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Database: PDB
Entry: 4GBE
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Original site: 4GBE 
HEADER    TRANSFERASE                             27-JUL-12   4GBE              
TITLE     CRYSTAL STRUCTURE OF E. COLI DNA ADENINE METHYLTRANSFERASE IN COMPLEX 
TITLE    2 WITH SAH                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA ADENINE METHYLASE;                                     
COMPND   3 CHAIN: D, E, F;                                                      
COMPND   4 SYNONYM: DNA ADENINE METHYLTRANSFERASE, DEOXYADENOSYL-               
COMPND   5 METHYLTRANSFERASE, M.ECODAM;                                         
COMPND   6 EC: 2.1.1.72;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K-12;                                                        
SOURCE   5 GENE: B3387, DAM, JW3350;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET24D                                    
KEYWDS    TRANSFERASE, METHYLATION                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.HARMER,P.L.ROACH                                                  
REVDAT   2   28-FEB-24 4GBE    1       REMARK SEQADV                            
REVDAT   1   26-FEB-14 4GBE    0                                                
JRNL        AUTH   J.E.HARMER,J.C.MCKELVIE,G.HOBLEY,P.L.ROACH                   
JRNL        TITL   STRUCTURAL BASIS OF SELECTIVE N-6 ADENINE METHYLTRANSFERASE  
JRNL        TITL 2 INHIBITION BY TRANSITION STATE MIMICS                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.66 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.66                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 39125                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2096                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.66                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.73                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2766                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.18                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 158                          
REMARK   3   BIN FREE R VALUE                    : 0.3570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6039                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 78                                      
REMARK   3   SOLVENT ATOMS            : 75                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 0.08000                                              
REMARK   3    B12 (A**2) : -0.03000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.348         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.258         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.172         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.089         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.923                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6285 ; 0.022 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8519 ; 1.860 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   722 ; 6.831 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   332 ;36.100 ;23.223       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1007 ;17.244 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    48 ;22.093 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   886 ; 0.126 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4909 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3655 ; 1.150 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5874 ; 2.238 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2630 ; 3.189 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2645 ; 5.323 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4GBE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000073973.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-AUG-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.924530                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.15                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41829                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.712                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.20                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.72                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.30                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.84800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.84800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 1600 MM AMMONIUM SULFATE,    
REMARK 280  16% GLYCEROL, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE    
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       31.85433            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       63.70867            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       63.70867            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       31.85433            
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 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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS D    -5                                                      
REMARK 465     HIS D    -4                                                      
REMARK 465     HIS D    -3                                                      
REMARK 465     HIS D    -2                                                      
REMARK 465     HIS D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     LYS D     2                                                      
REMARK 465     SER D   188                                                      
REMARK 465     ALA D   189                                                      
REMARK 465     THR D   190                                                      
REMARK 465     ALA D   191                                                      
REMARK 465     ASN D   192                                                      
REMARK 465     PHE D   193                                                      
REMARK 465     THR D   194                                                      
REMARK 465     ALA D   195                                                      
REMARK 465     TYR D   196                                                      
REMARK 465     HIS D   197                                                      
REMARK 465     THR D   198                                                      
REMARK 465     VAL D   247                                                      
REMARK 465     ARG D   248                                                      
REMARK 465     ARG D   249                                                      
REMARK 465     SER D   250                                                      
REMARK 465     ILE D   251                                                      
REMARK 465     SER D   252                                                      
REMARK 465     SER D   253                                                      
REMARK 465     ASN D   254                                                      
REMARK 465     GLY D   255                                                      
REMARK 465     GLY D   256                                                      
REMARK 465     THR D   257                                                      
REMARK 465     ARG D   258                                                      
REMARK 465     LYS D   259                                                      
REMARK 465     LYS D   260                                                      
REMARK 465     GLY D   271                                                      
REMARK 465     VAL D   272                                                      
REMARK 465     VAL D   273                                                      
REMARK 465     SER D   274                                                      
REMARK 465     PRO D   275                                                      
REMARK 465     ALA D   276                                                      
REMARK 465     LYS D   277                                                      
REMARK 465     LYS D   278                                                      
REMARK 465     HIS E    -5                                                      
REMARK 465     HIS E    -4                                                      
REMARK 465     HIS E    -3                                                      
REMARK 465     HIS E    -2                                                      
REMARK 465     HIS E    -1                                                      
REMARK 465     HIS E     0                                                      
REMARK 465     MET E     1                                                      
REMARK 465     LYS E     2                                                      
REMARK 465     SER E   188                                                      
REMARK 465     ALA E   189                                                      
REMARK 465     THR E   190                                                      
REMARK 465     ALA E   191                                                      
REMARK 465     ASN E   192                                                      
REMARK 465     PHE E   193                                                      
REMARK 465     THR E   194                                                      
REMARK 465     ALA E   195                                                      
REMARK 465     TYR E   196                                                      
REMARK 465     HIS E   197                                                      
REMARK 465     THR E   198                                                      
REMARK 465     ASN E   199                                                      
REMARK 465     ARG E   248                                                      
REMARK 465     ARG E   249                                                      
REMARK 465     SER E   250                                                      
REMARK 465     ILE E   251                                                      
REMARK 465     SER E   252                                                      
REMARK 465     SER E   253                                                      
REMARK 465     ASN E   254                                                      
REMARK 465     GLY E   255                                                      
REMARK 465     GLY E   256                                                      
REMARK 465     THR E   257                                                      
REMARK 465     ARG E   258                                                      
REMARK 465     LYS E   259                                                      
REMARK 465     GLY E   271                                                      
REMARK 465     VAL E   272                                                      
REMARK 465     VAL E   273                                                      
REMARK 465     SER E   274                                                      
REMARK 465     PRO E   275                                                      
REMARK 465     ALA E   276                                                      
REMARK 465     LYS E   277                                                      
REMARK 465     LYS E   278                                                      
REMARK 465     HIS F    -5                                                      
REMARK 465     HIS F    -4                                                      
REMARK 465     HIS F    -3                                                      
REMARK 465     HIS F    -2                                                      
REMARK 465     HIS F    -1                                                      
REMARK 465     HIS F     0                                                      
REMARK 465     MET F     1                                                      
REMARK 465     LYS F     2                                                      
REMARK 465     SER F   188                                                      
REMARK 465     ALA F   189                                                      
REMARK 465     THR F   190                                                      
REMARK 465     ALA F   191                                                      
REMARK 465     ASN F   192                                                      
REMARK 465     PHE F   193                                                      
REMARK 465     THR F   194                                                      
REMARK 465     ALA F   195                                                      
REMARK 465     TYR F   196                                                      
REMARK 465     HIS F   197                                                      
REMARK 465     THR F   198                                                      
REMARK 465     ARG F   248                                                      
REMARK 465     ARG F   249                                                      
REMARK 465     SER F   250                                                      
REMARK 465     ILE F   251                                                      
REMARK 465     SER F   252                                                      
REMARK 465     SER F   253                                                      
REMARK 465     ASN F   254                                                      
REMARK 465     GLY F   255                                                      
REMARK 465     GLY F   256                                                      
REMARK 465     THR F   257                                                      
REMARK 465     ARG F   258                                                      
REMARK 465     LYS F   259                                                      
REMARK 465     LYS F   260                                                      
REMARK 465     GLY F   271                                                      
REMARK 465     VAL F   272                                                      
REMARK 465     VAL F   273                                                      
REMARK 465     SER F   274                                                      
REMARK 465     PRO F   275                                                      
REMARK 465     ALA F   276                                                      
REMARK 465     LYS F   277                                                      
REMARK 465     LYS F   278                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS F   14   CD   CE   NZ                                        
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    PHE F 111   CD1   PHE F 111   CE1     0.137                       
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    ASP F 229   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 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    TYR D  15      -51.85    -22.57                                   
REMARK 500    PRO D  16       33.89    -98.21                                   
REMARK 500    LEU D  17      -11.82   -142.19                                   
REMARK 500    THR D  70      -70.14    -47.43                                   
REMARK 500    ASN D  86       53.80    -99.57                                   
REMARK 500    ASN D 120       19.45     53.55                                   
REMARK 500    ARG D 137       57.49     32.14                                   
REMARK 500    LYS D 140       92.50   -164.90                                   
REMARK 500    HIS D 220       25.80     83.25                                   
REMARK 500    PRO E  26      174.18    -59.22                                   
REMARK 500    ASN E  86       54.62    -92.35                                   
REMARK 500    TYR E 119      108.38    -32.66                                   
REMARK 500    ASN E 120       13.18     57.56                                   
REMARK 500    ARG E 137       64.38     39.02                                   
REMARK 500    LYS E 139      -96.25    -29.84                                   
REMARK 500    ASP E 181       75.05   -118.04                                   
REMARK 500    HIS E 220       33.62     70.16                                   
REMARK 500    ASP E 262      136.24     97.04                                   
REMARK 500    LEU F  17       36.81   -150.70                                   
REMARK 500    PHE F  81       41.54   -103.40                                   
REMARK 500    ASN F 120       19.56     54.68                                   
REMARK 500    ARG F 137       90.26     44.37                                   
REMARK 500    LYS F 139      -78.79    -43.43                                   
REMARK 500    SER F 200     -143.80     46.92                                   
REMARK 500    GLN F 238       -5.69    -52.54                                   
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 SAH D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH E 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH F 301                 
DBREF  4GBE D    1   278  UNP    P0AEE8   DMA_ECOLI        1    278             
DBREF  4GBE E    1   278  UNP    P0AEE8   DMA_ECOLI        1    278             
DBREF  4GBE F    1   278  UNP    P0AEE8   DMA_ECOLI        1    278             
SEQADV 4GBE HIS D   -5  UNP  P0AEE8              EXPRESSION TAG                 
SEQADV 4GBE HIS D   -4  UNP  P0AEE8              EXPRESSION TAG                 
SEQADV 4GBE HIS D   -3  UNP  P0AEE8              EXPRESSION TAG                 
SEQADV 4GBE HIS D   -2  UNP  P0AEE8              EXPRESSION TAG                 
SEQADV 4GBE HIS D   -1  UNP  P0AEE8              EXPRESSION TAG                 
SEQADV 4GBE HIS D    0  UNP  P0AEE8              EXPRESSION TAG                 
SEQADV 4GBE HIS E   -5  UNP  P0AEE8              EXPRESSION TAG                 
SEQADV 4GBE HIS E   -4  UNP  P0AEE8              EXPRESSION TAG                 
SEQADV 4GBE HIS E   -3  UNP  P0AEE8              EXPRESSION TAG                 
SEQADV 4GBE HIS E   -2  UNP  P0AEE8              EXPRESSION TAG                 
SEQADV 4GBE HIS E   -1  UNP  P0AEE8              EXPRESSION TAG                 
SEQADV 4GBE HIS E    0  UNP  P0AEE8              EXPRESSION TAG                 
SEQADV 4GBE HIS F   -5  UNP  P0AEE8              EXPRESSION TAG                 
SEQADV 4GBE HIS F   -4  UNP  P0AEE8              EXPRESSION TAG                 
SEQADV 4GBE HIS F   -3  UNP  P0AEE8              EXPRESSION TAG                 
SEQADV 4GBE HIS F   -2  UNP  P0AEE8              EXPRESSION TAG                 
SEQADV 4GBE HIS F   -1  UNP  P0AEE8              EXPRESSION TAG                 
SEQADV 4GBE HIS F    0  UNP  P0AEE8              EXPRESSION TAG                 
SEQRES   1 D  284  HIS HIS HIS HIS HIS HIS MET LYS LYS ASN ARG ALA PHE          
SEQRES   2 D  284  LEU LYS TRP ALA GLY GLY LYS TYR PRO LEU LEU ASP ASP          
SEQRES   3 D  284  ILE LYS ARG HIS LEU PRO LYS GLY GLU CYS LEU VAL GLU          
SEQRES   4 D  284  PRO PHE VAL GLY ALA GLY SER VAL PHE LEU ASN THR ASP          
SEQRES   5 D  284  PHE SER ARG TYR ILE LEU ALA ASP ILE ASN SER ASP LEU          
SEQRES   6 D  284  ILE SER LEU TYR ASN ILE VAL LYS MET ARG THR ASP GLU          
SEQRES   7 D  284  TYR VAL GLN ALA ALA ARG GLU LEU PHE VAL PRO GLU THR          
SEQRES   8 D  284  ASN CYS ALA GLU VAL TYR TYR GLN PHE ARG GLU GLU PHE          
SEQRES   9 D  284  ASN LYS SER GLN ASP PRO PHE ARG ARG ALA VAL LEU PHE          
SEQRES  10 D  284  LEU TYR LEU ASN ARG TYR GLY TYR ASN GLY LEU CYS ARG          
SEQRES  11 D  284  TYR ASN LEU ARG GLY GLU PHE ASN VAL PRO PHE GLY ARG          
SEQRES  12 D  284  TYR LYS LYS PRO TYR PHE PRO GLU ALA GLU LEU TYR HIS          
SEQRES  13 D  284  PHE ALA GLU LYS ALA GLN ASN ALA PHE PHE TYR CYS GLU          
SEQRES  14 D  284  SER TYR ALA ASP SER MET ALA ARG ALA ASP ASP ALA SER          
SEQRES  15 D  284  VAL VAL TYR CYS ASP PRO PRO TYR ALA PRO LEU SER ALA          
SEQRES  16 D  284  THR ALA ASN PHE THR ALA TYR HIS THR ASN SER PHE THR          
SEQRES  17 D  284  LEU GLU GLN GLN ALA HIS LEU ALA GLU ILE ALA GLU GLY          
SEQRES  18 D  284  LEU VAL GLU ARG HIS ILE PRO VAL LEU ILE SER ASN HIS          
SEQRES  19 D  284  ASP THR MET LEU THR ARG GLU TRP TYR GLN ARG ALA LYS          
SEQRES  20 D  284  LEU HIS VAL VAL LYS VAL ARG ARG SER ILE SER SER ASN          
SEQRES  21 D  284  GLY GLY THR ARG LYS LYS VAL ASP GLU LEU LEU ALA LEU          
SEQRES  22 D  284  TYR LYS PRO GLY VAL VAL SER PRO ALA LYS LYS                  
SEQRES   1 E  284  HIS HIS HIS HIS HIS HIS MET LYS LYS ASN ARG ALA PHE          
SEQRES   2 E  284  LEU LYS TRP ALA GLY GLY LYS TYR PRO LEU LEU ASP ASP          
SEQRES   3 E  284  ILE LYS ARG HIS LEU PRO LYS GLY GLU CYS LEU VAL GLU          
SEQRES   4 E  284  PRO PHE VAL GLY ALA GLY SER VAL PHE LEU ASN THR ASP          
SEQRES   5 E  284  PHE SER ARG TYR ILE LEU ALA ASP ILE ASN SER ASP LEU          
SEQRES   6 E  284  ILE SER LEU TYR ASN ILE VAL LYS MET ARG THR ASP GLU          
SEQRES   7 E  284  TYR VAL GLN ALA ALA ARG GLU LEU PHE VAL PRO GLU THR          
SEQRES   8 E  284  ASN CYS ALA GLU VAL TYR TYR GLN PHE ARG GLU GLU PHE          
SEQRES   9 E  284  ASN LYS SER GLN ASP PRO PHE ARG ARG ALA VAL LEU PHE          
SEQRES  10 E  284  LEU TYR LEU ASN ARG TYR GLY TYR ASN GLY LEU CYS ARG          
SEQRES  11 E  284  TYR ASN LEU ARG GLY GLU PHE ASN VAL PRO PHE GLY ARG          
SEQRES  12 E  284  TYR LYS LYS PRO TYR PHE PRO GLU ALA GLU LEU TYR HIS          
SEQRES  13 E  284  PHE ALA GLU LYS ALA GLN ASN ALA PHE PHE TYR CYS GLU          
SEQRES  14 E  284  SER TYR ALA ASP SER MET ALA ARG ALA ASP ASP ALA SER          
SEQRES  15 E  284  VAL VAL TYR CYS ASP PRO PRO TYR ALA PRO LEU SER ALA          
SEQRES  16 E  284  THR ALA ASN PHE THR ALA TYR HIS THR ASN SER PHE THR          
SEQRES  17 E  284  LEU GLU GLN GLN ALA HIS LEU ALA GLU ILE ALA GLU GLY          
SEQRES  18 E  284  LEU VAL GLU ARG HIS ILE PRO VAL LEU ILE SER ASN HIS          
SEQRES  19 E  284  ASP THR MET LEU THR ARG GLU TRP TYR GLN ARG ALA LYS          
SEQRES  20 E  284  LEU HIS VAL VAL LYS VAL ARG ARG SER ILE SER SER ASN          
SEQRES  21 E  284  GLY GLY THR ARG LYS LYS VAL ASP GLU LEU LEU ALA LEU          
SEQRES  22 E  284  TYR LYS PRO GLY VAL VAL SER PRO ALA LYS LYS                  
SEQRES   1 F  284  HIS HIS HIS HIS HIS HIS MET LYS LYS ASN ARG ALA PHE          
SEQRES   2 F  284  LEU LYS TRP ALA GLY GLY LYS TYR PRO LEU LEU ASP ASP          
SEQRES   3 F  284  ILE LYS ARG HIS LEU PRO LYS GLY GLU CYS LEU VAL GLU          
SEQRES   4 F  284  PRO PHE VAL GLY ALA GLY SER VAL PHE LEU ASN THR ASP          
SEQRES   5 F  284  PHE SER ARG TYR ILE LEU ALA ASP ILE ASN SER ASP LEU          
SEQRES   6 F  284  ILE SER LEU TYR ASN ILE VAL LYS MET ARG THR ASP GLU          
SEQRES   7 F  284  TYR VAL GLN ALA ALA ARG GLU LEU PHE VAL PRO GLU THR          
SEQRES   8 F  284  ASN CYS ALA GLU VAL TYR TYR GLN PHE ARG GLU GLU PHE          
SEQRES   9 F  284  ASN LYS SER GLN ASP PRO PHE ARG ARG ALA VAL LEU PHE          
SEQRES  10 F  284  LEU TYR LEU ASN ARG TYR GLY TYR ASN GLY LEU CYS ARG          
SEQRES  11 F  284  TYR ASN LEU ARG GLY GLU PHE ASN VAL PRO PHE GLY ARG          
SEQRES  12 F  284  TYR LYS LYS PRO TYR PHE PRO GLU ALA GLU LEU TYR HIS          
SEQRES  13 F  284  PHE ALA GLU LYS ALA GLN ASN ALA PHE PHE TYR CYS GLU          
SEQRES  14 F  284  SER TYR ALA ASP SER MET ALA ARG ALA ASP ASP ALA SER          
SEQRES  15 F  284  VAL VAL TYR CYS ASP PRO PRO TYR ALA PRO LEU SER ALA          
SEQRES  16 F  284  THR ALA ASN PHE THR ALA TYR HIS THR ASN SER PHE THR          
SEQRES  17 F  284  LEU GLU GLN GLN ALA HIS LEU ALA GLU ILE ALA GLU GLY          
SEQRES  18 F  284  LEU VAL GLU ARG HIS ILE PRO VAL LEU ILE SER ASN HIS          
SEQRES  19 F  284  ASP THR MET LEU THR ARG GLU TRP TYR GLN ARG ALA LYS          
SEQRES  20 F  284  LEU HIS VAL VAL LYS VAL ARG ARG SER ILE SER SER ASN          
SEQRES  21 F  284  GLY GLY THR ARG LYS LYS VAL ASP GLU LEU LEU ALA LEU          
SEQRES  22 F  284  TYR LYS PRO GLY VAL VAL SER PRO ALA LYS LYS                  
HET    SAH  D 301      26                                                       
HET    SAH  E 301      26                                                       
HET    SAH  F 301      26                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   4  SAH    3(C14 H20 N6 O5 S)                                           
FORMUL   7  HOH   *75(H2 O)                                                     
HELIX    1   1 LEU D   17  LEU D   25  1                                   9    
HELIX    2   2 GLY D   39  ASN D   44  1                                   6    
HELIX    3   3 ASN D   56  ARG D   69  1                                  14    
HELIX    4   4 ARG D   69  GLU D   79  1                                  11    
HELIX    5   5 LEU D   80  ASN D   86  5                                   7    
HELIX    6   6 CYS D   87  SER D  101  1                                  15    
HELIX    7   7 ASP D  103  GLY D  118  1                                  16    
HELIX    8   8 TYR D  119  LEU D  122  5                                   4    
HELIX    9   9 PRO D  144  GLN D  156  1                                  13    
HELIX   10  10 SER D  164  ALA D  170  1                                   7    
HELIX   11  11 THR D  202  ARG D  219  1                                  18    
HELIX   12  12 THR D  230  TYR D  237  1                                   8    
HELIX   13  13 LYS E   14  PRO E   16  5                                   3    
HELIX   14  14 LEU E   17  LEU E   25  1                                   9    
HELIX   15  15 GLY E   39  ASN E   44  1                                   6    
HELIX   16  16 ASN E   56  ARG E   69  1                                  14    
HELIX   17  17 ARG E   69  GLU E   79  1                                  11    
HELIX   18  18 LEU E   80  PHE E   81  5                                   2    
HELIX   19  19 VAL E   82  ASN E   86  5                                   5    
HELIX   20  20 CYS E   87  SER E  101  1                                  15    
HELIX   21  21 ASP E  103  GLY E  118  1                                  16    
HELIX   22  22 TYR E  119  LEU E  122  5                                   4    
HELIX   23  23 PRO E  144  GLN E  156  1                                  13    
HELIX   24  24 SER E  164  ALA E  170  1                                   7    
HELIX   25  25 THR E  202  ARG E  219  1                                  18    
HELIX   26  26 THR E  230  TYR E  237  1                                   8    
HELIX   27  27 LYS F   14  PRO F   16  5                                   3    
HELIX   28  28 LEU F   17  LEU F   25  1                                   9    
HELIX   29  29 VAL F   41  THR F   45  5                                   5    
HELIX   30  30 ASN F   56  ARG F   69  1                                  14    
HELIX   31  31 ARG F   69  GLU F   79  1                                  11    
HELIX   32  32 LEU F   80  PHE F   81  5                                   2    
HELIX   33  33 VAL F   82  ASN F   86  5                                   5    
HELIX   34  34 CYS F   87  SER F  101  1                                  15    
HELIX   35  35 ASP F  103  GLY F  118  1                                  16    
HELIX   36  36 TYR F  119  LEU F  122  5                                   4    
HELIX   37  37 PRO F  144  GLN F  156  1                                  13    
HELIX   38  38 SER F  164  ARG F  171  1                                   8    
HELIX   39  39 THR F  202  ARG F  219  1                                  18    
HELIX   40  40 THR F  230  TYR F  237  1                                   8    
SHEET    1   A 7 ALA D 158  CYS D 162  0                                        
SHEET    2   A 7 ARG D  49  ASP D  54  1  N  LEU D  52   O  PHE D 159           
SHEET    3   A 7 CYS D  30  GLU D  33  1  N  LEU D  31   O  ILE D  51           
SHEET    4   A 7 SER D 176  CYS D 180  1  O  VAL D 177   N  VAL D  32           
SHEET    5   A 7 VAL D 223  HIS D 228  1  O  LEU D 224   N  CYS D 180           
SHEET    6   A 7 GLU D 263  TYR D 268 -1  O  ALA D 266   N  ILE D 225           
SHEET    7   A 7 LYS D 241  VAL D 245 -1  N  VAL D 245   O  GLU D 263           
SHEET    1   B 7 ALA E 158  CYS E 162  0                                        
SHEET    2   B 7 ARG E  49  ASP E  54  1  N  LEU E  52   O  PHE E 159           
SHEET    3   B 7 CYS E  30  GLU E  33  1  N  GLU E  33   O  ILE E  51           
SHEET    4   B 7 SER E 176  CYS E 180  1  O  VAL E 177   N  VAL E  32           
SHEET    5   B 7 VAL E 223  HIS E 228  1  O  LEU E 224   N  CYS E 180           
SHEET    6   B 7 GLU E 263  TYR E 268 -1  O  LEU E 264   N  ASN E 227           
SHEET    7   B 7 LYS E 241  VAL E 245 -1  N  VAL E 245   O  GLU E 263           
SHEET    1   C 7 ALA F 158  TYR F 161  0                                        
SHEET    2   C 7 ARG F  49  ALA F  53  1  N  LEU F  52   O  PHE F 159           
SHEET    3   C 7 CYS F  30  GLU F  33  1  N  GLU F  33   O  ILE F  51           
SHEET    4   C 7 SER F 176  CYS F 180  1  O  VAL F 177   N  VAL F  32           
SHEET    5   C 7 VAL F 223  HIS F 228  1  O  LEU F 224   N  CYS F 180           
SHEET    6   C 7 GLU F 263  TYR F 268 -1  O  LEU F 264   N  ASN F 227           
SHEET    7   C 7 LYS F 241  VAL F 245 -1  N  VAL F 245   O  GLU F 263           
SITE     1 AC1 14 TRP D  10  GLY D  12  LYS D  14  PRO D  34                    
SITE     2 AC1 14 PHE D  35  GLY D  37  ASP D  54  ILE D  55                    
SITE     3 AC1 14 TYR D 165  ASP D 181  PRO D 182  PRO D 183                    
SITE     4 AC1 14 TYR D 184  HOH D 406                                          
SITE     1 AC2 13 TRP E  10  GLY E  13  LYS E  14  PRO E  34                    
SITE     2 AC2 13 PHE E  35  VAL E  36  ALA E  38  SER E  40                    
SITE     3 AC2 13 ASP E  54  ILE E  55  SER E 164  TYR E 165                    
SITE     4 AC2 13 ASP E 181                                                     
SITE     1 AC3 15 TRP F  10  LYS F  14  PRO F  34  PHE F  35                    
SITE     2 AC3 15 VAL F  36  GLY F  37  ALA F  38  GLY F  39                    
SITE     3 AC3 15 SER F  40  ASP F  54  ILE F  55  SER F 164                    
SITE     4 AC3 15 TYR F 165  ASP F 181  PRO F 183                               
CRYST1  161.176  161.176   95.563  90.00  90.00 120.00 P 31 2 1     18          
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      0.006204  0.003582  0.000000        0.00000                         
SCALE2      0.000000  0.007164  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010464        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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