH A2455  HOH A2456  HOH A2457                    
SITE     1 BC1  6 LYS A 466  PHE A 467  GLU A 468  PHE A 469                    
SITE     2 BC1  6 HOH A2453  HOH A2458                                          
SITE     1 BC2  8 HIS A 298  PHE A 311  GLU A 336  ASP A 473                    
SITE     2 BC2  8 HOH A2286  HOH A2310  HOH A2459  HOH A2460                    
SITE     1 BC3  2 LEU A 270  HOH A2461                                          
SITE     1 BC4 28 THR C 173  LYS C 175  LYS C 177  KCX C 201                    
SITE     2 BC4 28 ASP C 203  GLU C 204  HIS C 294  ARG C 295                    
SITE     3 BC4 28 HIS C 327  LYS C 334  LEU C 335  SER C 379                    
SITE     4 BC4 28 GLY C 380  GLY C 381  GLY C 403  GLY C 404                    
SITE     5 BC4 28  MG C1476  HOH C2453  HOH C2454  HOH C2455                    
SITE     6 BC4 28 HOH C2456  HOH C2457  HOH C2458  GLU G  60                    
SITE     7 BC4 28 THR G  65  TRP G  66  ASN G 123  HOH G2174                    
SITE     1 BC5 10 TYR C  24  GLY C  64  THR C  68  VAL C  69                    
SITE     2 BC5 10 ASP C  72  LEU C  77  EDO C1479  HOH C2459                    
SITE     3 BC5 10 HOH C2460  HOH C2461                                          
SITE     1 BC6 10 GLY C  16  VAL C  17  LYS C  18  THR C  65                    
SITE     2 BC6 10 TRP C  66  THR C  67  THR C  68  EDO C1478                    
SITE     3 BC6 10 HOH C2043  HOH C2461                                          
SITE     1 BC7  3 GLU C  52  HOH C2462  HOH C2463                               
SITE     1 BC8  6 LYS C 466  PHE C 467  GLU C 468  PHE C 469                    
SITE     2 BC8  6 HOH C2464  HOH G2470                                          
SITE     1 BC9  8 HIS C 298  PHE C 311  GLU C 336  ASP C 473                    
SITE     2 BC9  8 HOH C2286  HOH C2309  HOH C2465  HOH C2466                    
SITE     1 CC1 28 GLU E  60  THR E  65  TRP E  66  ASN E 123                    
SITE     2 CC1 28 THR E 173  LYS E 175  LYS E 177  KCX E 201                    
SITE     3 CC1 28 ASP E 203  GLU E 204  HIS E 294  ARG E 295                    
SITE     4 CC1 28 HIS E 327  LYS E 334  LEU E 335  SER E 379                    
SITE     5 CC1 28 GLY E 380  GLY E 381  GLY E 403  GLY E 404                    
SITE     6 CC1 28  MG E1476  HOH E2161  HOH E2469  HOH E2470                    
SITE     7 CC1 28 HOH E2471  HOH E2472  HOH E2473  HOH E2474                    
SITE     1 CC2  9 TYR E  24  GLY E  64  THR E  68  VAL E  69                    
SITE     2 CC2  9 ASP E  72  LEU E  77  HOH E2475  HOH E2476                    
SITE     3 CC2  9 HOH E2478                                                     
SITE     1 CC3  8 VAL E  17  LYS E  18  THR E  65  TRP E  66                    
SITE     2 CC3  8 THR E  67  THR E  68  HOH E2477  HOH E2478                    
SITE     1 CC4  5 GLU E  52  EDO E1481  HOH E2479  HOH E2480                    
SITE     2 CC4  5 HOH E2483                                                     
SITE     1 CC5  9 GLY E  47  VAL E  48  PRO E  49  GLU E  52                    
SITE     2 CC5  9 EDO E1480  HOH E2018  HOH E2481  HOH E2482                    
SITE     3 CC5  9 HOH E2483                                                     
SITE     1 CC6  6 LYS E 466  PHE E 467  GLU E 468  PHE E 469                    
SITE     2 CC6  6 HOH E2480  HOH E2484                                          
SITE     1 CC7  8 HIS E 298  PHE E 311  GLU E 336  ASP E 473                    
SITE     2 CC7  8 HOH E2301  HOH E2325  HOH E2485  HOH E2486                    
SITE     1 CC8  2 LEU E 270  HOH E2487                                          
SITE     1 CC9 28 GLU C  60  THR C  65  TRP C  66  ASN C 123                    
SITE     2 CC9 28 HOH C2150  THR G 173  LYS G 175  LYS G 177                    
SITE     3 CC9 28 KCX G 201  ASP G 203  GLU G 204  HIS G 294                    
SITE     4 CC9 28 ARG G 295  HIS G 327  LYS G 334  LEU G 335                    
SITE     5 CC9 28 SER G 379  GLY G 380  GLY G 381  GLY G 403                    
SITE     6 CC9 28 GLY G 404   MG G1476  HOH G2458  HOH G2459                    
SITE     7 CC9 28 HOH G2460  HOH G2461  HOH G2462  HOH G2463                    
SITE     1 DC1  9 TYR G  24  GLY G  64  THR G  68  VAL G  69                    
SITE     2 DC1  9 ASP G  72  LEU G  77  HOH G2464  HOH G2465                    
SITE     3 DC1  9 HOH G2466                                                     
SITE     1 DC2  8 VAL G  17  LYS G  18  THR G  65  TRP G  66                    
SITE     2 DC2  8 THR G  67  THR G  68  HOH G2466  HOH G2467                    
SITE     1 DC3  3 GLU G  52  HOH G2468  HOH G2470                               
SITE     1 DC4  7 HOH C2463  GLU G 464  LYS G 466  PHE G 467                    
SITE     2 DC4  7 GLU G 468  PHE G 469  HOH G2442                               
SITE     1 DC5  8 HIS G 298  PHE G 311  GLU G 336  ASP G 473                    
SITE     2 DC5  8 HOH G2300  HOH G2326  HOH G2471  HOH G2472                    
SITE     1 DC6  4 LEU C 270  LEU G 270  HOH G2473  HOH G2474                    
SITE     1 DC7  5 TYR C 226  HOH C2237  LYS I  49  GLU I  55                    
SITE     2 DC7  5 HOH I2104                                                     
SITE     1 DC8  7 GLY I  37  TRP I  38  ILE I  39  PHE I  81                    
SITE     2 DC8  7 GLY I  82  CYS I  83  HOH I2157                               
SITE     1 DC9  6 TYR E 226  HOH E2251  LYS K  49  GLU K  55                    
SITE     2 DC9  6 HOH K2110  HOH K2166                                          
SITE     1 EC1  7 GLY K  37  TRP K  38  ILE K  39  GLY K  82                    
SITE     2 EC1  7 CYS K  83  HOH K2167  HOH K2168                               
SITE     1 EC2  6 TYR G 226  HOH G2254  LYS M  49  GLU M  55                    
SITE     2 EC2  6 HOH M2113  HOH M2168                                          
SITE     1 EC3  7 GLY M  37  TRP M  38  ILE M  39  GLY M  82                    
SITE     2 EC3  7 CYS M  83  ARG M  84  HOH M2170                               
SITE     1 EC4  7 TYR A 226  ALA A 230  HOH A2237  LYS O  49                    
SITE     2 EC4  7 GLU O  55  HOH O2113  HOH O2171                               
SITE     1 EC5  6 GLY O  37  TRP O  38  ILE O  39  GLY O  82                    
SITE     2 EC5  6 CYS O  83  HOH O2172                                          
CRYST1  171.375  142.638  124.717  90.00 124.13  90.00 C 1 2 1      16          
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      0.005835  0.000000  0.003955        0.00000                         
SCALE2      0.000000  0.007011  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009686        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system