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Database: PDB
Entry: 3AXM
LinkDB: 3AXM
Original site: 3AXM 
HEADER    LYASE                                   11-APR-11   3AXM              
TITLE     STRUCTURE OF RICE RUBISCO IN COMPLEX WITH 6PG                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;             
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: RUBISCO LARGE SUBUNIT, D-RIBULOSE 1,5-BISPHOSPHATE          
COMPND   5 CARBOXYLASE/OXYGENASE LARGE SUBUNIT;                                 
COMPND   6 EC: 4.1.1.39;                                                        
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN,             
COMPND   9 CHLOROPLASTIC;                                                       
COMPND  10 CHAIN: S, T, U, V, W, X, Y, Z;                                       
COMPND  11 SYNONYM: RUBISCO SMALL SUBUNIT, D-RIBULOSE 1,5-BISPHOSPHATE          
COMPND  12 CARBOXYLASE/OXYGENASE SMALL SUBUNIT;                                 
COMPND  13 EC: 4.1.1.39                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ORYZA SATIVA JAPONICA GROUP;                    
SOURCE   3 ORGANISM_COMMON: JAPANESE RICE;                                      
SOURCE   4 ORGANISM_TAXID: 39947;                                               
SOURCE   5 TISSUE: LEAVES;                                                      
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: ORYZA SATIVA JAPONICA GROUP;                    
SOURCE   8 ORGANISM_COMMON: JAPANESE RICE;                                      
SOURCE   9 ORGANISM_TAXID: 39947;                                               
SOURCE  10 TISSUE: LEAVES                                                       
KEYWDS    ALPHA/BETA BARREL, PHOTOSYNTHETIC CARBON REDUCTION, LYASE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.MATSUMURA,E.MIZOHATA,H.ISHIDA,A.KOGAMI,T.UENO,A.MAKINO,T.INOUE,     
AUTHOR   2 A.YOKOTA,T.MAE,Y.KAI                                                 
REVDAT   3   05-JUN-13 3AXM    1       JRNL                                     
REVDAT   2   13-JUN-12 3AXM    1       JRNL                                     
REVDAT   1   11-APR-12 3AXM    0                                                
JRNL        AUTH   H.MATSUMURA,E.MIZOHATA,H.ISHIDA,A.KOGAMI,T.UENO,A.MAKINO,    
JRNL        AUTH 2 T.INOUE,A.YOKOTA,T.MAE,Y.KAI                                 
JRNL        TITL   CRYSTAL STRUCTURE OF RICE RUBISCO AND IMPLICATIONS FOR       
JRNL        TITL 2 ACTIVATION INDUCED BY POSITIVE EFFECTORS NADPH AND           
JRNL        TITL 3 6-PHOSPHOGLUCONATE                                           
JRNL        REF    J.MOL.BIOL.                   V. 422    75 2012              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   22609438                                                     
JRNL        DOI    10.1016/J.JMB.2012.05.014                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 74.26                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 266882.850                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 489320                         
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 SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.190                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 24285                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.001                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 74025                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2130                       
REMARK   3   BIN FREE R VALUE                    : 0.2320                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 3803                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.004                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 35806                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 144                                     
REMARK   3   SOLVENT ATOMS            : 3607                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.19000                                             
REMARK   3    B22 (A**2) : -1.65000                                             
REMARK   3    B33 (A**2) : 3.84000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.40000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.16                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.13                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.18                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.15                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.85                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.050 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.630 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.770 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.580 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.39                                                 
REMARK   3   BSOL        : 56.81                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : RUB.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : RUB.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3AXM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-APR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB029822.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-NOV-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL44XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : OTHERS                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 511171                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 74.260                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 13.100                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 75MM HEPES-KOH(PH 7.75), 9% PEG4000,     
REMARK 280  25% GLYCEROL, VAPOR DIFFUSION, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       99.81200            
REMARK 290   SMTRY3   2  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 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: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 98720 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 120810 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -409.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, T, S, C, D, U, V, E,            
REMARK 350                    AND CHAINS: F, X, W, G, H, Z, Y                   
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     VAL A    11                                                      
REMARK 465     LYS A    18                                                      
REMARK 465     ASP A    19                                                      
REMARK 465     TYR A    20                                                      
REMARK 465     LYS A    21                                                      
REMARK 465     LEU A    22                                                      
REMARK 465     LEU A   335                                                      
REMARK 465     GLU A   336                                                      
REMARK 465     GLY A   337                                                      
REMARK 465     ALA A   464                                                      
REMARK 465     ILE A   465                                                      
REMARK 465     LYS A   466                                                      
REMARK 465     PHE A   467                                                      
REMARK 465     GLU A   468                                                      
REMARK 465     PHE A   469                                                      
REMARK 465     GLU A   470                                                      
REMARK 465     PRO A   471                                                      
REMARK 465     VAL A   472                                                      
REMARK 465     ASP A   473                                                      
REMARK 465     LYS A   474                                                      
REMARK 465     LEU A   475                                                      
REMARK 465     ASP A   476                                                      
REMARK 465     SER A   477                                                      
REMARK 465     GLU S   124                                                      
REMARK 465     GLU S   125                                                      
REMARK 465     SER S   126                                                      
REMARK 465     GLY S   127                                                      
REMARK 465     GLY S   128                                                      
REMARK 465     ASN S   129                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     VAL B    11                                                      
REMARK 465     LYS B    18                                                      
REMARK 465     ASP B    19                                                      
REMARK 465     TYR B    20                                                      
REMARK 465     VAL B   332                                                      
REMARK 465     GLY B   333                                                      
REMARK 465     LYS B   334                                                      
REMARK 465     LEU B   335                                                      
REMARK 465     GLU B   336                                                      
REMARK 465     GLY B   337                                                      
REMARK 465     ALA B   464                                                      
REMARK 465     ILE B   465                                                      
REMARK 465     LYS B   466                                                      
REMARK 465     PHE B   467                                                      
REMARK 465     GLU B   468                                                      
REMARK 465     PHE B   469                                                      
REMARK 465     GLU B   470                                                      
REMARK 465     PRO B   471                                                      
REMARK 465     VAL B   472                                                      
REMARK 465     ASP B   473                                                      
REMARK 465     LYS B   474                                                      
REMARK 465     LEU B   475                                                      
REMARK 465     ASP B   476                                                      
REMARK 465     SER B   477                                                      
REMARK 465     GLU T   124                                                      
REMARK 465     GLU T   125                                                      
REMARK 465     SER T   126                                                      
REMARK 465     GLY T   127                                                      
REMARK 465     GLY T   128                                                      
REMARK 465     ASN T   129                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     PRO C     3                                                      
REMARK 465     GLN C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     GLU C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     ALA C     9                                                      
REMARK 465     SER C    10                                                      
REMARK 465     VAL C    11                                                      
REMARK 465     LYS C    18                                                      
REMARK 465     ASP C    19                                                      
REMARK 465     TYR C    20                                                      
REMARK 465     LYS C    21                                                      
REMARK 465     GLY C   333                                                      
REMARK 465     LYS C   334                                                      
REMARK 465     LEU C   335                                                      
REMARK 465     GLU C   336                                                      
REMARK 465     GLY C   337                                                      
REMARK 465     ALA C   464                                                      
REMARK 465     ILE C   465                                                      
REMARK 465     LYS C   466                                                      
REMARK 465     PHE C   467                                                      
REMARK 465     GLU C   468                                                      
REMARK 465     PHE C   469                                                      
REMARK 465     GLU C   470                                                      
REMARK 465     PRO C   471                                                      
REMARK 465     VAL C   472                                                      
REMARK 465     ASP C   473                                                      
REMARK 465     LYS C   474                                                      
REMARK 465     LEU C   475                                                      
REMARK 465     ASP C   476                                                      
REMARK 465     SER C   477                                                      
REMARK 465     GLU U   124                                                      
REMARK 465     GLU U   125                                                      
REMARK 465     SER U   126                                                      
REMARK 465     GLY U   127                                                      
REMARK 465     GLY U   128                                                      
REMARK 465     ASN U   129                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     PRO D     3                                                      
REMARK 465     GLN D     4                                                      
REMARK 465     THR D     5                                                      
REMARK 465     GLU D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     LYS D     8                                                      
REMARK 465     ALA D     9                                                      
REMARK 465     SER D    10                                                      
REMARK 465     VAL D    11                                                      
REMARK 465     LYS D    18                                                      
REMARK 465     ASP D    19                                                      
REMARK 465     TYR D    20                                                      
REMARK 465     GLY D   333                                                      
REMARK 465     LYS D   334                                                      
REMARK 465     LEU D   335                                                      
REMARK 465     GLU D   336                                                      
REMARK 465     GLY D   337                                                      
REMARK 465     ALA D   464                                                      
REMARK 465     ILE D   465                                                      
REMARK 465     LYS D   466                                                      
REMARK 465     PHE D   467                                                      
REMARK 465     GLU D   468                                                      
REMARK 465     PHE D   469                                                      
REMARK 465     GLU D   470                                                      
REMARK 465     PRO D   471                                                      
REMARK 465     VAL D   472                                                      
REMARK 465     ASP D   473                                                      
REMARK 465     LYS D   474                                                      
REMARK 465     LEU D   475                                                      
REMARK 465     ASP D   476                                                      
REMARK 465     SER D   477                                                      
REMARK 465     GLU V   124                                                      
REMARK 465     GLU V   125                                                      
REMARK 465     SER V   126                                                      
REMARK 465     GLY V   127                                                      
REMARK 465     GLY V   128                                                      
REMARK 465     ASN V   129                                                      
REMARK 465     MET E     1                                                      
REMARK 465     SER 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     SER E    10                                                      
REMARK 465     VAL E    11                                                      
REMARK 465     LYS E    18                                                      
REMARK 465     ASP E    19                                                      
REMARK 465     TYR E    20                                                      
REMARK 465     LYS E    21                                                      
REMARK 465     VAL E   331                                                      
REMARK 465     VAL E   332                                                      
REMARK 465     GLY E   333                                                      
REMARK 465     LYS E   334                                                      
REMARK 465     LEU E   335                                                      
REMARK 465     GLU E   336                                                      
REMARK 465     GLY E   337                                                      
REMARK 465     ALA E   464                                                      
REMARK 465     ILE E   465                                                      
REMARK 465     LYS E   466                                                      
REMARK 465     PHE E   467                                                      
REMARK 465     GLU E   468                                                      
REMARK 465     PHE E   469                                                      
REMARK 465     GLU E   470                                                      
REMARK 465     PRO E   471                                                      
REMARK 465     VAL E   472                                                      
REMARK 465     ASP E   473                                                      
REMARK 465     LYS E   474                                                      
REMARK 465     LEU E   475                                                      
REMARK 465     ASP E   476                                                      
REMARK 465     SER E   477                                                      
REMARK 465     GLU W   124                                                      
REMARK 465     GLU W   125                                                      
REMARK 465     SER W   126                                                      
REMARK 465     GLY W   127                                                      
REMARK 465     GLY W   128                                                      
REMARK 465     ASN W   129                                                      
REMARK 465     MET F     1                                                      
REMARK 465     SER F     2                                                      
REMARK 465     PRO F     3                                                      
REMARK 465     GLN F     4                                                      
REMARK 465     THR F     5                                                      
REMARK 465     GLU F     6                                                      
REMARK 465     THR F     7                                                      
REMARK 465     LYS F     8                                                      
REMARK 465     ALA F     9                                                      
REMARK 465     SER F    10                                                      
REMARK 465     VAL F    11                                                      
REMARK 465     LYS F    18                                                      
REMARK 465     ASP F    19                                                      
REMARK 465     TYR F    20                                                      
REMARK 465     GLY F   333                                                      
REMARK 465     LYS F   334                                                      
REMARK 465     LEU F   335                                                      
REMARK 465     GLU F   336                                                      
REMARK 465     GLY F   337                                                      
REMARK 465     ALA F   464                                                      
REMARK 465     ILE F   465                                                      
REMARK 465     LYS F   466                                                      
REMARK 465     PHE F   467                                                      
REMARK 465     GLU F   468                                                      
REMARK 465     PHE F   469                                                      
REMARK 465     GLU F   470                                                      
REMARK 465     PRO F   471                                                      
REMARK 465     VAL F   472                                                      
REMARK 465     ASP F   473                                                      
REMARK 465     LYS F   474                                                      
REMARK 465     LEU F   475                                                      
REMARK 465     ASP F   476                                                      
REMARK 465     SER F   477                                                      
REMARK 465     GLU X   124                                                      
REMARK 465     GLU X   125                                                      
REMARK 465     SER X   126                                                      
REMARK 465     GLY X   127                                                      
REMARK 465     GLY X   128                                                      
REMARK 465     ASN X   129                                                      
REMARK 465     MET G     1                                                      
REMARK 465     SER 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     ALA G     9                                                      
REMARK 465     SER G    10                                                      
REMARK 465     VAL G    11                                                      
REMARK 465     LYS G    18                                                      
REMARK 465     ASP G    19                                                      
REMARK 465     TYR G    20                                                      
REMARK 465     LYS G    21                                                      
REMARK 465     VAL G   331                                                      
REMARK 465     VAL G   332                                                      
REMARK 465     GLY G   333                                                      
REMARK 465     LYS G   334                                                      
REMARK 465     LEU G   335                                                      
REMARK 465     GLU G   336                                                      
REMARK 465     GLY G   337                                                      
REMARK 465     ALA G   464                                                      
REMARK 465     ILE G   465                                                      
REMARK 465     LYS G   466                                                      
REMARK 465     PHE G   467                                                      
REMARK 465     GLU G   468                                                      
REMARK 465     PHE G   469                                                      
REMARK 465     GLU G   470                                                      
REMARK 465     PRO G   471                                                      
REMARK 465     VAL G   472                                                      
REMARK 465     ASP G   473                                                      
REMARK 465     LYS G   474                                                      
REMARK 465     LEU G   475                                                      
REMARK 465     ASP G   476                                                      
REMARK 465     SER G   477                                                      
REMARK 465     GLU Y   124                                                      
REMARK 465     GLU Y   125                                                      
REMARK 465     SER Y   126                                                      
REMARK 465     GLY Y   127                                                      
REMARK 465     GLY Y   128                                                      
REMARK 465     ASN Y   129                                                      
REMARK 465     MET H     1                                                      
REMARK 465     SER H     2                                                      
REMARK 465     PRO H     3                                                      
REMARK 465     GLN H     4                                                      
REMARK 465     THR H     5                                                      
REMARK 465     GLU H     6                                                      
REMARK 465     THR H     7                                                      
REMARK 465     LYS H     8                                                      
REMARK 465     ALA H     9                                                      
REMARK 465     SER H    10                                                      
REMARK 465     VAL H    11                                                      
REMARK 465     LYS H    18                                                      
REMARK 465     ASP H    19                                                      
REMARK 465     TYR H    20                                                      
REMARK 465     GLY H   333                                                      
REMARK 465     LYS H   334                                                      
REMARK 465     LEU H   335                                                      
REMARK 465     GLU H   336                                                      
REMARK 465     GLY H   337                                                      
REMARK 465     ALA H   464                                                      
REMARK 465     ILE H   465                                                      
REMARK 465     LYS H   466                                                      
REMARK 465     PHE H   467                                                      
REMARK 465     GLU H   468                                                      
REMARK 465     PHE H   469                                                      
REMARK 465     GLU H   470                                                      
REMARK 465     PRO H   471                                                      
REMARK 465     VAL H   472                                                      
REMARK 465     ASP H   473                                                      
REMARK 465     LYS H   474                                                      
REMARK 465     LEU H   475                                                      
REMARK 465     ASP H   476                                                      
REMARK 465     SER H   477                                                      
REMARK 465     GLU Z   124                                                      
REMARK 465     GLU Z   125                                                      
REMARK 465     SER Z   126                                                      
REMARK 465     GLY Z   127                                                      
REMARK 465     GLY Z   128                                                      
REMARK 465     ASN Z   129                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     NME S   0    N                                                   
REMARK 470     NME T   0    N                                                   
REMARK 470     NME U   0    N                                                   
REMARK 470     NME V   0    N                                                   
REMARK 470     NME W   0    N                                                   
REMARK 470     NME X   0    N                                                   
REMARK 470     NME Y   0    N                                                   
REMARK 470     NME Z   0    N                                                   
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 A   949     O    HOH B  1425              1.76            
REMARK 500   O    HOH B  1425     O    HOH B  3596              2.03            
REMARK 500   O    ALA D    15     O    HOH D  3479              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLY C  12   N     GLY C  12   CA      0.161                       
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    ALA B  15   N   -  CA  -  C   ANGL. DEV. =  17.9 DEGREES          
REMARK 500    PHE C  13   N   -  CA  -  C   ANGL. DEV. = -17.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  13     -100.34    -37.63                                   
REMARK 500    LYS A  14       95.49     79.96                                   
REMARK 500    SER A  62     -144.78   -155.44                                   
REMARK 500    THR A  63       12.44    -63.32                                   
REMARK 500    ASN A  95       42.46   -147.28                                   
REMARK 500    ASN A 123      -37.61   -130.62                                   
REMARK 500    HIS A 153      -53.49   -134.42                                   
REMARK 500    ASN A 207      -87.68   -122.71                                   
REMARK 500    PHE A 211      -24.32     80.79                                   
REMARK 500    ARG A 295       32.10    -95.79                                   
REMARK 500    MET A 297       -2.48     81.65                                   
REMARK 500    THR A 330      -33.31   -130.15                                   
REMARK 500    VAL A 331        5.69     41.81                                   
REMARK 500    VAL A 332      -63.14    -27.97                                   
REMARK 500    ASP A 357       85.12   -155.04                                   
REMARK 500    VAL A 369       54.52     35.65                                   
REMARK 500    GLU S  13     -145.83     63.55                                   
REMARK 500    LEU S  15       -5.50     85.29                                   
REMARK 500    LYS S  71     -128.03     58.59                                   
REMARK 500    SER S 114      111.40   -172.09                                   
REMARK 500    PRO S 120     -166.69    -51.46                                   
REMARK 500    LYS B  14      -68.74   -100.88                                   
REMARK 500    THR B  23      -34.74   -144.79                                   
REMARK 500    SER B  62     -111.78   -150.67                                   
REMARK 500    VAL B  91      105.50    -50.03                                   
REMARK 500    ASN B  95       39.10   -161.75                                   
REMARK 500    HIS B 153      -52.99   -136.36                                   
REMARK 500    ASN B 207      -87.31   -122.70                                   
REMARK 500    PHE B 211      -20.73     80.34                                   
REMARK 500    MET B 212       86.27   -150.19                                   
REMARK 500    ARG B 295       31.77    -93.11                                   
REMARK 500    MET B 297       -1.42     79.43                                   
REMARK 500    THR B 330       -9.46   -143.82                                   
REMARK 500    ASP B 357       89.78   -164.71                                   
REMARK 500    VAL B 369       58.29     32.83                                   
REMARK 500    GLU T  13     -148.30     63.40                                   
REMARK 500    LEU T  15       -7.59     85.64                                   
REMARK 500    LYS T  71     -129.88     60.95                                   
REMARK 500    LEU T 112       11.66   -143.99                                   
REMARK 500    SER T 114      112.94   -173.48                                   
REMARK 500    THR C  23      -27.30   -149.09                                   
REMARK 500    SER C  62     -119.88   -146.95                                   
REMARK 500    ASN C  95       32.42   -173.07                                   
REMARK 500    HIS C 153      -53.04   -135.63                                   
REMARK 500    ASN C 207      -86.04   -123.58                                   
REMARK 500    PHE C 211      -21.98     82.79                                   
REMARK 500    ARG C 295       30.68    -92.35                                   
REMARK 500    MET C 297       -3.77     80.46                                   
REMARK 500    THR C 330      -37.54   -133.77                                   
REMARK 500    VAL C 331      -20.11     52.14                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     150 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A 332        24.1      L          L   OUTSIDE RANGE           
REMARK 500    ALA B  15        22.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2798        DISTANCE =  7.02 ANGSTROMS                       
REMARK 525    HOH E2272        DISTANCE =  7.10 ANGSTROMS                       
REMARK 525    HOH H1955        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH T2323        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH U2096        DISTANCE =  5.57 ANGSTROMS                       
REMARK 525    HOH U2318        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH X2374        DISTANCE =  5.05 ANGSTROMS                       
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 G 478  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G 203   OD1                                                    
REMARK 620 2 6PG G 479   O1A  92.3                                              
REMARK 620 3 KCX G 201   OQ1  93.2 102.3                                        
REMARK 620 4 GLU G 204   OE1  93.4 173.6  80.2                                  
REMARK 620 5 6PG G 479   O2  169.2  77.2  87.1  97.2                            
REMARK 620 6 HOH G1909   O    93.8  90.2 165.4  86.6  88.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 478  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 203   OD2                                                    
REMARK 620 2 6PG A 479   O1   93.4                                              
REMARK 620 3 KCX A 201   OQ1  92.6  98.1                                        
REMARK 620 4 GLU A 204   OE1  94.2 172.3  82.4                                  
REMARK 620 5 6PG A 479   O2  167.9  74.7  87.2  97.7                            
REMARK 620 6 HOH A2934   O    98.2  90.8 165.6  87.3  84.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 478  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 6PG D 479   O1A                                                    
REMARK 620 2 ASP D 203   OD2  92.1                                              
REMARK 620 3 KCX D 201   OQ1 103.0  92.2                                        
REMARK 620 4 GLU D 204   OE1 174.2  92.4  80.5                                  
REMARK 620 5 6PG D 479   O2   76.3 168.3  88.4  99.2                            
REMARK 620 6 HOH D3132   O    88.8  94.7 166.1  87.3  87.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 478  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 203   OD1                                                    
REMARK 620 2 6PG E 479   O1A  93.0                                              
REMARK 620 3 KCX E 201   OQ1  90.5 102.0                                        
REMARK 620 4 GLU E 204   OE1  92.9 173.2  81.4                                  
REMARK 620 5 6PG E 479   O2  167.0  75.1  87.2  99.4                            
REMARK 620 6 HOH E1908   O    95.4  89.5 166.8  86.5  89.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 478  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 6PG B 479   O1A                                                    
REMARK 620 2 KCX B 201   OQ1  99.9                                              
REMARK 620 3 ASP B 203   OD2  90.4  94.1                                        
REMARK 620 4 GLU B 204   OE1 173.4  82.4  95.6                                  
REMARK 620 5 6PG B 479   O2   72.4  96.8 160.9 101.3                            
REMARK 620 6 HOH B2967   O    88.7 170.5  89.6  88.6  82.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 478  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F 204   OE1                                                    
REMARK 620 2 KCX F 201   OQ1  84.5                                              
REMARK 620 3 6PG F 479   O2  102.7  88.7                                        
REMARK 620 4 ASP F 203   OD2  94.1  95.3 163.0                                  
REMARK 620 5 6PG F 479   O1A 173.7 101.2  74.9  88.1                            
REMARK 620 6 HOH F2817   O    86.5 170.2  89.6  89.1  87.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 478  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX H 201   OQ1                                                    
REMARK 620 2 ASP H 203   OD2  91.8                                              
REMARK 620 3 6PG H 479   O1A 100.2  91.3                                        
REMARK 620 4 6PG H 479   O2   89.3 166.6  75.4                                  
REMARK 620 5 GLU H 204   OE2  81.7  92.4 175.9 101.1                            
REMARK 620 6 HOH H3197   O   167.5  94.3  90.6  87.3  87.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 478  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 6PG C 479   O1A                                                    
REMARK 620 2 6PG C 479   O2   78.4                                              
REMARK 620 3 ASP C 203   OD2  88.3 164.4                                        
REMARK 620 4 GLU C 204   OE1 177.9 100.0  93.5                                  
REMARK 620 5 KCX C 201   OQ1 100.8  84.7  89.9  80.2                            
REMARK 620 6 HOH C 481   O    91.1  91.8  96.6  87.7 166.6                      
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 A 478                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6PG A 479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 478                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6PG B 479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 478                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6PG C 479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 478                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6PG D 479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 478                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6PG E 479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 478                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6PG F 479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 478                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6PG G 479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 478                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6PG H 479                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1WDD   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF RICE RUBISCO IN COMPLEX WITH CABP                       
REMARK 900 RELATED ID: 3AXK   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF RICE RUBISCO IN COMPLEX WITH NADP(H)                    
DBREF  3AXM A    1   477  UNP    P0C512   RBL_ORYSJ        1    477             
DBREF  3AXM S    1   129  UNP    Q0INY7   RBS1_ORYSJ      48    175             
DBREF  3AXM B    1   477  UNP    P0C512   RBL_ORYSJ        1    477             
DBREF  3AXM T    1   129  UNP    Q0INY7   RBS1_ORYSJ      48    175             
DBREF  3AXM C    1   477  UNP    P0C512   RBL_ORYSJ        1    477             
DBREF  3AXM U    1   129  UNP    Q0INY7   RBS1_ORYSJ      48    175             
DBREF  3AXM D    1   477  UNP    P0C512   RBL_ORYSJ        1    477             
DBREF  3AXM V    1   129  UNP    Q0INY7   RBS1_ORYSJ      48    175             
DBREF  3AXM E    1   477  UNP    P0C512   RBL_ORYSJ        1    477             
DBREF  3AXM W    1   129  UNP    Q0INY7   RBS1_ORYSJ      48    175             
DBREF  3AXM F    1   477  UNP    P0C512   RBL_ORYSJ        1    477             
DBREF  3AXM X    1   129  UNP    Q0INY7   RBS1_ORYSJ      48    175             
DBREF  3AXM G    1   477  UNP    P0C512   RBL_ORYSJ        1    477             
DBREF  3AXM Y    1   129  UNP    Q0INY7   RBS1_ORYSJ      48    175             
DBREF  3AXM H    1   477  UNP    P0C512   RBL_ORYSJ        1    477             
DBREF  3AXM Z    1   129  UNP    Q0INY7   RBS1_ORYSJ      48    175             
SEQADV 3AXM NME S    0  UNP  Q0INY7              AMIDATION                      
SEQADV 3AXM NME T    0  UNP  Q0INY7              AMIDATION                      
SEQADV 3AXM NME U    0  UNP  Q0INY7              AMIDATION                      
SEQADV 3AXM NME V    0  UNP  Q0INY7              AMIDATION                      
SEQADV 3AXM NME W    0  UNP  Q0INY7              AMIDATION                      
SEQADV 3AXM NME X    0  UNP  Q0INY7              AMIDATION                      
SEQADV 3AXM NME Y    0  UNP  Q0INY7              AMIDATION                      
SEQADV 3AXM NME Z    0  UNP  Q0INY7              AMIDATION                      
SEQRES   1 A  477  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY PHE          
SEQRES   2 A  477  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR          
SEQRES   3 A  477  PRO GLU TYR GLU THR LYS ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 A  477  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 A  477  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 A  477  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 A  477  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL VAL          
SEQRES   8 A  477  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR PRO          
SEQRES   9 A  477  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 A  477  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 A  477  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO THR          
SEQRES  12 A  477  TYR SER LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN          
SEQRES  13 A  477  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU          
SEQRES  14 A  477  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 A  477  LYS ASN TYR GLY ARG ALA CYS TYR GLU CYS LEU ARG GLY          
SEQRES  16 A  477  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 A  477  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE VAL PHE CYS          
SEQRES  18 A  477  ALA GLU ALA ILE TYR LYS SER GLN ALA GLU THR GLY GLU          
SEQRES  19 A  477  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 A  477  GLU GLU MET ILE LYS ARG ALA VAL PHE ALA ARG GLU LEU          
SEQRES  21 A  477  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 A  477  PHE THR ALA ASN THR SER LEU ALA HIS TYR CYS ARG ASP          
SEQRES  23 A  477  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 A  477  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG          
SEQRES  25 A  477  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 A  477  ILE HIS ALA GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 A  477  ARG GLU MET THR LEU GLY PHE VAL ASP LEU LEU ARG ASP          
SEQRES  28 A  477  ASP PHE ILE GLU LYS ASP ARG ALA ARG GLY ILE PHE PHE          
SEQRES  29 A  477  THR GLN ASP TRP VAL SER MET PRO GLY VAL ILE PRO VAL          
SEQRES  30 A  477  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 A  477  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY          
SEQRES  32 A  477  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 A  477  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN          
SEQRES  34 A  477  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN          
SEQRES  35 A  477  GLU ILE ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 A  477  ALA ALA ALA CYS GLU ILE TRP LYS ALA ILE LYS PHE GLU          
SEQRES  37 A  477  PHE GLU PRO VAL ASP LYS LEU ASP SER                          
SEQRES   1 S  129  NME MET GLN VAL TRP PRO ILE GLU GLY ILE LYS LYS PHE          
SEQRES   2 S  129  GLU THR LEU SER TYR LEU PRO PRO LEU THR VAL GLU ASP          
SEQRES   3 S  129  LEU LEU LYS GLN ILE GLU TYR LEU LEU ARG SER LYS TRP          
SEQRES   4 S  129  VAL PRO CYS LEU GLU PHE SER LYS VAL GLY PHE VAL TYR          
SEQRES   5 S  129  ARG GLU ASN HIS ARG SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 S  129  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR          
SEQRES   7 S  129  ASP ALA THR GLN VAL LEU LYS GLU LEU GLU GLU ALA LYS          
SEQRES   8 S  129  LYS ALA TYR PRO ASP ALA PHE VAL ARG ILE ILE GLY PHE          
SEQRES   9 S  129  ASP ASN VAL ARG GLN VAL GLN LEU ILE SER PHE ILE ALA          
SEQRES  10 S  129  TYR LYS PRO PRO GLY CYS GLU GLU SER GLY GLY ASN              
SEQRES   1 B  477  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY PHE          
SEQRES   2 B  477  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR          
SEQRES   3 B  477  PRO GLU TYR GLU THR LYS ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 B  477  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 B  477  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 B  477  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 B  477  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL VAL          
SEQRES   8 B  477  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR PRO          
SEQRES   9 B  477  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 B  477  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 B  477  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO THR          
SEQRES  12 B  477  TYR SER LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN          
SEQRES  13 B  477  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU          
SEQRES  14 B  477  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 B  477  LYS ASN TYR GLY ARG ALA CYS TYR GLU CYS LEU ARG GLY          
SEQRES  16 B  477  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 B  477  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE VAL PHE CYS          
SEQRES  18 B  477  ALA GLU ALA ILE TYR LYS SER GLN ALA GLU THR GLY GLU          
SEQRES  19 B  477  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 B  477  GLU GLU MET ILE LYS ARG ALA VAL PHE ALA ARG GLU LEU          
SEQRES  21 B  477  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 B  477  PHE THR ALA ASN THR SER LEU ALA HIS TYR CYS ARG ASP          
SEQRES  23 B  477  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 B  477  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG          
SEQRES  25 B  477  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 B  477  ILE HIS ALA GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 B  477  ARG GLU MET THR LEU GLY PHE VAL ASP LEU LEU ARG ASP          
SEQRES  28 B  477  ASP PHE ILE GLU LYS ASP ARG ALA ARG GLY ILE PHE PHE          
SEQRES  29 B  477  THR GLN ASP TRP VAL SER MET PRO GLY VAL ILE PRO VAL          
SEQRES  30 B  477  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 B  477  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY          
SEQRES  32 B  477  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 B  477  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN          
SEQRES  34 B  477  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN          
SEQRES  35 B  477  GLU ILE ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 B  477  ALA ALA ALA CYS GLU ILE TRP LYS ALA ILE LYS PHE GLU          
SEQRES  37 B  477  PHE GLU PRO VAL ASP LYS LEU ASP SER                          
SEQRES   1 T  129  NME MET GLN VAL TRP PRO ILE GLU GLY ILE LYS LYS PHE          
SEQRES   2 T  129  GLU THR LEU SER TYR LEU PRO PRO LEU THR VAL GLU ASP          
SEQRES   3 T  129  LEU LEU LYS GLN ILE GLU TYR LEU LEU ARG SER LYS TRP          
SEQRES   4 T  129  VAL PRO CYS LEU GLU PHE SER LYS VAL GLY PHE VAL TYR          
SEQRES   5 T  129  ARG GLU ASN HIS ARG SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 T  129  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR          
SEQRES   7 T  129  ASP ALA THR GLN VAL LEU LYS GLU LEU GLU GLU ALA LYS          
SEQRES   8 T  129  LYS ALA TYR PRO ASP ALA PHE VAL ARG ILE ILE GLY PHE          
SEQRES   9 T  129  ASP ASN VAL ARG GLN VAL GLN LEU ILE SER PHE ILE ALA          
SEQRES  10 T  129  TYR LYS PRO PRO GLY CYS GLU GLU SER GLY GLY ASN              
SEQRES   1 C  477  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY PHE          
SEQRES   2 C  477  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR          
SEQRES   3 C  477  PRO GLU TYR GLU THR LYS ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 C  477  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 C  477  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 C  477  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 C  477  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL VAL          
SEQRES   8 C  477  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR PRO          
SEQRES   9 C  477  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 C  477  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 C  477  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO THR          
SEQRES  12 C  477  TYR SER LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN          
SEQRES  13 C  477  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU          
SEQRES  14 C  477  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 C  477  LYS ASN TYR GLY ARG ALA CYS TYR GLU CYS LEU ARG GLY          
SEQRES  16 C  477  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 C  477  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE VAL PHE CYS          
SEQRES  18 C  477  ALA GLU ALA ILE TYR LYS SER GLN ALA GLU THR GLY GLU          
SEQRES  19 C  477  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 C  477  GLU GLU MET ILE LYS ARG ALA VAL PHE ALA ARG GLU LEU          
SEQRES  21 C  477  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 C  477  PHE THR ALA ASN THR SER LEU ALA HIS TYR CYS ARG ASP          
SEQRES  23 C  477  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 C  477  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG          
SEQRES  25 C  477  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 C  477  ILE HIS ALA GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 C  477  ARG GLU MET THR LEU GLY PHE VAL ASP LEU LEU ARG ASP          
SEQRES  28 C  477  ASP PHE ILE GLU LYS ASP ARG ALA ARG GLY ILE PHE PHE          
SEQRES  29 C  477  THR GLN ASP TRP VAL SER MET PRO GLY VAL ILE PRO VAL          
SEQRES  30 C  477  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 C  477  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY          
SEQRES  32 C  477  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 C  477  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN          
SEQRES  34 C  477  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN          
SEQRES  35 C  477  GLU ILE ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 C  477  ALA ALA ALA CYS GLU ILE TRP LYS ALA ILE LYS PHE GLU          
SEQRES  37 C  477  PHE GLU PRO VAL ASP LYS LEU ASP SER                          
SEQRES   1 U  129  NME MET GLN VAL TRP PRO ILE GLU GLY ILE LYS LYS PHE          
SEQRES   2 U  129  GLU THR LEU SER TYR LEU PRO PRO LEU THR VAL GLU ASP          
SEQRES   3 U  129  LEU LEU LYS GLN ILE GLU TYR LEU LEU ARG SER LYS TRP          
SEQRES   4 U  129  VAL PRO CYS LEU GLU PHE SER LYS VAL GLY PHE VAL TYR          
SEQRES   5 U  129  ARG GLU ASN HIS ARG SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 U  129  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR          
SEQRES   7 U  129  ASP ALA THR GLN VAL LEU LYS GLU LEU GLU GLU ALA LYS          
SEQRES   8 U  129  LYS ALA TYR PRO ASP ALA PHE VAL ARG ILE ILE GLY PHE          
SEQRES   9 U  129  ASP ASN VAL ARG GLN VAL GLN LEU ILE SER PHE ILE ALA          
SEQRES  10 U  129  TYR LYS PRO PRO GLY CYS GLU GLU SER GLY GLY ASN              
SEQRES   1 D  477  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY PHE          
SEQRES   2 D  477  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR          
SEQRES   3 D  477  PRO GLU TYR GLU THR LYS ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 D  477  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 D  477  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 D  477  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 D  477  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL VAL          
SEQRES   8 D  477  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR PRO          
SEQRES   9 D  477  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 D  477  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 D  477  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO THR          
SEQRES  12 D  477  TYR SER LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN          
SEQRES  13 D  477  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU          
SEQRES  14 D  477  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 D  477  LYS ASN TYR GLY ARG ALA CYS TYR GLU CYS LEU ARG GLY          
SEQRES  16 D  477  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 D  477  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE VAL PHE CYS          
SEQRES  18 D  477  ALA GLU ALA ILE TYR LYS SER GLN ALA GLU THR GLY GLU          
SEQRES  19 D  477  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 D  477  GLU GLU MET ILE LYS ARG ALA VAL PHE ALA ARG GLU LEU          
SEQRES  21 D  477  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 D  477  PHE THR ALA ASN THR SER LEU ALA HIS TYR CYS ARG ASP          
SEQRES  23 D  477  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 D  477  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG          
SEQRES  25 D  477  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 D  477  ILE HIS ALA GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 D  477  ARG GLU MET THR LEU GLY PHE VAL ASP LEU LEU ARG ASP          
SEQRES  28 D  477  ASP PHE ILE GLU LYS ASP ARG ALA ARG GLY ILE PHE PHE          
SEQRES  29 D  477  THR GLN ASP TRP VAL SER MET PRO GLY VAL ILE PRO VAL          
SEQRES  30 D  477  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 D  477  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY          
SEQRES  32 D  477  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 D  477  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN          
SEQRES  34 D  477  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN          
SEQRES  35 D  477  GLU ILE ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 D  477  ALA ALA ALA CYS GLU ILE TRP LYS ALA ILE LYS PHE GLU          
SEQRES  37 D  477  PHE GLU PRO VAL ASP LYS LEU ASP SER                          
SEQRES   1 V  129  NME MET GLN VAL TRP PRO ILE GLU GLY ILE LYS LYS PHE          
SEQRES   2 V  129  GLU THR LEU SER TYR LEU PRO PRO LEU THR VAL GLU ASP          
SEQRES   3 V  129  LEU LEU LYS GLN ILE GLU TYR LEU LEU ARG SER LYS TRP          
SEQRES   4 V  129  VAL PRO CYS LEU GLU PHE SER LYS VAL GLY PHE VAL TYR          
SEQRES   5 V  129  ARG GLU ASN HIS ARG SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 V  129  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR          
SEQRES   7 V  129  ASP ALA THR GLN VAL LEU LYS GLU LEU GLU GLU ALA LYS          
SEQRES   8 V  129  LYS ALA TYR PRO ASP ALA PHE VAL ARG ILE ILE GLY PHE          
SEQRES   9 V  129  ASP ASN VAL ARG GLN VAL GLN LEU ILE SER PHE ILE ALA          
SEQRES  10 V  129  TYR LYS PRO PRO GLY CYS GLU GLU SER GLY GLY ASN              
SEQRES   1 E  477  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY PHE          
SEQRES   2 E  477  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR          
SEQRES   3 E  477  PRO GLU TYR GLU THR LYS ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 E  477  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 E  477  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 E  477  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 E  477  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL VAL          
SEQRES   8 E  477  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR PRO          
SEQRES   9 E  477  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 E  477  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 E  477  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO THR          
SEQRES  12 E  477  TYR SER LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN          
SEQRES  13 E  477  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU          
SEQRES  14 E  477  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 E  477  LYS ASN TYR GLY ARG ALA CYS TYR GLU CYS LEU ARG GLY          
SEQRES  16 E  477  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 E  477  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE VAL PHE CYS          
SEQRES  18 E  477  ALA GLU ALA ILE TYR LYS SER GLN ALA GLU THR GLY GLU          
SEQRES  19 E  477  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 E  477  GLU GLU MET ILE LYS ARG ALA VAL PHE ALA ARG GLU LEU          
SEQRES  21 E  477  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 E  477  PHE THR ALA ASN THR SER LEU ALA HIS TYR CYS ARG ASP          
SEQRES  23 E  477  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 E  477  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG          
SEQRES  25 E  477  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 E  477  ILE HIS ALA GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 E  477  ARG GLU MET THR LEU GLY PHE VAL ASP LEU LEU ARG ASP          
SEQRES  28 E  477  ASP PHE ILE GLU LYS ASP ARG ALA ARG GLY ILE PHE PHE          
SEQRES  29 E  477  THR GLN ASP TRP VAL SER MET PRO GLY VAL ILE PRO VAL          
SEQRES  30 E  477  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 E  477  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY          
SEQRES  32 E  477  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 E  477  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN          
SEQRES  34 E  477  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN          
SEQRES  35 E  477  GLU ILE ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 E  477  ALA ALA ALA CYS GLU ILE TRP LYS ALA ILE LYS PHE GLU          
SEQRES  37 E  477  PHE GLU PRO VAL ASP LYS LEU ASP SER                          
SEQRES   1 W  129  NME MET GLN VAL TRP PRO ILE GLU GLY ILE LYS LYS PHE          
SEQRES   2 W  129  GLU THR LEU SER TYR LEU PRO PRO LEU THR VAL GLU ASP          
SEQRES   3 W  129  LEU LEU LYS GLN ILE GLU TYR LEU LEU ARG SER LYS TRP          
SEQRES   4 W  129  VAL PRO CYS LEU GLU PHE SER LYS VAL GLY PHE VAL TYR          
SEQRES   5 W  129  ARG GLU ASN HIS ARG SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 W  129  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR          
SEQRES   7 W  129  ASP ALA THR GLN VAL LEU LYS GLU LEU GLU GLU ALA LYS          
SEQRES   8 W  129  LYS ALA TYR PRO ASP ALA PHE VAL ARG ILE ILE GLY PHE          
SEQRES   9 W  129  ASP ASN VAL ARG GLN VAL GLN LEU ILE SER PHE ILE ALA          
SEQRES  10 W  129  TYR LYS PRO PRO GLY CYS GLU GLU SER GLY GLY ASN              
SEQRES   1 F  477  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY PHE          
SEQRES   2 F  477  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR          
SEQRES   3 F  477  PRO GLU TYR GLU THR LYS ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 F  477  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 F  477  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 F  477  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 F  477  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL VAL          
SEQRES   8 F  477  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR PRO          
SEQRES   9 F  477  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 F  477  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 F  477  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO THR          
SEQRES  12 F  477  TYR SER LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN          
SEQRES  13 F  477  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU          
SEQRES  14 F  477  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 F  477  LYS ASN TYR GLY ARG ALA CYS TYR GLU CYS LEU ARG GLY          
SEQRES  16 F  477  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 F  477  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE VAL PHE CYS          
SEQRES  18 F  477  ALA GLU ALA ILE TYR LYS SER GLN ALA GLU THR GLY GLU          
SEQRES  19 F  477  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 F  477  GLU GLU MET ILE LYS ARG ALA VAL PHE ALA ARG GLU LEU          
SEQRES  21 F  477  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 F  477  PHE THR ALA ASN THR SER LEU ALA HIS TYR CYS ARG ASP          
SEQRES  23 F  477  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 F  477  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG          
SEQRES  25 F  477  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 F  477  ILE HIS ALA GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 F  477  ARG GLU MET THR LEU GLY PHE VAL ASP LEU LEU ARG ASP          
SEQRES  28 F  477  ASP PHE ILE GLU LYS ASP ARG ALA ARG GLY ILE PHE PHE          
SEQRES  29 F  477  THR GLN ASP TRP VAL SER MET PRO GLY VAL ILE PRO VAL          
SEQRES  30 F  477  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 F  477  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY          
SEQRES  32 F  477  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 F  477  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN          
SEQRES  34 F  477  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN          
SEQRES  35 F  477  GLU ILE ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 F  477  ALA ALA ALA CYS GLU ILE TRP LYS ALA ILE LYS PHE GLU          
SEQRES  37 F  477  PHE GLU PRO VAL ASP LYS LEU ASP SER                          
SEQRES   1 X  129  NME MET GLN VAL TRP PRO ILE GLU GLY ILE LYS LYS PHE          
SEQRES   2 X  129  GLU THR LEU SER TYR LEU PRO PRO LEU THR VAL GLU ASP          
SEQRES   3 X  129  LEU LEU LYS GLN ILE GLU TYR LEU LEU ARG SER LYS TRP          
SEQRES   4 X  129  VAL PRO CYS LEU GLU PHE SER LYS VAL GLY PHE VAL TYR          
SEQRES   5 X  129  ARG GLU ASN HIS ARG SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 X  129  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR          
SEQRES   7 X  129  ASP ALA THR GLN VAL LEU LYS GLU LEU GLU GLU ALA LYS          
SEQRES   8 X  129  LYS ALA TYR PRO ASP ALA PHE VAL ARG ILE ILE GLY PHE          
SEQRES   9 X  129  ASP ASN VAL ARG GLN VAL GLN LEU ILE SER PHE ILE ALA          
SEQRES  10 X  129  TYR LYS PRO PRO GLY CYS GLU GLU SER GLY GLY ASN              
SEQRES   1 G  477  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY PHE          
SEQRES   2 G  477  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR          
SEQRES   3 G  477  PRO GLU TYR GLU THR LYS ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 G  477  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 G  477  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 G  477  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 G  477  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL VAL          
SEQRES   8 G  477  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR PRO          
SEQRES   9 G  477  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 G  477  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 G  477  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO THR          
SEQRES  12 G  477  TYR SER LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN          
SEQRES  13 G  477  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU          
SEQRES  14 G  477  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 G  477  LYS ASN TYR GLY ARG ALA CYS TYR GLU CYS LEU ARG GLY          
SEQRES  16 G  477  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 G  477  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE VAL PHE CYS          
SEQRES  18 G  477  ALA GLU ALA ILE TYR LYS SER GLN ALA GLU THR GLY GLU          
SEQRES  19 G  477  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 G  477  GLU GLU MET ILE LYS ARG ALA VAL PHE ALA ARG GLU LEU          
SEQRES  21 G  477  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 G  477  PHE THR ALA ASN THR SER LEU ALA HIS TYR CYS ARG ASP          
SEQRES  23 G  477  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 G  477  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG          
SEQRES  25 G  477  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 G  477  ILE HIS ALA GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 G  477  ARG GLU MET THR LEU GLY PHE VAL ASP LEU LEU ARG ASP          
SEQRES  28 G  477  ASP PHE ILE GLU LYS ASP ARG ALA ARG GLY ILE PHE PHE          
SEQRES  29 G  477  THR GLN ASP TRP VAL SER MET PRO GLY VAL ILE PRO VAL          
SEQRES  30 G  477  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 G  477  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY          
SEQRES  32 G  477  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 G  477  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN          
SEQRES  34 G  477  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN          
SEQRES  35 G  477  GLU ILE ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 G  477  ALA ALA ALA CYS GLU ILE TRP LYS ALA ILE LYS PHE GLU          
SEQRES  37 G  477  PHE GLU PRO VAL ASP LYS LEU ASP SER                          
SEQRES   1 Y  129  NME MET GLN VAL TRP PRO ILE GLU GLY ILE LYS LYS PHE          
SEQRES   2 Y  129  GLU THR LEU SER TYR LEU PRO PRO LEU THR VAL GLU ASP          
SEQRES   3 Y  129  LEU LEU LYS GLN ILE GLU TYR LEU LEU ARG SER LYS TRP          
SEQRES   4 Y  129  VAL PRO CYS LEU GLU PHE SER LYS VAL GLY PHE VAL TYR          
SEQRES   5 Y  129  ARG GLU ASN HIS ARG SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 Y  129  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR          
SEQRES   7 Y  129  ASP ALA THR GLN VAL LEU LYS GLU LEU GLU GLU ALA LYS          
SEQRES   8 Y  129  LYS ALA TYR PRO ASP ALA PHE VAL ARG ILE ILE GLY PHE          
SEQRES   9 Y  129  ASP ASN VAL ARG GLN VAL GLN LEU ILE SER PHE ILE ALA          
SEQRES  10 Y  129  TYR LYS PRO PRO GLY CYS GLU GLU SER GLY GLY ASN              
SEQRES   1 H  477  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY PHE          
SEQRES   2 H  477  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR          
SEQRES   3 H  477  PRO GLU TYR GLU THR LYS ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 H  477  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 H  477  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 H  477  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 H  477  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL VAL          
SEQRES   8 H  477  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR PRO          
SEQRES   9 H  477  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 H  477  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 H  477  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO THR          
SEQRES  12 H  477  TYR SER LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN          
SEQRES  13 H  477  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU          
SEQRES  14 H  477  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 H  477  LYS ASN TYR GLY ARG ALA CYS TYR GLU CYS LEU ARG GLY          
SEQRES  16 H  477  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 H  477  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE VAL PHE CYS          
SEQRES  18 H  477  ALA GLU ALA ILE TYR LYS SER GLN ALA GLU THR GLY GLU          
SEQRES  19 H  477  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 H  477  GLU GLU MET ILE LYS ARG ALA VAL PHE ALA ARG GLU LEU          
SEQRES  21 H  477  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 H  477  PHE THR ALA ASN THR SER LEU ALA HIS TYR CYS ARG ASP          
SEQRES  23 H  477  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 H  477  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG          
SEQRES  25 H  477  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 H  477  ILE HIS ALA GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 H  477  ARG GLU MET THR LEU GLY PHE VAL ASP LEU LEU ARG ASP          
SEQRES  28 H  477  ASP PHE ILE GLU LYS ASP ARG ALA ARG GLY ILE PHE PHE          
SEQRES  29 H  477  THR GLN ASP TRP VAL SER MET PRO GLY VAL ILE PRO VAL          
SEQRES  30 H  477  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 H  477  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY          
SEQRES  32 H  477  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 H  477  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN          
SEQRES  34 H  477  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN          
SEQRES  35 H  477  GLU ILE ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 H  477  ALA ALA ALA CYS GLU ILE TRP LYS ALA ILE LYS PHE GLU          
SEQRES  37 H  477  PHE GLU PRO VAL ASP LYS LEU ASP SER                          
SEQRES   1 Z  129  NME MET GLN VAL TRP PRO ILE GLU GLY ILE LYS LYS PHE          
SEQRES   2 Z  129  GLU THR LEU SER TYR LEU PRO PRO LEU THR VAL GLU ASP          
SEQRES   3 Z  129  LEU LEU LYS GLN ILE GLU TYR LEU LEU ARG SER LYS TRP          
SEQRES   4 Z  129  VAL PRO CYS LEU GLU PHE SER LYS VAL GLY PHE VAL TYR          
SEQRES   5 Z  129  ARG GLU ASN HIS ARG SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 Z  129  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR          
SEQRES   7 Z  129  ASP ALA THR GLN VAL LEU LYS GLU LEU GLU GLU ALA LYS          
SEQRES   8 Z  129  LYS ALA TYR PRO ASP ALA PHE VAL ARG ILE ILE GLY PHE          
SEQRES   9 Z  129  ASP ASN VAL ARG GLN VAL GLN LEU ILE SER PHE ILE ALA          
SEQRES  10 Z  129  TYR LYS PRO PRO GLY CYS GLU GLU SER GLY GLY ASN              
MODRES 3AXM KCX A  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3AXM KCX B  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3AXM KCX C  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3AXM KCX D  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3AXM KCX E  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3AXM KCX F  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3AXM KCX G  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3AXM KCX H  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
HET    KCX  A 201      12                                                       
HET    NME  S   0       1                                                       
HET    KCX  B 201      12                                                       
HET    NME  T   0       1                                                       
HET    KCX  C 201      12                                                       
HET    NME  U   0       1                                                       
HET    KCX  D 201      12                                                       
HET    NME  V   0       1                                                       
HET    KCX  E 201      12                                                       
HET    NME  W   0       1                                                       
HET    KCX  F 201      12                                                       
HET    NME  X   0       1                                                       
HET    KCX  G 201      12                                                       
HET    NME  Y   0       1                                                       
HET    KCX  H 201      12                                                       
HET    NME  Z   0       1                                                       
HET     MG  A 478       1                                                       
HET    6PG  A 479      17                                                       
HET     MG  B 478       1                                                       
HET    6PG  B 479      17                                                       
HET     MG  C 478       1                                                       
HET    6PG  C 479      17                                                       
HET     MG  D 478       1                                                       
HET    6PG  D 479      17                                                       
HET     MG  E 478       1                                                       
HET    6PG  E 479      17                                                       
HET     MG  F 478       1                                                       
HET    6PG  F 479      17                                                       
HET     MG  G 478       1                                                       
HET    6PG  G 479      17                                                       
HET     MG  H 478       1                                                       
HET    6PG  H 479      17                                                       
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM     NME METHYLAMINE                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     6PG 6-PHOSPHOGLUCONIC ACID                                           
FORMUL   1  KCX    8(C7 H14 N2 O4)                                              
FORMUL   2  NME    8(C H5 N)                                                    
FORMUL  17   MG    8(MG 2+)                                                     
FORMUL  18  6PG    8(C6 H13 O10 P)                                              
FORMUL  33  HOH   *3607(H2 O)                                                   
HELIX    1   1 PRO A   49  GLU A   60  1                                  12    
HELIX    2   2 VAL A   69  THR A   75  5                                   7    
HELIX    3   3 SER A   76  TYR A   80  5                                   5    
HELIX    4   4 PRO A  104  PHE A  108  5                                   5    
HELIX    5   5 SER A  112  GLY A  122  1                                  11    
HELIX    6   6 ASN A  123  PHE A  127  5                                   5    
HELIX    7   7 PRO A  141  LYS A  146  1                                   6    
HELIX    8   8 GLY A  154  ASN A  163  1                                  10    
HELIX    9   9 SER A  181  GLY A  195  1                                  15    
HELIX   10  10 ARG A  213  GLY A  233  1                                  21    
HELIX   11  11 THR A  246  GLY A  261  1                                  16    
HELIX   12  12 TYR A  269  GLY A  273  1                                   5    
HELIX   13  13 GLY A  273  GLY A  288  1                                  16    
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 ASP A  357  GLY A  361  5                                   5    
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  GLY A  434  1                                  23    
HELIX   22  22 ASP A  436  LYS A  450  1                                  15    
HELIX   23  23 SER A  452  TRP A  462  1                                  11    
HELIX   24  24 THR S   22  SER S   36  1                                  15    
HELIX   25  25 ASP S   79  TYR S   94  1                                  16    
HELIX   26  26 PRO B   49  GLU B   60  1                                  12    
HELIX   27  27 VAL B   69  THR B   75  5                                   7    
HELIX   28  28 SER B   76  TYR B   80  5                                   5    
HELIX   29  29 PRO B  104  PHE B  108  5                                   5    
HELIX   30  30 SER B  112  GLY B  122  1                                  11    
HELIX   31  31 ASN B  123  PHE B  127  5                                   5    
HELIX   32  32 PRO B  141  LYS B  146  1                                   6    
HELIX   33  33 GLY B  154  ASN B  163  1                                  10    
HELIX   34  34 SER B  181  GLY B  195  1                                  15    
HELIX   35  35 ARG B  213  GLY B  233  1                                  21    
HELIX   36  36 THR B  246  GLY B  261  1                                  16    
HELIX   37  37 TYR B  269  GLY B  273  1                                   5    
HELIX   38  38 GLY B  273  GLY B  288  1                                  16    
HELIX   39  39 MET B  297  ARG B  303  1                                   7    
HELIX   40  40 HIS B  310  GLY B  322  1                                  13    
HELIX   41  41 GLU B  338  ASP B  351  1                                  14    
HELIX   42  42 ASP B  357  GLY B  361  5                                   5    
HELIX   43  43 HIS B  383  TRP B  385  5                                   3    
HELIX   44  44 HIS B  386  GLY B  395  1                                  10    
HELIX   45  45 GLY B  403  GLY B  408  1                                   6    
HELIX   46  46 GLY B  412  GLY B  434  1                                  23    
HELIX   47  47 ASP B  436  LYS B  450  1                                  15    
HELIX   48  48 SER B  452  TRP B  462  1                                  11    
HELIX   49  49 THR T   22  SER T   36  1                                  15    
HELIX   50  50 ASP T   79  TYR T   94  1                                  16    
HELIX   51  51 PRO C   49  SER C   61  1                                  13    
HELIX   52  52 VAL C   69  THR C   75  5                                   7    
HELIX   53  53 SER C   76  TYR C   80  5                                   5    
HELIX   54  54 PRO C  104  PHE C  108  5                                   5    
HELIX   55  55 SER C  112  GLY C  122  1                                  11    
HELIX   56  56 ASN C  123  PHE C  127  5                                   5    
HELIX   57  57 PRO C  141  LYS C  146  1                                   6    
HELIX   58  58 GLY C  154  ASN C  163  1                                  10    
HELIX   59  59 SER C  181  GLY C  195  1                                  15    
HELIX   60  60 ARG C  213  GLY C  233  1                                  21    
HELIX   61  61 THR C  246  GLY C  261  1                                  16    
HELIX   62  62 TYR C  269  GLY C  273  1                                   5    
HELIX   63  63 GLY C  273  GLY C  288  1                                  16    
HELIX   64  64 MET C  297  ARG C  303  1                                   7    
HELIX   65  65 HIS C  310  GLY C  322  1                                  13    
HELIX   66  66 GLU C  338  ASP C  351  1                                  14    
HELIX   67  67 ASP C  357  GLY C  361  5                                   5    
HELIX   68  68 HIS C  383  TRP C  385  5                                   3    
HELIX   69  69 HIS C  386  GLY C  395  1                                  10    
HELIX   70  70 GLY C  403  GLY C  408  1                                   6    
HELIX   71  71 GLY C  412  GLY C  434  1                                  23    
HELIX   72  72 ASP C  436  LYS C  450  1                                  15    
HELIX   73  73 SER C  452  TRP C  462  1                                  11    
HELIX   74  74 THR U   22  SER U   36  1                                  15    
HELIX   75  75 ASP U   79  TYR U   94  1                                  16    
HELIX   76  76 PRO D   49  GLU D   60  1                                  12    
HELIX   77  77 VAL D   69  THR D   75  5                                   7    
HELIX   78  78 SER D   76  TYR D   80  5                                   5    
HELIX   79  79 PRO D  104  PHE D  108  5                                   5    
HELIX   80  80 SER D  112  GLY D  122  1                                  11    
HELIX   81  81 ASN D  123  PHE D  127  5                                   5    
HELIX   82  82 PRO D  141  LYS D  146  1                                   6    
HELIX   83  83 GLY D  154  ASN D  163  1                                  10    
HELIX   84  84 SER D  181  GLY D  195  1                                  15    
HELIX   85  85 ARG D  213  GLY D  233  1                                  21    
HELIX   86  86 THR D  246  GLY D  261  1                                  16    
HELIX   87  87 TYR D  269  GLY D  273  1                                   5    
HELIX   88  88 GLY D  273  GLY D  288  1                                  16    
HELIX   89  89 MET D  297  ARG D  303  1                                   7    
HELIX   90  90 HIS D  310  GLY D  322  1                                  13    
HELIX   91  91 GLU D  338  ASP D  351  1                                  14    
HELIX   92  92 ASP D  357  GLY D  361  5                                   5    
HELIX   93  93 HIS D  383  TRP D  385  5                                   3    
HELIX   94  94 HIS D  386  GLY D  395  1                                  10    
HELIX   95  95 GLY D  403  GLY D  408  1                                   6    
HELIX   96  96 GLY D  412  GLU D  433  1                                  22    
HELIX   97  97 ASP D  436  LYS D  450  1                                  15    
HELIX   98  98 SER D  452  TRP D  462  1                                  11    
HELIX   99  99 THR V   22  SER V   36  1                                  15    
HELIX  100 100 ASP V   79  TYR V   94  1                                  16    
HELIX  101 101 PRO E   49  SER E   61  1                                  13    
HELIX  102 102 VAL E   69  THR E   75  5                                   7    
HELIX  103 103 SER E   76  TYR E   80  5                                   5    
HELIX  104 104 PRO E  104  PHE E  108  5                                   5    
HELIX  105 105 SER E  112  GLY E  122  1                                  11    
HELIX  106 106 ASN E  123  PHE E  127  5                                   5    
HELIX  107 107 PRO E  141  LYS E  146  1                                   6    
HELIX  108 108 GLY E  154  ASN E  163  1                                  10    
HELIX  109 109 SER E  181  GLY E  195  1                                  15    
HELIX  110 110 ARG E  213  GLY E  233  1                                  21    
HELIX  111 111 THR E  246  GLY E  261  1                                  16    
HELIX  112 112 TYR E  269  GLY E  273  1                                   5    
HELIX  113 113 GLY E  273  GLY E  288  1                                  16    
HELIX  114 114 MET E  297  ARG E  303  1                                   7    
HELIX  115 115 HIS E  310  GLY E  322  1                                  13    
HELIX  116 116 GLU E  338  ASP E  351  1                                  14    
HELIX  117 117 ASP E  357  GLY E  361  5                                   5    
HELIX  118 118 HIS E  383  TRP E  385  5                                   3    
HELIX  119 119 HIS E  386  GLY E  395  1                                  10    
HELIX  120 120 GLY E  403  GLY E  408  1                                   6    
HELIX  121 121 GLY E  412  GLY E  434  1                                  23    
HELIX  122 122 ASP E  436  SER E  452  1                                  17    
HELIX  123 123 SER E  452  TRP E  462  1                                  11    
HELIX  124 124 THR W   22  SER W   36  1                                  15    
HELIX  125 125 ASP W   79  TYR W   94  1                                  16    
HELIX  126 126 PRO F   49  SER F   61  1                                  13    
HELIX  127 127 VAL F   69  THR F   75  5                                   7    
HELIX  128 128 SER F   76  TYR F   80  5                                   5    
HELIX  129 129 PRO F  104  PHE F  108  5                                   5    
HELIX  130 130 SER F  112  GLY F  122  1                                  11    
HELIX  131 131 ASN F  123  PHE F  127  5                                   5    
HELIX  132 132 PRO F  141  LYS F  146  1                                   6    
HELIX  133 133 GLY F  154  ASN F  163  1                                  10    
HELIX  134 134 SER F  181  GLY F  195  1                                  15    
HELIX  135 135 ARG F  213  GLY F  233  1                                  21    
HELIX  136 136 THR F  246  GLY F  261  1                                  16    
HELIX  137 137 TYR F  269  GLY F  273  1                                   5    
HELIX  138 138 GLY F  273  GLY F  288  1                                  16    
HELIX  139 139 MET F  297  ARG F  303  1                                   7    
HELIX  140 140 HIS F  310  GLY F  322  1                                  13    
HELIX  141 141 GLU F  338  ASP F  351  1                                  14    
HELIX  142 142 ASP F  357  GLY F  361  5                                   5    
HELIX  143 143 HIS F  383  TRP F  385  5                                   3    
HELIX  144 144 HIS F  386  GLY F  395  1                                  10    
HELIX  145 145 GLY F  403  GLY F  408  1                                   6    
HELIX  146 146 GLY F  412  GLU F  433  1                                  22    
HELIX  147 147 ASP F  436  LYS F  450  1                                  15    
HELIX  148 148 SER F  452  TRP F  462  1                                  11    
HELIX  149 149 THR X   22  SER X   36  1                                  15    
HELIX  150 150 ASP X   79  TYR X   94  1                                  16    
HELIX  151 151 PRO G   49  GLU G   60  1                                  12    
HELIX  152 152 VAL G   69  THR G   75  5                                   7    
HELIX  153 153 SER G   76  TYR G   80  5                                   5    
HELIX  154 154 PRO G  104  PHE G  108  5                                   5    
HELIX  155 155 SER G  112  GLY G  122  1                                  11    
HELIX  156 156 ASN G  123  PHE G  127  5                                   5    
HELIX  157 157 PRO G  141  LYS G  146  1                                   6    
HELIX  158 158 GLY G  154  ASN G  163  1                                  10    
HELIX  159 159 SER G  181  GLY G  195  1                                  15    
HELIX  160 160 ARG G  213  GLY G  233  1                                  21    
HELIX  161 161 THR G  246  GLY G  261  1                                  16    
HELIX  162 162 TYR G  269  GLY G  273  1                                   5    
HELIX  163 163 GLY G  273  GLY G  288  1                                  16    
HELIX  164 164 MET G  297  ARG G  303  1                                   7    
HELIX  165 165 HIS G  310  GLY G  322  1                                  13    
HELIX  166 166 GLU G  338  ASP G  351  1                                  14    
HELIX  167 167 ASP G  357  GLY G  361  5                                   5    
HELIX  168 168 HIS G  383  TRP G  385  5                                   3    
HELIX  169 169 HIS G  386  GLY G  395  1                                  10    
HELIX  170 170 GLY G  403  GLY G  408  1                                   6    
HELIX  171 171 GLY G  412  GLY G  434  1                                  23    
HELIX  172 172 ASP G  436  LYS G  450  1                                  15    
HELIX  173 173 SER G  452  TRP G  462  1                                  11    
HELIX  174 174 THR Y   22  SER Y   36  1                                  15    
HELIX  175 175 ASP Y   79  TYR Y   94  1                                  16    
HELIX  176 176 PRO H   49  GLU H   60  1                                  12    
HELIX  177 177 VAL H   69  THR H   75  5                                   7    
HELIX  178 178 SER H   76  TYR H   80  5                                   5    
HELIX  179 179 PRO H  104  PHE H  108  5                                   5    
HELIX  180 180 SER H  112  GLY H  122  1                                  11    
HELIX  181 181 ASN H  123  PHE H  127  5                                   5    
HELIX  182 182 PRO H  141  LYS H  146  1                                   6    
HELIX  183 183 GLY H  154  ASN H  163  1                                  10    
HELIX  184 184 SER H  181  GLY H  195  1                                  15    
HELIX  185 185 ARG H  213  GLY H  233  1                                  21    
HELIX  186 186 THR H  246  GLY H  261  1                                  16    
HELIX  187 187 TYR H  269  GLY H  273  1                                   5    
HELIX  188 188 GLY H  273  GLY H  288  1                                  16    
HELIX  189 189 MET H  297  ARG H  303  1                                   7    
HELIX  190 190 HIS H  310  GLY H  322  1                                  13    
HELIX  191 191 GLU H  338  ASP H  351  1                                  14    
HELIX  192 192 ASP H  357  GLY H  361  5                                   5    
HELIX  193 193 HIS H  383  TRP H  385  5                                   3    
HELIX  194 194 HIS H  386  GLY H  395  1                                  10    
HELIX  195 195 GLY H  403  GLY H  408  1                                   6    
HELIX  196 196 GLY H  412  GLY H  434  1                                  23    
HELIX  197 197 ASP H  436  LYS H  450  1                                  15    
HELIX  198 198 SER H  452  TRP H  462  1                                  11    
HELIX  199 199 THR Z   22  SER Z   36  1                                  15    
HELIX  200 200 ASP Z   79  TYR Z   94  1                                  16    
SHEET    1   A 5 ARG A  83  PRO A  89  0                                        
SHEET    2   A 5 TYR A  97  TYR A 103 -1  O  TYR A 100   N  HIS A  86           
SHEET    3   A 5 ILE A  36  PRO A  44 -1  N  VAL A  42   O  TYR A  97           
SHEET    4   A 5 LEU A 130  ARG A 139 -1  O  ARG A 134   N  ARG A  41           
SHEET    5   A 5 GLY A 308  MET A 309  1  O  GLY A 308   N  LEU A 135           
SHEET    1   B 9 LEU A 169  THR A 173  0                                        
SHEET    2   B 9 PHE A 199  KCX A 201  1  O  PHE A 199   N  LEU A 170           
SHEET    3   B 9 GLY A 237  ASN A 241  1  O  TYR A 239   N  THR A 200           
SHEET    4   B 9 ILE A 264  ASP A 268  1  O  MET A 266   N  LEU A 240           
SHEET    5   B 9 LEU A 290  HIS A 294  1  O  HIS A 292   N  VAL A 265           
SHEET    6   B 9 HIS A 325  GLY A 329  1  N  HIS A 325   O  LEU A 291           
SHEET    7   B 9 ILE A 375  ALA A 378  1  O  VAL A 377   N  ALA A 328           
SHEET    8   B 9 VAL A 399  GLN A 401  1  O  GLN A 401   N  ALA A 378           
SHEET    9   B 9 LEU A 169  THR A 173  1  N  LEU A 169   O  LEU A 400           
SHEET    1   C 2 PHE A 353  ILE A 354  0                                        
SHEET    2   C 2 GLN A 366  ASP A 367 -1  O  GLN A 366   N  ILE A 354           
SHEET    1   D 4 THR S  68  TRP S  70  0                                        
SHEET    2   D 4 VAL S  39  SER S  45 -1  N  LEU S  42   O  TRP S  70           
SHEET    3   D 4 PHE S  98  ASP S 105 -1  O  PHE S  98   N  SER S  45           
SHEET    4   D 4 VAL S 110  TYR S 118 -1  O  PHE S 115   N  ILE S 101           
SHEET    1   E 5 ARG B  83  PRO B  89  0                                        
SHEET    2   E 5 TYR B  97  TYR B 103 -1  O  ILE B  98   N  GLU B  88           
SHEET    3   E 5 ILE B  36  PRO B  44 -1  N  VAL B  42   O  TYR B  97           
SHEET    4   E 5 LEU B 130  ARG B 139 -1  O  ARG B 134   N  ARG B  41           
SHEET    5   E 5 GLY B 308  MET B 309  1  O  GLY B 308   N  LEU B 135           
SHEET    1   F 9 LEU B 169  THR B 173  0                                        
SHEET    2   F 9 PHE B 199  KCX B 201  1  O  KCX B 201   N  CYS B 172           
SHEET    3   F 9 GLY B 237  ASN B 241  1  O  TYR B 239   N  THR B 200           
SHEET    4   F 9 ILE B 264  ASP B 268  1  O  MET B 266   N  LEU B 240           
SHEET    5   F 9 LEU B 290  HIS B 294  1  O  HIS B 292   N  VAL B 265           
SHEET    6   F 9 HIS B 325  GLY B 329  1  N  HIS B 325   O  LEU B 291           
SHEET    7   F 9 ILE B 375  ALA B 378  1  O  VAL B 377   N  ALA B 328           
SHEET    8   F 9 VAL B 399  GLN B 401  1  O  GLN B 401   N  ALA B 378           
SHEET    9   F 9 LEU B 169  THR B 173  1  N  LEU B 169   O  LEU B 400           
SHEET    1   G 2 PHE B 353  ILE B 354  0                                        
SHEET    2   G 2 GLN B 366  ASP B 367 -1  O  GLN B 366   N  ILE B 354           
SHEET    1   H 4 THR T  68  TRP T  70  0                                        
SHEET    2   H 4 VAL T  39  SER T  45 -1  N  LEU T  42   O  TRP T  70           
SHEET    3   H 4 PHE T  98  ASP T 105 -1  O  PHE T  98   N  SER T  45           
SHEET    4   H 4 VAL T 110  TYR T 118 -1  O  PHE T 115   N  ILE T 101           
SHEET    1   I 5 ARG C  83  PRO C  89  0                                        
SHEET    2   I 5 TYR C  97  TYR C 103 -1  O  TYR C 100   N  HIS C  86           
SHEET    3   I 5 ILE C  36  PRO C  44 -1  N  PHE C  40   O  ALA C  99           
SHEET    4   I 5 LEU C 130  ARG C 139 -1  O  ARG C 134   N  ARG C  41           
SHEET    5   I 5 GLY C 308  MET C 309  1  O  GLY C 308   N  LEU C 133           
SHEET    1   J 9 LEU C 169  THR C 173  0                                        
SHEET    2   J 9 PHE C 199  KCX C 201  1  O  PHE C 199   N  LEU C 170           
SHEET    3   J 9 GLY C 237  ASN C 241  1  O  TYR C 239   N  THR C 200           
SHEET    4   J 9 ILE C 264  ASP C 268  1  O  MET C 266   N  LEU C 240           
SHEET    5   J 9 LEU C 290  HIS C 294  1  O  HIS C 292   N  VAL C 265           
SHEET    6   J 9 HIS C 325  GLY C 329  1  N  HIS C 325   O  LEU C 291           
SHEET    7   J 9 ILE C 375  ALA C 378  1  O  VAL C 377   N  ALA C 328           
SHEET    8   J 9 VAL C 399  GLN C 401  1  O  GLN C 401   N  ALA C 378           
SHEET    9   J 9 LEU C 169  THR C 173  1  N  LEU C 169   O  LEU C 400           
SHEET    1   K 2 PHE C 353  ILE C 354  0                                        
SHEET    2   K 2 GLN C 366  ASP C 367 -1  O  GLN C 366   N  ILE C 354           
SHEET    1   L 4 THR U  68  TRP U  70  0                                        
SHEET    2   L 4 VAL U  39  SER U  45 -1  N  LEU U  42   O  TRP U  70           
SHEET    3   L 4 PHE U  98  ASP U 105 -1  O  PHE U  98   N  SER U  45           
SHEET    4   L 4 VAL U 110  TYR U 118 -1  O  PHE U 115   N  ILE U 101           
SHEET    1   M 5 ARG D  83  PRO D  89  0                                        
SHEET    2   M 5 TYR D  97  TYR D 103 -1  O  TYR D 100   N  HIS D  86           
SHEET    3   M 5 ILE D  36  PRO D  44 -1  N  VAL D  42   O  TYR D  97           
SHEET    4   M 5 LEU D 130  ARG D 139 -1  O  ARG D 134   N  ARG D  41           
SHEET    5   M 5 GLY D 308  MET D 309  1  O  GLY D 308   N  LEU D 135           
SHEET    1   N 9 LEU D 169  THR D 173  0                                        
SHEET    2   N 9 PHE D 199  KCX D 201  1  O  PHE D 199   N  LEU D 170           
SHEET    3   N 9 GLY D 237  ASN D 241  1  O  TYR D 239   N  THR D 200           
SHEET    4   N 9 ILE D 264  ASP D 268  1  O  MET D 266   N  LEU D 240           
SHEET    5   N 9 LEU D 290  HIS D 294  1  O  HIS D 292   N  VAL D 265           
SHEET    6   N 9 HIS D 325  GLY D 329  1  N  HIS D 325   O  LEU D 291           
SHEET    7   N 9 ILE D 375  ALA D 378  1  O  VAL D 377   N  ALA D 328           
SHEET    8   N 9 VAL D 399  GLN D 401  1  O  GLN D 401   N  ALA D 378           
SHEET    9   N 9 LEU D 169  THR D 173  1  N  LEU D 169   O  LEU D 400           
SHEET    1   O 2 PHE D 353  ILE D 354  0                                        
SHEET    2   O 2 GLN D 366  ASP D 367 -1  O  GLN D 366   N  ILE D 354           
SHEET    1   P 4 THR V  68  TRP V  70  0                                        
SHEET    2   P 4 VAL V  39  SER V  45 -1  N  LEU V  42   O  TRP V  70           
SHEET    3   P 4 PHE V  98  ASP V 105 -1  O  PHE V 104   N  VAL V  39           
SHEET    4   P 4 VAL V 110  TYR V 118 -1  O  PHE V 115   N  ILE V 101           
SHEET    1   Q 5 ARG E  83  PRO E  89  0                                        
SHEET    2   Q 5 TYR E  97  TYR E 103 -1  O  TYR E 100   N  HIS E  86           
SHEET    3   Q 5 ILE E  36  PRO E  44 -1  N  VAL E  42   O  TYR E  97           
SHEET    4   Q 5 LEU E 130  ARG E 139 -1  O  ARG E 134   N  ARG E  41           
SHEET    5   Q 5 GLY E 308  MET E 309  1  O  GLY E 308   N  LEU E 133           
SHEET    1   R 9 LEU E 169  THR E 173  0                                        
SHEET    2   R 9 PHE E 199  KCX E 201  1  O  PHE E 199   N  LEU E 170           
SHEET    3   R 9 GLY E 237  ASN E 241  1  O  TYR E 239   N  THR E 200           
SHEET    4   R 9 ILE E 264  ASP E 268  1  O  MET E 266   N  LEU E 240           
SHEET    5   R 9 LEU E 290  HIS E 294  1  O  HIS E 292   N  VAL E 265           
SHEET    6   R 9 HIS E 325  GLY E 329  1  N  HIS E 325   O  LEU E 291           
SHEET    7   R 9 ILE E 375  ALA E 378  1  O  VAL E 377   N  ALA E 328           
SHEET    8   R 9 VAL E 399  GLN E 401  1  O  GLN E 401   N  ALA E 378           
SHEET    9   R 9 LEU E 169  THR E 173  1  N  LEU E 169   O  LEU E 400           
SHEET    1   S 2 PHE E 353  ILE E 354  0                                        
SHEET    2   S 2 GLN E 366  ASP E 367 -1  O  GLN E 366   N  ILE E 354           
SHEET    1   T 4 THR W  68  TRP W  70  0                                        
SHEET    2   T 4 VAL W  39  SER W  45 -1  N  LEU W  42   O  TRP W  70           
SHEET    3   T 4 PHE W  98  ASP W 105 -1  O  PHE W 104   N  VAL W  39           
SHEET    4   T 4 VAL W 110  TYR W 118 -1  O  PHE W 115   N  ILE W 101           
SHEET    1   U 5 ARG F  83  PRO F  89  0                                        
SHEET    2   U 5 TYR F  97  TYR F 103 -1  O  ILE F  98   N  GLU F  88           
SHEET    3   U 5 ILE F  36  PRO F  44 -1  N  VAL F  42   O  TYR F  97           
SHEET    4   U 5 LEU F 130  ARG F 139 -1  O  ARG F 134   N  ARG F  41           
SHEET    5   U 5 GLY F 308  MET F 309  1  O  GLY F 308   N  LEU F 133           
SHEET    1   V 9 LEU F 169  THR F 173  0                                        
SHEET    2   V 9 PHE F 199  KCX F 201  1  O  PHE F 199   N  LEU F 170           
SHEET    3   V 9 GLY F 237  ASN F 241  1  O  TYR F 239   N  THR F 200           
SHEET    4   V 9 ILE F 264  ASP F 268  1  O  MET F 266   N  LEU F 240           
SHEET    5   V 9 LEU F 290  HIS F 294  1  O  HIS F 292   N  VAL F 265           
SHEET    6   V 9 HIS F 325  GLY F 329  1  O  HIS F 325   N  ILE F 293           
SHEET    7   V 9 ILE F 375  ALA F 378  1  O  VAL F 377   N  ALA F 328           
SHEET    8   V 9 VAL F 399  GLN F 401  1  O  GLN F 401   N  ALA F 378           
SHEET    9   V 9 LEU F 169  THR F 173  1  N  LEU F 169   O  LEU F 400           
SHEET    1   W 2 PHE F 353  ILE F 354  0                                        
SHEET    2   W 2 GLN F 366  ASP F 367 -1  O  GLN F 366   N  ILE F 354           
SHEET    1   X 4 THR X  68  TRP X  70  0                                        
SHEET    2   X 4 VAL X  39  SER X  45 -1  N  LEU X  42   O  TRP X  70           
SHEET    3   X 4 PHE X  98  ASP X 105 -1  O  ILE X 102   N  CYS X  41           
SHEET    4   X 4 VAL X 110  TYR X 118 -1  O  PHE X 115   N  ILE X 101           
SHEET    1   Y 5 ARG G  83  PRO G  89  0                                        
SHEET    2   Y 5 TYR G  97  TYR G 103 -1  O  TYR G 100   N  HIS G  86           
SHEET    3   Y 5 ILE G  36  PRO G  44 -1  N  PHE G  40   O  ALA G  99           
SHEET    4   Y 5 LEU G 130  ARG G 139 -1  O  ARG G 134   N  ARG G  41           
SHEET    5   Y 5 GLY G 308  MET G 309  1  O  GLY G 308   N  LEU G 135           
SHEET    1   Z 9 LEU G 169  THR G 173  0                                        
SHEET    2   Z 9 PHE G 199  KCX G 201  1  O  KCX G 201   N  CYS G 172           
SHEET    3   Z 9 GLY G 237  ASN G 241  1  O  TYR G 239   N  THR G 200           
SHEET    4   Z 9 ILE G 264  ASP G 268  1  O  MET G 266   N  LEU G 240           
SHEET    5   Z 9 LEU G 290  HIS G 294  1  O  HIS G 292   N  VAL G 265           
SHEET    6   Z 9 HIS G 325  GLY G 329  1  N  HIS G 325   O  LEU G 291           
SHEET    7   Z 9 ILE G 375  ALA G 378  1  O  VAL G 377   N  ALA G 328           
SHEET    8   Z 9 VAL G 399  GLN G 401  1  O  GLN G 401   N  ALA G 378           
SHEET    9   Z 9 LEU G 169  THR G 173  1  N  LEU G 169   O  LEU G 400           
SHEET    1  AA 2 PHE G 353  ILE G 354  0                                        
SHEET    2  AA 2 GLN G 366  ASP G 367 -1  O  GLN G 366   N  ILE G 354           
SHEET    1  AB 4 THR Y  68  TRP Y  70  0                                        
SHEET    2  AB 4 VAL Y  39  SER Y  45 -1  N  PHE Y  44   O  THR Y  68           
SHEET    3  AB 4 PHE Y  98  ASP Y 105 -1  O  ILE Y 102   N  CYS Y  41           
SHEET    4  AB 4 VAL Y 110  TYR Y 118 -1  O  PHE Y 115   N  ILE Y 101           
SHEET    1  AC 5 ARG H  83  PRO H  89  0                                        
SHEET    2  AC 5 TYR H  97  TYR H 103 -1  O  TYR H 100   N  HIS H  86           
SHEET    3  AC 5 ILE H  36  PRO H  44 -1  N  VAL H  42   O  TYR H  97           
SHEET    4  AC 5 LEU H 130  ARG H 139 -1  O  ARG H 134   N  ARG H  41           
SHEET    5  AC 5 GLY H 308  MET H 309  1  O  GLY H 308   N  LEU H 135           
SHEET    1  AD 9 LEU H 169  THR H 173  0                                        
SHEET    2  AD 9 PHE H 199  KCX H 201  1  O  PHE H 199   N  LEU H 170           
SHEET    3  AD 9 GLY H 237  ASN H 241  1  O  TYR H 239   N  THR H 200           
SHEET    4  AD 9 ILE H 264  ASP H 268  1  O  MET H 266   N  LEU H 240           
SHEET    5  AD 9 LEU H 290  HIS H 294  1  O  HIS H 292   N  VAL H 265           
SHEET    6  AD 9 HIS H 325  HIS H 327  1  N  HIS H 325   O  LEU H 291           
SHEET    7  AD 9 ILE H 375  ALA H 378  1  O  VAL H 377   N  ILE H 326           
SHEET    8  AD 9 VAL H 399  GLN H 401  1  O  GLN H 401   N  ALA H 378           
SHEET    9  AD 9 LEU H 169  THR H 173  1  N  LEU H 169   O  LEU H 400           
SHEET    1  AE 2 PHE H 353  ILE H 354  0                                        
SHEET    2  AE 2 GLN H 366  ASP H 367 -1  O  GLN H 366   N  ILE H 354           
SHEET    1  AF 4 THR Z  68  TRP Z  70  0                                        
SHEET    2  AF 4 VAL Z  39  SER Z  45 -1  N  LEU Z  42   O  TRP Z  70           
SHEET    3  AF 4 PHE Z  98  ASP Z 105 -1  O  PHE Z  98   N  SER Z  45           
SHEET    4  AF 4 VAL Z 110  TYR Z 118 -1  O  PHE Z 115   N  ILE Z 101           
SSBOND   1 CYS A  247    CYS B  247                          1555   1555  2.69  
SSBOND   2 CYS C  247    CYS D  247                          1555   1555  2.67  
SSBOND   3 CYS E  247    CYS F  247                          1555   1555  2.70  
SSBOND   4 CYS G  247    CYS H  247                          1555   1555  2.61  
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         C   THR B 200                 N   KCX B 201     1555   1555  1.33  
LINK         C   KCX B 201                 N   ASP B 202     1555   1555  1.34  
LINK         C   THR C 200                 N   KCX C 201     1555   1555  1.33  
LINK         C   KCX C 201                 N   ASP C 202     1555   1555  1.34  
LINK         C   THR D 200                 N   KCX D 201     1555   1555  1.33  
LINK         C   KCX D 201                 N   ASP D 202     1555   1555  1.34  
LINK         C   THR E 200                 N   KCX E 201     1555   1555  1.33  
LINK         C   KCX E 201                 N   ASP E 202     1555   1555  1.33  
LINK         C   THR F 200                 N   KCX F 201     1555   1555  1.33  
LINK         C   KCX F 201                 N   ASP F 202     1555   1555  1.34  
LINK         C   THR G 200                 N   KCX G 201     1555   1555  1.33  
LINK         C   KCX G 201                 N   ASP G 202     1555   1555  1.34  
LINK         C   THR H 200                 N   KCX H 201     1555   1555  1.33  
LINK         C   KCX H 201                 N   ASP H 202     1555   1555  1.34  
LINK         OD1 ASP G 203                MG    MG G 478     1555   1555  2.00  
LINK         OD2 ASP A 203                MG    MG A 478     1555   1555  2.00  
LINK        MG    MG D 478                 O1A 6PG D 479     1555   1555  2.00  
LINK         OD1 ASP E 203                MG    MG E 478     1555   1555  2.01  
LINK        MG    MG B 478                 O1A 6PG B 479     1555   1555  2.01  
LINK         OD2 ASP D 203                MG    MG D 478     1555   1555  2.01  
LINK         OE1 GLU F 204                MG    MG F 478     1555   1555  2.03  
LINK         OQ1 KCX H 201                MG    MG H 478     1555   1555  2.04  
LINK         OD2 ASP H 203                MG    MG H 478     1555   1555  2.05  
LINK         OQ1 KCX F 201                MG    MG F 478     1555   1555  2.06  
LINK        MG    MG A 478                 O1  6PG A 479     1555   1555  2.06  
LINK        MG    MG C 478                 O1A 6PG C 479     1555   1555  2.07  
LINK         OQ1 KCX D 201                MG    MG D 478     1555   1555  2.07  
LINK         OQ1 KCX B 201                MG    MG B 478     1555   1555  2.07  
LINK        MG    MG G 478                 O1A 6PG G 479     1555   1555  2.07  
LINK        MG    MG H 478                 O1A 6PG H 479     1555   1555  2.07  
LINK         OQ1 KCX G 201                MG    MG G 478     1555   1555  2.07  
LINK        MG    MG C 478                 O2  6PG C 479     1555   1555  2.08  
LINK         OD2 ASP C 203                MG    MG C 478     1555   1555  2.08  
LINK        MG    MG H 478                 O2  6PG H 479     1555   1555  2.08  
LINK        MG    MG F 478                 O2  6PG F 479     1555   1555  2.08  
LINK         OD2 ASP B 203                MG    MG B 478     1555   1555  2.08  
LINK        MG    MG E 478                 O1A 6PG E 479     1555   1555  2.09  
LINK         OQ1 KCX E 201                MG    MG E 478     1555   1555  2.10  
LINK         OE1 GLU B 204                MG    MG B 478     1555   1555  2.10  
LINK         OE1 GLU C 204                MG    MG C 478     1555   1555  2.10  
LINK         OE1 GLU D 204                MG    MG D 478     1555   1555  2.11  
LINK         OE2 GLU H 204                MG    MG H 478     1555   1555  2.11  
LINK        MG    MG D 478                 O2  6PG D 479     1555   1555  2.11  
LINK         OQ1 KCX A 201                MG    MG A 478     1555   1555  2.11  
LINK         OE1 GLU E 204                MG    MG E 478     1555   1555  2.12  
LINK         OE1 GLU A 204                MG    MG A 478     1555   1555  2.12  
LINK         OD2 ASP F 203                MG    MG F 478     1555   1555  2.13  
LINK        MG    MG A 478                 O2  6PG A 479     1555   1555  2.14  
LINK        MG    MG F 478                 O1A 6PG F 479     1555   1555  2.14  
LINK        MG    MG E 478                 O2  6PG E 479     1555   1555  2.14  
LINK        MG    MG B 478                 O2  6PG B 479     1555   1555  2.14  
LINK         OE1 GLU G 204                MG    MG G 478     1555   1555  2.15  
LINK        MG    MG G 478                 O2  6PG G 479     1555   1555  2.16  
LINK         OQ1 KCX C 201                MG    MG C 478     1555   1555  2.20  
LINK        MG    MG C 478                 O   HOH C 481     1555   1555  2.00  
LINK        MG    MG G 478                 O   HOH G1909     1555   1555  2.08  
LINK        MG    MG E 478                 O   HOH E1908     1555   1555  2.12  
LINK        MG    MG F 478                 O   HOH F2817     1555   1555  2.14  
LINK        MG    MG A 478                 O   HOH A2934     1555   1555  2.15  
LINK        MG    MG D 478                 O   HOH D3132     1555   1555  2.18  
LINK        MG    MG B 478                 O   HOH B2967     1555   1555  2.22  
LINK        MG    MG H 478                 O   HOH H3197     1555   1555  2.22  
LINK         C   NME S   0                 N   MET S   1     1555   1555  1.33  
LINK         C   NME T   0                 N   MET T   1     1555   1555  1.33  
LINK         C   NME U   0                 N   MET U   1     1555   1555  1.33  
LINK         C   NME V   0                 N   MET V   1     1555   1555  1.33  
LINK         C   NME W   0                 N   MET W   1     1555   1555  1.33  
LINK         C   NME X   0                 N   MET X   1     1555   1555  1.33  
LINK         C   NME Y   0                 N   MET Y   1     1555   1555  1.33  
LINK         C   NME Z   0                 N   MET Z   1     1555   1555  1.33  
CISPEP   1 LYS A  175    PRO A  176          0        -0.15                     
CISPEP   2 LYS B  175    PRO B  176          0        -0.63                     
CISPEP   3 LYS C  175    PRO C  176          0        -0.41                     
CISPEP   4 LYS D  175    PRO D  176          0        -0.32                     
CISPEP   5 LYS E  175    PRO E  176          0         1.37                     
CISPEP   6 LYS F  175    PRO F  176          0        -2.14                     
CISPEP   7 LYS G  175    PRO G  176          0         0.11                     
CISPEP   8 LYS H  175    PRO H  176          0        -0.20                     
SITE     1 AC1  5 KCX A 201  ASP A 203  GLU A 204  6PG A 479                    
SITE     2 AC1  5 HOH A2934                                                     
SITE     1 AC2 20 THR A 173  LYS A 175  KCX A 201  ASP A 203                    
SITE     2 AC2 20 GLU A 204  HIS A 294  ARG A 295  HIS A 298                    
SITE     3 AC2 20 SER A 379   MG A 478  HOH A 497  HOH A 498                    
SITE     4 AC2 20 HOH A 884  HOH A1916  HOH A2402  HOH A2491                    
SITE     5 AC2 20 HOH A2648  HOH A2934  HOH A3580  ASN B 123                    
SITE     1 AC3  5 KCX B 201  ASP B 203  GLU B 204  6PG B 479                    
SITE     2 AC3  5 HOH B2967                                                     
SITE     1 AC4 19 ASN A 123  THR B 173  LYS B 175  KCX B 201                    
SITE     2 AC4 19 ASP B 203  GLU B 204  HIS B 294  ARG B 295                    
SITE     3 AC4 19 HIS B 298  SER B 379   MG B 478  HOH B 649                    
SITE     4 AC4 19 HOH B1425  HOH B1849  HOH B1984  HOH B2967                    
SITE     5 AC4 19 HOH B3286  HOH B3596  HOH B3597                               
SITE     1 AC5  5 KCX C 201  ASP C 203  GLU C 204  6PG C 479                    
SITE     2 AC5  5 HOH C 481                                                     
SITE     1 AC6 17 LYS C 175  KCX C 201  ASP C 203  GLU C 204                    
SITE     2 AC6 17 HIS C 294  ARG C 295  HIS C 298  SER C 379                    
SITE     3 AC6 17  MG C 478  HOH C 481  HOH C 695  HOH C1439                    
SITE     4 AC6 17 HOH C1507  HOH C1962  HOH C2485  HOH C3592                    
SITE     5 AC6 17 ASN D 123                                                     
SITE     1 AC7  5 KCX D 201  ASP D 203  GLU D 204  6PG D 479                    
SITE     2 AC7  5 HOH D3132                                                     
SITE     1 AC8 17 ASN C 123  LYS D 175  KCX D 201  ASP D 203                    
SITE     2 AC8 17 GLU D 204  HIS D 294  ARG D 295  HIS D 298                    
SITE     3 AC8 17 SER D 379   MG D 478  HOH D1958  HOH D2156                    
SITE     4 AC8 17 HOH D2304  HOH D2356  HOH D3132  HOH D3437                    
SITE     5 AC8 17 HOH D3598                                                     
SITE     1 AC9  5 KCX E 201  ASP E 203  GLU E 204  6PG E 479                    
SITE     2 AC9  5 HOH E1908                                                     
SITE     1 BC1 18 THR E 173  LYS E 175  KCX E 201  ASP E 203                    
SITE     2 BC1 18 GLU E 204  HIS E 294  ARG E 295  HIS E 298                    
SITE     3 BC1 18 SER E 379   MG E 478  HOH E 512  HOH E 794                    
SITE     4 BC1 18 HOH E1908  HOH E1929  HOH E2080  HOH E2752                    
SITE     5 BC1 18 HOH E3520  ASN F 123                                          
SITE     1 BC2  5 KCX F 201  ASP F 203  GLU F 204  6PG F 479                    
SITE     2 BC2  5 HOH F2817                                                     
SITE     1 BC3 20 ASN E 123  HOH E 524  HOH E3356  THR F 173                    
SITE     2 BC3 20 LYS F 175  KCX F 201  ASP F 203  GLU F 204                    
SITE     3 BC3 20 HIS F 294  ARG F 295  HIS F 298  GLY F 329                    
SITE     4 BC3 20 SER F 379   MG F 478  HOH F 508  HOH F1401                    
SITE     5 BC3 20 HOH F1445  HOH F2795  HOH F2817  HOH F3601                    
SITE     1 BC4  5 KCX G 201  ASP G 203  GLU G 204  6PG G 479                    
SITE     2 BC4  5 HOH G1909                                                     
SITE     1 BC5 19 THR G 173  LYS G 175  KCX G 201  ASP G 203                    
SITE     2 BC5 19 GLU G 204  HIS G 294  ARG G 295  HIS G 298                    
SITE     3 BC5 19 SER G 379   MG G 478  HOH G 756  HOH G1909                    
SITE     4 BC5 19 HOH G3396  HOH G3584  HOH G3585  HOH G3586                    
SITE     5 BC5 19 HOH G3588  ASN H 123  HOH H3483                               
SITE     1 BC6  5 KCX H 201  ASP H 203  GLU H 204  6PG H 479                    
SITE     2 BC6  5 HOH H3197                                                     
SITE     1 BC7 18 ASN G 123  THR H 173  LYS H 175  KCX H 201                    
SITE     2 BC7 18 ASP H 203  GLU H 204  HIS H 294  ARG H 295                    
SITE     3 BC7 18 HIS H 298  GLY H 329  SER H 379   MG H 478                    
SITE     4 BC7 18 HOH H 522  HOH H1446  HOH H2251  HOH H3197                    
SITE     5 BC7 18 HOH H3314  HOH H3604                                          
CRYST1  110.408  199.624  111.169  90.00  91.45  90.00 P 1 21 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      0.009057  0.000000  0.000229        0.00000                         
SCALE2      0.000000  0.005009  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008998        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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