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Database: PDB
Entry: 2H2E
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Original site: 2H2E 
HEADER    TRANSFERASE                             18-MAY-06   2H2E              
TITLE     STRUCTURE OF RUBISCO LSMT BOUND TO AZAADOMET AND LYSINE               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE-1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE LARGE      
COMPND   3 SUBUNIT N-METHYLTRANSFERASE;                                         
COMPND   4 CHAIN: A, B, C;                                                      
COMPND   5 FRAGMENT: RUBISCO LSMT (RESIDUES 49-482);                            
COMPND   6 SYNONYM: [RIBULOSE- BISPHOSPHATE CARBOXYLASE]-LYSINE N-              
COMPND   7 METHYLTRANSFERASE, RUBISCO METHYLTRANSFERASE, RUBISCO LSMT, RBCMT;   
COMPND   8 EC: 2.1.1.127;                                                       
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE   3 ORGANISM_COMMON: PEA;                                                
SOURCE   4 ORGANISM_TAXID: 3888;                                                
SOURCE   5 GENE: RBCMT;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST14                                   
KEYWDS    SET DOMAIN, PROTEIN LYSINE METHYLTRANSFERASE, TRANSFERASE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.F.COUTURE,G.HAUK,R.C.TRIEVEL                                        
REVDAT   5   18-OCT-17 2H2E    1       REMARK                                   
REVDAT   4   13-JUL-11 2H2E    1       VERSN                                    
REVDAT   3   24-FEB-09 2H2E    1       VERSN                                    
REVDAT   2   25-JUL-06 2H2E    1       JRNL                                     
REVDAT   1   30-MAY-06 2H2E    0                                                
JRNL        AUTH   J.F.COUTURE,G.HAUK,M.J.THOMPSON,G.M.BLACKBURN,R.C.TRIEVEL    
JRNL        TITL   CATALYTIC ROLES FOR CARBON-OXYGEN HYDROGEN BONDING IN SET    
JRNL        TITL 2 DOMAIN LYSINE METHYLTRANSFERASES.                            
JRNL        REF    J.BIOL.CHEM.                  V. 281 19280 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16682405                                                     
JRNL        DOI    10.1074/JBC.M602257200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 16.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 582909.510                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 85270                          
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) : 0.262                           
REMARK   3   FREE R VALUE                     : 0.298                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4320                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 13443                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4740                       
REMARK   3   BIN FREE R VALUE                    : 0.4500                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 740                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.017                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10481                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 111                                     
REMARK   3   SOLVENT ATOMS            : 385                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 5.50                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -11.45000                                            
REMARK   3    B22 (A**2) : 16.46000                                             
REMARK   3    B33 (A**2) : -5.02000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.47                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.99                            
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) : 0.51                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 1.03                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.850                           
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) : 1.270 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.240 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.620 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.680 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 48.88                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
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  : AZA.PAR                                        
REMARK   3  PARAMETER FILE  4  : LYS.PAR                                        
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   : AZA.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : LYS.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2H2E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000037843.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-AUG-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 32-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686                             
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR                                
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 85610                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 16.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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   (%): 73.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NACITRATE PH 6.8, 1.43-1.74 M     
REMARK 280  NAACETATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       66.31500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       79.74500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      133.75500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       66.31500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       79.74500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      133.75500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       66.31500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       79.74500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      133.75500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       66.31500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       79.74500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      133.75500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THERE ARE THREE MOLECULES OF LSMT IN THE ASYMMETRIC UNIT.    
REMARK 300 LSMT IS A MONOMER IN SOLUTION.                                       
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 7980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 59130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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     SER A    49                                                      
REMARK 465     ARG A   228                                                      
REMARK 465     ASN A   229                                                      
REMARK 465     GLU A   230                                                      
REMARK 465     LYS A   257                                                      
REMARK 465     GLY A   258                                                      
REMARK 465     ALA A   259                                                      
REMARK 465     ALA A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     LEU A   262                                                      
REMARK 465     PHE A   263                                                      
REMARK 465     SER A   264                                                      
REMARK 465     TRP A   265                                                      
REMARK 465     ASP A   266                                                      
REMARK 465     PHE A   487                                                      
REMARK 465     GLN A   488                                                      
REMARK 465     SER C    49                                                      
REMARK 465     GLN C   488                                                      
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   NE1  TRP B   104     O    HOH B   910              2.14            
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    PRO B  72   C   -  N   -  CA  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    PRO B 236   C   -  N   -  CA  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    PRO C 236   C   -  N   -  CA  ANGL. DEV. =  10.0 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    SER A  51      133.80   -170.03                                   
REMARK 500    THR A  68     -128.06   -131.49                                   
REMARK 500    PRO A  72       47.62    -90.00                                   
REMARK 500    LYS A  88      148.69   -171.59                                   
REMARK 500    ASP A  89      108.74    -38.00                                   
REMARK 500    ASN A  93       10.76     54.14                                   
REMARK 500    TRP A 104     -168.55    -58.12                                   
REMARK 500    ILE A 105       72.19   -167.73                                   
REMARK 500    ARG A 138      105.15    -57.47                                   
REMARK 500    GLU A 139       37.08    -73.38                                   
REMARK 500    ASP A 140        9.23   -153.50                                   
REMARK 500    ILE A 158        2.79    -64.81                                   
REMARK 500    ILE A 195      -41.85   -130.73                                   
REMARK 500    ASN A 199       57.19    -98.74                                   
REMARK 500    LYS A 200       -5.36    -56.88                                   
REMARK 500    PHE A 203       66.59   -114.76                                   
REMARK 500    PRO A 204      -78.17    -53.17                                   
REMARK 500    ASP A 205      154.09    -47.79                                   
REMARK 500    SER A 225       51.65   -112.91                                   
REMARK 500    LEU A 232       73.06   -179.78                                   
REMARK 500    PRO A 236      -30.82    -24.66                                   
REMARK 500    ILE A 241      135.49    -30.89                                   
REMARK 500    THR A 248       32.99   -140.86                                   
REMARK 500    ASP A 251      101.52   -169.32                                   
REMARK 500    HIS A 252       50.99   -157.79                                   
REMARK 500    LEU A 268     -162.17   -162.37                                   
REMARK 500    ASP A 288       97.48   -174.19                                   
REMARK 500    ASN A 306      105.88    -56.18                                   
REMARK 500    ASN A 348        5.13     58.63                                   
REMARK 500    THR A 379      -24.35   -144.96                                   
REMARK 500    SER A 387      144.16    108.94                                   
REMARK 500    VAL A 388      -74.09    -88.97                                   
REMARK 500    SER A 428      -73.76    -26.13                                   
REMARK 500    LEU A 469       15.07    -66.90                                   
REMARK 500    ASP A 471       50.41   -107.66                                   
REMARK 500    GLU B  80       31.45    -93.91                                   
REMARK 500    ILE B 105      100.41   -162.66                                   
REMARK 500    GLU B 139       44.78    -81.55                                   
REMARK 500    ASP B 140       27.83   -163.30                                   
REMARK 500    TRP B 143       37.24    -95.14                                   
REMARK 500    ILE B 195      -61.91   -139.68                                   
REMARK 500    ASN B 199       59.18    -98.00                                   
REMARK 500    PHE B 203       78.16   -114.14                                   
REMARK 500    PRO B 204      -78.88    -61.37                                   
REMARK 500    SER B 225      -96.23    -90.94                                   
REMARK 500    ARG B 226       87.60    -10.78                                   
REMARK 500    LEU B 227     -151.95   -148.32                                   
REMARK 500    ASN B 229      -14.40     80.13                                   
REMARK 500    ASN B 231        9.55   -163.80                                   
REMARK 500    LEU B 232       82.72   -152.80                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      92 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SA8 A 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SA8 B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SA8 C 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LYS B 900                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LYS C 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LYS A 902                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MLV   RELATED DB: PDB                                   
REMARK 900 THE SAME ENZYME IN COMPLEX WITH ADOHCY AND HEPES.                    
REMARK 900 RELATED ID: 1OZV   RELATED DB: PDB                                   
REMARK 900 THE SAME ENZYME IN COMPLEX WITH ADOHCY AND LYSINE.                   
REMARK 900 RELATED ID: 1P0Y   RELATED DB: PDB                                   
REMARK 900 THE SAME ENZYME IN COMPLEX WITH ADOHCY AND MONOMETHYLLYSINE.         
REMARK 900 RELATED ID: 2H21   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2H23   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2H2J   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 THE ENGINEERED CONSTRUCT POSSESSES AN ENLYFQ SEQUENCE ON ITS C-      
REMARK 999 TERMINUS DUE TO A TEV PROTEASE CLEAVAGE SITE.                        
DBREF  2H2E A   49   482  UNP    Q43088   RBCMT_PEA       49    482             
DBREF  2H2E B   49   482  UNP    Q43088   RBCMT_PEA       49    482             
DBREF  2H2E C   49   482  UNP    Q43088   RBCMT_PEA       49    482             
SEQADV 2H2E GLU A  483  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2E ASN A  484  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2E LEU A  485  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2E TYR A  486  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2E PHE A  487  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2E GLN A  488  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2E GLU B  483  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2E ASN B  484  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2E LEU B  485  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2E TYR B  486  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2E PHE B  487  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2E GLN B  488  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2E GLU C  483  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2E ASN C  484  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2E LEU C  485  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2E TYR C  486  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2E PHE C  487  UNP  Q43088              CLONING ARTIFACT               
SEQADV 2H2E GLN C  488  UNP  Q43088              CLONING ARTIFACT               
SEQRES   1 A  440  SER LEU SER PRO ALA VAL GLN THR PHE TRP LYS TRP LEU          
SEQRES   2 A  440  GLN GLU GLU GLY VAL ILE THR ALA LYS THR PRO VAL LYS          
SEQRES   3 A  440  ALA SER VAL VAL THR GLU GLY LEU GLY LEU VAL ALA LEU          
SEQRES   4 A  440  LYS ASP ILE SER ARG ASN ASP VAL ILE LEU GLN VAL PRO          
SEQRES   5 A  440  LYS ARG LEU TRP ILE ASN PRO ASP ALA VAL ALA ALA SER          
SEQRES   6 A  440  GLU ILE GLY ARG VAL CYS SER GLU LEU LYS PRO TRP LEU          
SEQRES   7 A  440  SER VAL ILE LEU PHE LEU ILE ARG GLU ARG SER ARG GLU          
SEQRES   8 A  440  ASP SER VAL TRP LYS HIS TYR PHE GLY ILE LEU PRO GLN          
SEQRES   9 A  440  GLU THR ASP SER THR ILE TYR TRP SER GLU GLU GLU LEU          
SEQRES  10 A  440  GLN GLU LEU GLN GLY SER GLN LEU LEU LYS THR THR VAL          
SEQRES  11 A  440  SER VAL LYS GLU TYR VAL LYS ASN GLU CYS LEU LYS LEU          
SEQRES  12 A  440  GLU GLN GLU ILE ILE LEU PRO ASN LYS ARG LEU PHE PRO          
SEQRES  13 A  440  ASP PRO VAL THR LEU ASP ASP PHE PHE TRP ALA PHE GLY          
SEQRES  14 A  440  ILE LEU ARG SER ARG ALA PHE SER ARG LEU ARG ASN GLU          
SEQRES  15 A  440  ASN LEU VAL VAL VAL PRO MET ALA ASP LEU ILE ASN HIS          
SEQRES  16 A  440  SER ALA GLY VAL THR THR GLU ASP HIS ALA TYR GLU VAL          
SEQRES  17 A  440  LYS GLY ALA ALA GLY LEU PHE SER TRP ASP TYR LEU PHE          
SEQRES  18 A  440  SER LEU LYS SER PRO LEU SER VAL LYS ALA GLY GLU GLN          
SEQRES  19 A  440  VAL TYR ILE GLN TYR ASP LEU ASN LYS SER ASN ALA GLU          
SEQRES  20 A  440  LEU ALA LEU ASP TYR GLY PHE ILE GLU PRO ASN GLU ASN          
SEQRES  21 A  440  ARG HIS ALA TYR THR LEU THR LEU GLU ILE SER GLU SER          
SEQRES  22 A  440  ASP PRO PHE PHE ASP ASP LYS LEU ASP VAL ALA GLU SER          
SEQRES  23 A  440  ASN GLY PHE ALA GLN THR ALA TYR PHE ASP ILE PHE TYR          
SEQRES  24 A  440  ASN ARG THR LEU PRO PRO GLY LEU LEU PRO TYR LEU ARG          
SEQRES  25 A  440  LEU VAL ALA LEU GLY GLY THR ASP ALA PHE LEU LEU GLU          
SEQRES  26 A  440  SER LEU PHE ARG ASP THR ILE TRP GLY HIS LEU GLU LEU          
SEQRES  27 A  440  SER VAL SER ARG ASP ASN GLU GLU LEU LEU CYS LYS ALA          
SEQRES  28 A  440  VAL ARG GLU ALA CYS LYS SER ALA LEU ALA GLY TYR HIS          
SEQRES  29 A  440  THR THR ILE GLU GLN ASP ARG GLU LEU LYS GLU GLY ASN          
SEQRES  30 A  440  LEU ASP SER ARG LEU ALA ILE ALA VAL GLY ILE ARG GLU          
SEQRES  31 A  440  GLY GLU LYS MET VAL LEU GLN GLN ILE ASP GLY ILE PHE          
SEQRES  32 A  440  GLU GLN LYS GLU LEU GLU LEU ASP GLN LEU GLU TYR TYR          
SEQRES  33 A  440  GLN GLU ARG ARG LEU LYS ASP LEU GLY LEU CYS GLY GLU          
SEQRES  34 A  440  ASN GLY ASP ILE LEU GLU ASN LEU TYR PHE GLN                  
SEQRES   1 B  440  SER LEU SER PRO ALA VAL GLN THR PHE TRP LYS TRP LEU          
SEQRES   2 B  440  GLN GLU GLU GLY VAL ILE THR ALA LYS THR PRO VAL LYS          
SEQRES   3 B  440  ALA SER VAL VAL THR GLU GLY LEU GLY LEU VAL ALA LEU          
SEQRES   4 B  440  LYS ASP ILE SER ARG ASN ASP VAL ILE LEU GLN VAL PRO          
SEQRES   5 B  440  LYS ARG LEU TRP ILE ASN PRO ASP ALA VAL ALA ALA SER          
SEQRES   6 B  440  GLU ILE GLY ARG VAL CYS SER GLU LEU LYS PRO TRP LEU          
SEQRES   7 B  440  SER VAL ILE LEU PHE LEU ILE ARG GLU ARG SER ARG GLU          
SEQRES   8 B  440  ASP SER VAL TRP LYS HIS TYR PHE GLY ILE LEU PRO GLN          
SEQRES   9 B  440  GLU THR ASP SER THR ILE TYR TRP SER GLU GLU GLU LEU          
SEQRES  10 B  440  GLN GLU LEU GLN GLY SER GLN LEU LEU LYS THR THR VAL          
SEQRES  11 B  440  SER VAL LYS GLU TYR VAL LYS ASN GLU CYS LEU LYS LEU          
SEQRES  12 B  440  GLU GLN GLU ILE ILE LEU PRO ASN LYS ARG LEU PHE PRO          
SEQRES  13 B  440  ASP PRO VAL THR LEU ASP ASP PHE PHE TRP ALA PHE GLY          
SEQRES  14 B  440  ILE LEU ARG SER ARG ALA PHE SER ARG LEU ARG ASN GLU          
SEQRES  15 B  440  ASN LEU VAL VAL VAL PRO MET ALA ASP LEU ILE ASN HIS          
SEQRES  16 B  440  SER ALA GLY VAL THR THR GLU ASP HIS ALA TYR GLU VAL          
SEQRES  17 B  440  LYS GLY ALA ALA GLY LEU PHE SER TRP ASP TYR LEU PHE          
SEQRES  18 B  440  SER LEU LYS SER PRO LEU SER VAL LYS ALA GLY GLU GLN          
SEQRES  19 B  440  VAL TYR ILE GLN TYR ASP LEU ASN LYS SER ASN ALA GLU          
SEQRES  20 B  440  LEU ALA LEU ASP TYR GLY PHE ILE GLU PRO ASN GLU ASN          
SEQRES  21 B  440  ARG HIS ALA TYR THR LEU THR LEU GLU ILE SER GLU SER          
SEQRES  22 B  440  ASP PRO PHE PHE ASP ASP LYS LEU ASP VAL ALA GLU SER          
SEQRES  23 B  440  ASN GLY PHE ALA GLN THR ALA TYR PHE ASP ILE PHE TYR          
SEQRES  24 B  440  ASN ARG THR LEU PRO PRO GLY LEU LEU PRO TYR LEU ARG          
SEQRES  25 B  440  LEU VAL ALA LEU GLY GLY THR ASP ALA PHE LEU LEU GLU          
SEQRES  26 B  440  SER LEU PHE ARG ASP THR ILE TRP GLY HIS LEU GLU LEU          
SEQRES  27 B  440  SER VAL SER ARG ASP ASN GLU GLU LEU LEU CYS LYS ALA          
SEQRES  28 B  440  VAL ARG GLU ALA CYS LYS SER ALA LEU ALA GLY TYR HIS          
SEQRES  29 B  440  THR THR ILE GLU GLN ASP ARG GLU LEU LYS GLU GLY ASN          
SEQRES  30 B  440  LEU ASP SER ARG LEU ALA ILE ALA VAL GLY ILE ARG GLU          
SEQRES  31 B  440  GLY GLU LYS MET VAL LEU GLN GLN ILE ASP GLY ILE PHE          
SEQRES  32 B  440  GLU GLN LYS GLU LEU GLU LEU ASP GLN LEU GLU TYR TYR          
SEQRES  33 B  440  GLN GLU ARG ARG LEU LYS ASP LEU GLY LEU CYS GLY GLU          
SEQRES  34 B  440  ASN GLY ASP ILE LEU GLU ASN LEU TYR PHE GLN                  
SEQRES   1 C  440  SER LEU SER PRO ALA VAL GLN THR PHE TRP LYS TRP LEU          
SEQRES   2 C  440  GLN GLU GLU GLY VAL ILE THR ALA LYS THR PRO VAL LYS          
SEQRES   3 C  440  ALA SER VAL VAL THR GLU GLY LEU GLY LEU VAL ALA LEU          
SEQRES   4 C  440  LYS ASP ILE SER ARG ASN ASP VAL ILE LEU GLN VAL PRO          
SEQRES   5 C  440  LYS ARG LEU TRP ILE ASN PRO ASP ALA VAL ALA ALA SER          
SEQRES   6 C  440  GLU ILE GLY ARG VAL CYS SER GLU LEU LYS PRO TRP LEU          
SEQRES   7 C  440  SER VAL ILE LEU PHE LEU ILE ARG GLU ARG SER ARG GLU          
SEQRES   8 C  440  ASP SER VAL TRP LYS HIS TYR PHE GLY ILE LEU PRO GLN          
SEQRES   9 C  440  GLU THR ASP SER THR ILE TYR TRP SER GLU GLU GLU LEU          
SEQRES  10 C  440  GLN GLU LEU GLN GLY SER GLN LEU LEU LYS THR THR VAL          
SEQRES  11 C  440  SER VAL LYS GLU TYR VAL LYS ASN GLU CYS LEU LYS LEU          
SEQRES  12 C  440  GLU GLN GLU ILE ILE LEU PRO ASN LYS ARG LEU PHE PRO          
SEQRES  13 C  440  ASP PRO VAL THR LEU ASP ASP PHE PHE TRP ALA PHE GLY          
SEQRES  14 C  440  ILE LEU ARG SER ARG ALA PHE SER ARG LEU ARG ASN GLU          
SEQRES  15 C  440  ASN LEU VAL VAL VAL PRO MET ALA ASP LEU ILE ASN HIS          
SEQRES  16 C  440  SER ALA GLY VAL THR THR GLU ASP HIS ALA TYR GLU VAL          
SEQRES  17 C  440  LYS GLY ALA ALA GLY LEU PHE SER TRP ASP TYR LEU PHE          
SEQRES  18 C  440  SER LEU LYS SER PRO LEU SER VAL LYS ALA GLY GLU GLN          
SEQRES  19 C  440  VAL TYR ILE GLN TYR ASP LEU ASN LYS SER ASN ALA GLU          
SEQRES  20 C  440  LEU ALA LEU ASP TYR GLY PHE ILE GLU PRO ASN GLU ASN          
SEQRES  21 C  440  ARG HIS ALA TYR THR LEU THR LEU GLU ILE SER GLU SER          
SEQRES  22 C  440  ASP PRO PHE PHE ASP ASP LYS LEU ASP VAL ALA GLU SER          
SEQRES  23 C  440  ASN GLY PHE ALA GLN THR ALA TYR PHE ASP ILE PHE TYR          
SEQRES  24 C  440  ASN ARG THR LEU PRO PRO GLY LEU LEU PRO TYR LEU ARG          
SEQRES  25 C  440  LEU VAL ALA LEU GLY GLY THR ASP ALA PHE LEU LEU GLU          
SEQRES  26 C  440  SER LEU PHE ARG ASP THR ILE TRP GLY HIS LEU GLU LEU          
SEQRES  27 C  440  SER VAL SER ARG ASP ASN GLU GLU LEU LEU CYS LYS ALA          
SEQRES  28 C  440  VAL ARG GLU ALA CYS LYS SER ALA LEU ALA GLY TYR HIS          
SEQRES  29 C  440  THR THR ILE GLU GLN ASP ARG GLU LEU LYS GLU GLY ASN          
SEQRES  30 C  440  LEU ASP SER ARG LEU ALA ILE ALA VAL GLY ILE ARG GLU          
SEQRES  31 C  440  GLY GLU LYS MET VAL LEU GLN GLN ILE ASP GLY ILE PHE          
SEQRES  32 C  440  GLU GLN LYS GLU LEU GLU LEU ASP GLN LEU GLU TYR TYR          
SEQRES  33 C  440  GLN GLU ARG ARG LEU LYS ASP LEU GLY LEU CYS GLY GLU          
SEQRES  34 C  440  ASN GLY ASP ILE LEU GLU ASN LEU TYR PHE GLN                  
HET    SA8  A 800      27                                                       
HET    LYS  A 902      10                                                       
HET    SA8  B 801      27                                                       
HET    LYS  B 900      10                                                       
HET    SA8  C 802      27                                                       
HET    LYS  C 901      10                                                       
HETNAM     SA8 S-5'-AZAMETHIONINE-5'-DEOXYADENOSINE                             
HETNAM     LYS LYSINE                                                           
HETSYN     SA8 5'-[N-[(3S)-3-AMINO-3-CARBOXYPROPYL]-N-METHYLAMINO]-5'-          
HETSYN   2 SA8  DEOXYADENOSINE                                                  
FORMUL   4  SA8    3(C15 H23 N7 O5)                                             
FORMUL   5  LYS    3(C6 H15 N2 O2 1+)                                           
FORMUL  10  HOH   *385(H2 O)                                                    
HELIX    1   1 SER A   51  GLU A   64  1                                  14    
HELIX    2   2 ARG A  102  TRP A  104  5                                   3    
HELIX    3   3 ASN A  106  ALA A  112  1                                   7    
HELIX    4   4 SER A  113  ARG A  117  5                                   5    
HELIX    5   5 LYS A  123  ARG A  138  1                                  16    
HELIX    6   6 SER A  156  TRP A  160  5                                   5    
HELIX    7   7 SER A  161  GLN A  166  1                                   6    
HELIX    8   8 GLU A  167  GLN A  169  5                                   3    
HELIX    9   9 SER A  171  ILE A  195  1                                  25    
HELIX   10  10 THR A  208  ALA A  223  1                                  16    
HELIX   11  11 SER A  292  TYR A  300  1                                   9    
HELIX   12  12 ASN A  306  ARG A  309  5                                   4    
HELIX   13  13 PHE A  324  SER A  334  1                                  11    
HELIX   14  14 GLY A  354  LEU A  364  1                                  11    
HELIX   15  15 GLY A  365  GLU A  373  5                                   9    
HELIX   16  16 THR A  379  SER A  387  1                                   9    
HELIX   17  17 SER A  389  ALA A  409  1                                  21    
HELIX   18  18 THR A  414  LYS A  422  1                                   9    
HELIX   19  19 ASP A  427  GLU A  457  1                                  31    
HELIX   20  20 TYR A  463  LEU A  469  1                                   7    
HELIX   21  21 LYS A  470  LEU A  472  5                                   3    
HELIX   22  22 GLY A  479  ASN A  484  1                                   6    
HELIX   23  23 SER B   49  GLU B   64  1                                  16    
HELIX   24  24 ARG B  102  TRP B  104  5                                   3    
HELIX   25  25 ASN B  106  ALA B  112  1                                   7    
HELIX   26  26 LYS B  123  ARG B  138  1                                  16    
HELIX   27  27 TRP B  143  GLY B  148  1                                   6    
HELIX   28  28 SER B  156  TRP B  160  5                                   5    
HELIX   29  29 SER B  161  GLN B  166  1                                   6    
HELIX   30  30 GLU B  167  GLN B  169  5                                   3    
HELIX   31  31 SER B  171  ILE B  195  1                                  25    
HELIX   32  32 THR B  208  ALA B  223  1                                  16    
HELIX   33  33 MET B  237  ILE B  241  5                                   5    
HELIX   34  34 PHE B  263  ASP B  266  5                                   4    
HELIX   35  35 SER B  292  TYR B  300  1                                   9    
HELIX   36  36 ASN B  306  ARG B  309  5                                   4    
HELIX   37  37 PHE B  324  SER B  334  1                                  11    
HELIX   38  38 GLY B  354  LEU B  364  1                                  11    
HELIX   39  39 GLY B  365  ARG B  377  5                                  13    
HELIX   40  40 THR B  379  SER B  387  1                                   9    
HELIX   41  41 SER B  389  GLY B  410  1                                  22    
HELIX   42  42 THR B  414  GLU B  423  1                                  10    
HELIX   43  43 ASP B  427  GLU B  457  1                                  31    
HELIX   44  44 TYR B  463  LEU B  469  1                                   7    
HELIX   45  45 ASN B  478  ASN B  484  1                                   7    
HELIX   46  46 SER C   51  GLU C   64  1                                  14    
HELIX   47  47 ARG C  102  TRP C  104  5                                   3    
HELIX   48  48 ASN C  106  ALA C  112  1                                   7    
HELIX   49  49 LYS C  123  ARG C  136  1                                  14    
HELIX   50  50 TRP C  143  GLY C  148  1                                   6    
HELIX   51  51 SER C  161  GLU C  167  1                                   7    
HELIX   52  52 SER C  171  ILE C  195  1                                  25    
HELIX   53  53 THR C  208  ALA C  223  1                                  16    
HELIX   54  54 MET C  237  ILE C  241  5                                   5    
HELIX   55  55 PHE C  263  ASP C  266  5                                   4    
HELIX   56  56 SER C  292  TYR C  300  1                                   9    
HELIX   57  57 ASN C  306  ARG C  309  5                                   4    
HELIX   58  58 PHE C  324  SER C  334  1                                  11    
HELIX   59  59 GLY C  354  LEU C  364  1                                  11    
HELIX   60  60 GLY C  365  ARG C  377  5                                  13    
HELIX   61  61 THR C  379  SER C  387  1                                   9    
HELIX   62  62 SER C  389  GLY C  410  1                                  22    
HELIX   63  63 THR C  414  GLU C  423  1                                  10    
HELIX   64  64 ASP C  427  GLU C  457  1                                  31    
HELIX   65  65 TYR C  463  LEU C  469  1                                   7    
HELIX   66  66 GLY C  479  ASN C  484  1                                   6    
SHEET    1   A 2 VAL A  73  VAL A  78  0                                        
SHEET    2   A 2 GLY A  81  ALA A  86 -1  O  VAL A  85   N  LYS A  74           
SHEET    1   B 3 ASP A  94  PRO A 100  0                                        
SHEET    2   B 3 LEU A 268  SER A 273 -1  O  LEU A 271   N  ILE A  96           
SHEET    3   B 3 ALA A 253  TYR A 254 -1  N  TYR A 254   O  SER A 270           
SHEET    1   C 2 ASN A 242  HIS A 243  0                                        
SHEET    2   C 2 TYR A 284  ILE A 285  1  O  ILE A 285   N  ASN A 242           
SHEET    1   D 2 ALA A 311  GLU A 317  0                                        
SHEET    2   D 2 THR A 340  PHE A 346 -1  O  ALA A 341   N  LEU A 316           
SHEET    1   E 2 VAL B  73  VAL B  78  0                                        
SHEET    2   E 2 GLY B  81  ALA B  86 -1  O  VAL B  85   N  LYS B  74           
SHEET    1   F 3 VAL B  95  PRO B 100  0                                        
SHEET    2   F 3 LEU B 268  LYS B 272 -1  O  PHE B 269   N  VAL B  99           
SHEET    3   F 3 ALA B 253  VAL B 256 -1  N  TYR B 254   O  SER B 270           
SHEET    1   G 2 ASN B 242  HIS B 243  0                                        
SHEET    2   G 2 TYR B 284  ILE B 285  1  O  ILE B 285   N  ASN B 242           
SHEET    1   H 2 ALA B 311  GLU B 317  0                                        
SHEET    2   H 2 THR B 340  PHE B 346 -1  O  ALA B 341   N  LEU B 316           
SHEET    1   I 2 VAL C  73  VAL C  78  0                                        
SHEET    2   I 2 GLY C  81  ALA C  86 -1  O  GLY C  81   N  VAL C  78           
SHEET    1   J 3 VAL C  95  PRO C 100  0                                        
SHEET    2   J 3 LEU C 268  LYS C 272 -1  O  PHE C 269   N  VAL C  99           
SHEET    3   J 3 TYR C 254  LYS C 257 -1  N  GLU C 255   O  SER C 270           
SHEET    1   K 2 ASN C 242  HIS C 243  0                                        
SHEET    2   K 2 TYR C 284  ILE C 285  1  O  ILE C 285   N  ASN C 242           
SHEET    1   L 2 ALA C 311  GLU C 317  0                                        
SHEET    2   L 2 THR C 340  PHE C 346 -1  O  PHE C 343   N  LEU C 314           
SITE     1 AC1 17 GLU A  80  GLY A  81  LEU A  82  SER A 221                    
SITE     2 AC1 17 ARG A 222  ASP A 239  LEU A 240  ASN A 242                    
SITE     3 AC1 17 HIS A 243  TYR A 287  PHE A 302  LYS A 902                    
SITE     4 AC1 17 HOH A 903  HOH A 939  HOH A 951  HOH A 975                    
SITE     5 AC1 17 HOH A 987                                                     
SITE     1 AC2 17 LEU B  82  SER B 221  ARG B 222  ASP B 239                    
SITE     2 AC2 17 LEU B 240  ASN B 242  HIS B 243  TYR B 287                    
SITE     3 AC2 17 PHE B 302  LYS B 900  HOH B 901  HOH B 904                    
SITE     4 AC2 17 HOH B 913  HOH B 929  HOH B 948  HOH B 958                    
SITE     5 AC2 17 HOH B 981                                                     
SITE     1 AC3 12 GLY C  81  LEU C  82  SER C 221  ARG C 222                    
SITE     2 AC3 12 ASP C 239  LEU C 240  ASN C 242  HIS C 243                    
SITE     3 AC3 12 TYR C 287  LYS C 901  HOH C 924  HOH C 983                    
SITE     1 AC4  9 SER B 221  ARG B 222  ALA B 223  PHE B 224                    
SITE     2 AC4  9 SER B 225  ASP B 239  TYR B 287  TYR B 300                    
SITE     3 AC4  9 SA8 B 801                                                     
SITE     1 AC5  9 ARG C 222  SER C 225  ARG C 226  ASP C 239                    
SITE     2 AC5  9 TYR C 254  TYR C 287  TYR C 300  SA8 C 802                    
SITE     3 AC5  9 HOH C 948                                                     
SITE     1 AC6  7 SER A 221  ARG A 222  ALA A 223  PHE A 224                    
SITE     2 AC6  7 TYR A 287  TYR A 300  SA8 A 800                               
CRYST1  132.630  159.490  267.510  90.00  90.00  90.00 I 2 2 2      24          
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      0.007540  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006270  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003738        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system