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Entry: 1A0E
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HEADER    KETOLISOMERASE                          28-NOV-97   1A0E              
TITLE     XYLOSE ISOMERASE FROM THERMOTOGA NEAPOLITANA                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: XYLOSE ISOMERASE;                                          
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 SYNONYM: GLUCOSE ISOMERASE;                                          
COMPND   5 EC: 5.3.1.5;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOTOGA NEAPOLITANA;                         
SOURCE   3 ORGANISM_TAXID: 2337;                                                
SOURCE   4 STRAIN: 5068;                                                        
SOURCE   5 CELLULAR_LOCATION: CYTOPLASM;                                        
SOURCE   6 GENE: XYLA;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: HB101;                                     
SOURCE  10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;                      
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PTNE2;                                    
SOURCE  13 EXPRESSION_SYSTEM_GENE: XYLA                                         
KEYWDS    KETOLISOMERASE, XYLOSE METABOLISM, GLUCOSE-FRUCTOSE INTERCONVERSION,  
KEYWDS   2 HYDRIDE TRANSFER, ALPHA-BETA BARREL, METALLOENZYME, THERMOPHILE      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.GALLAY,R.CHOPRA,E.CONTI,P.BRICK,D.BLOW                              
REVDAT   3   13-JUL-11 1A0E    1       VERSN                                    
REVDAT   2   24-FEB-09 1A0E    1       VERSN                                    
REVDAT   1   03-JUN-98 1A0E    0                                                
JRNL        AUTH   O.GALLAY,R.CHOPRA,E.CONTI,P.BRICK,R.JACKSON,B.HARTLEY,       
JRNL        AUTH 2 C.VIEILLE,J.G.ZEIKUS,D.BLOW                                  
JRNL        TITL   CRYSTAL STRUCTURES OF CLASS II XYLOSE ISOMERASES FROM TWO    
JRNL        TITL 2 THERMOPHILES AND A HYPERTHERMOPHILE                          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   N.E.CHAYEN,E.CONTI,C.VIEILLE,J.G.ZEIKUS                      
REMARK   1  TITL   CRYSTALLIZATION AND INITIAL X-RAY ANALYSIS OF XYLOSE         
REMARK   1  TITL 2 ISOMERASE FROM THERMOTOGA NEAPOLITANA                        
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  53   229 1997              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.VIEILLE,J.M.HESS,R.M.KELLY,J.G.ZEIKUS                      
REMARK   1  TITL   XYLA CLONING AND SEQUENCING AND BIOCHEMICAL CHARACTERIZATION 
REMARK   1  TITL 2 OF XYLOSE ISOMERASE FROM THERMOTOGA NEAPOLITANA              
REMARK   1  REF    APPL.ENVIRON.MICROBIOL.       V.  61  1867 1995              
REMARK   1  REFN                   ISSN 0099-2240                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 26119                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : A POSTERIORI                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1265                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2957                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2880                       
REMARK   3   BIN FREE R VALUE                    : 0.3130                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 144                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.026                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7012                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 256                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.22                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : PARAM.ION                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : TOPH.ION                                       
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: DISORDERED SIDE CHAINS WERE NOT           
REMARK   3  INCLUDED IN REFINEMENT.                                             
REMARK   4                                                                      
REMARK   4 1A0E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JUN-94                             
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : ELLIOTT GX-21                      
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : DUAL SLIT, COLLIMATOR              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : ENRAF-NONIUS FAST                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MADNES                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26137                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 12.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : 0.07600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: XYLOSE ISOMERASE FROM THERMOANAEROBACTERIUM          
REMARK 200  THERMOSULFURIGENES                                                  
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 14%        
REMARK 280  JEFFAMINE ED 4000, 5 MM MGSO4, 0.5 MM COCL2, 50 MM MOPS, PH 7.0     
REMARK 280  (FOR DETAILS SEE REFERENCE 1).                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
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                                         
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       49.43000            
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       49.43000            
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       80.89500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       60.93500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       80.89500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       60.93500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       49.43000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       80.89500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       60.93500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       49.43000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       80.89500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       60.93500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 30610 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 55690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -287.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 109    CG   CD   CE   NZ                                   
REMARK 470     LYS A 120    CG   CD   CE   NZ                                   
REMARK 470     GLU A 123    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 128    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 130    CG   CD   CE   NZ                                   
REMARK 470     ASP A 131    CG   OD1  OD2                                       
REMARK 470     ASN A 133    CG   OD1                                            
REMARK 470     ARG A 221    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 384    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 390    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 395    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 399    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 401    CG   CD   CE   NZ                                   
REMARK 470     LYS A 406    CG   CD   CE   NZ                                   
REMARK 470     GLU A 409    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 412    CG1  CG2  CD1                                       
REMARK 470     LYS A 414    CG   CD   CE   NZ                                   
REMARK 470     GLU A 415    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 418    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 443    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 109    CG   CD   CE   NZ                                   
REMARK 470     LYS D 120    CG   CD   CE   NZ                                   
REMARK 470     GLU D 123    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 128    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 130    CG   CD   CE   NZ                                   
REMARK 470     ASP D 131    CG   OD1  OD2                                       
REMARK 470     ASN D 133    CG   OD1                                            
REMARK 470     ARG D 221    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 384    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 390    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 395    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 399    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 401    CG   CD   CE   NZ                                   
REMARK 470     LYS D 406    CG   CD   CE   NZ                                   
REMARK 470     GLU D 409    CG   CD   OE1  OE2                                  
REMARK 470     ILE D 412    CG1  CG2  CD1                                       
REMARK 470     LYS D 414    CG   CD   CE   NZ                                   
REMARK 470     GLU D 415    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 418    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 443    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500  CO     CO A   493    CO     CO A   493     3655     0.32            
REMARK 500   CG   GLU D     2    CO     CO D   493     3555     1.42            
REMARK 500   OE2  GLU D     2    CO     CO D   493     3555     1.67            
REMARK 500   CB   GLU D     2     OE2  GLU D     2     3555     2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A   4       67.86   -116.44                                   
REMARK 500    TRP A  68        1.36    -62.03                                   
REMARK 500    SER A 132     -165.24   -115.86                                   
REMARK 500    PHE A 144      -25.06   -144.67                                   
REMARK 500    ALA A 153      -85.31   -107.41                                   
REMARK 500    LYS A 235     -176.60   -176.00                                   
REMARK 500    GLU A 236      112.91     62.94                                   
REMARK 500    THR A 331      -87.34   -114.25                                   
REMARK 500    LYS A 332       55.65   -103.82                                   
REMARK 500    ILE A 412      -37.71    -39.54                                   
REMARK 500    PHE D   4       67.87   -116.43                                   
REMARK 500    TRP D  68        1.34    -62.01                                   
REMARK 500    SER D 132     -165.27   -115.86                                   
REMARK 500    PHE D 144      -25.10   -144.65                                   
REMARK 500    ALA D 153      -85.29   -107.45                                   
REMARK 500    LYS D 235     -176.58   -175.95                                   
REMARK 500    GLU D 236      112.89     62.90                                   
REMARK 500    THR D 331      -87.29   -114.22                                   
REMARK 500    LYS D 332       55.60   -103.86                                   
REMARK 500    ILE D 412      -37.69    -39.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO A 491  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 231   OE2                                                    
REMARK 620 2 GLU A 267   OE1  89.6                                              
REMARK 620 3 ASP A 295   OD2  84.8  88.6                                        
REMARK 620 4 ASP A 338   OD2 172.5  82.9  94.8                                  
REMARK 620 5 HOH A 613   O    94.4  73.4 162.0  83.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO A 492  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 267   OE2                                                    
REMARK 620 2 HIS A 270   NE2  79.6                                              
REMARK 620 3 HOH A 613   O    94.8  78.9                                        
REMARK 620 4 HOH A 615   O    97.5 151.8  73.4                                  
REMARK 620 5 HOH A 616   O    84.0  96.5 175.3 111.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO D 491  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 231   OE2                                                    
REMARK 620 2 GLU D 267   OE1  89.6                                              
REMARK 620 3 ASP D 295   OD2  84.8  88.6                                        
REMARK 620 4 ASP D 338   OD2 172.5  82.9  94.8                                  
REMARK 620 5 HOH D 618   O    94.4  73.4 162.0  83.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO D 492  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 267   OE2                                                    
REMARK 620 2 HIS D 270   NE2  79.6                                              
REMARK 620 3 HOH D 620   O    97.5 151.7                                        
REMARK 620 4 HOH D 621   O    84.0  96.5 111.3                                  
REMARK 620 5 HOH D 618   O    94.8  78.8  73.4 175.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CO1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CO BINDING SITE 1 OF MOLECULE A                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CO2                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CO BINDING SITE 2 OF MOLECULE A (HOH629 WAS        
REMARK 800  ADDED AFTER LAST REFINEMENT RESULTED IN A NEW FO-FC PEAK AT THIS    
REMARK 800  SITE).                                                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CO3                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CO BINDING SITE 3 OF MOLECULE A (SITE CO3 IS ON    
REMARK 800  A CRYSTALLOGRAPHIC TWO-FOLD SYMMETRY AXIS: INTERPRETATION OF THE    
REMARK 800  OBSERVED DENSITY PEAK AS A CO CATION WAS PRAGMATIC RATHER THAN      
REMARK 800  RIGOROUS, AS THIS SITE IS CLEARLY NOT A FEATURE OF THE PROTEIN IN   
REMARK 800  SOLUTION).                                                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CO4                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CO BINDING SITE 1 OF MOLECULE D                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CO5                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CO BINDING SITE 2 OF MOLECULE D (HOH629 WAS        
REMARK 800  ADDED AFTER LAST REFINEMENT RESULTED IN A NEW FO-FC PEAK AT THIS    
REMARK 800  SITE).                                                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CO6                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CO BINDING SITE 3 OF MOLECULE D (SITE CO3 IS ON    
REMARK 800  A CRYSTALLOGRAPHIC TWO-FOLD SYMMETRY AXIS: INTERPRETATION OF THE    
REMARK 800  OBSERVED DENSITY PEAK AS A CO CATION WAS PRAGMATIC RATHER THAN      
REMARK 800  RIGOROUS, AS THIS SITE IS CLEARLY NOT A FEATURE OF THE PROTEIN IN   
REMARK 800  SOLUTION).                                                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 491                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 492                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 493                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO D 491                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO D 492                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO D 493                  
DBREF  1A0E A    1   443  UNP    P45687   XYLA_THENE       2    444             
DBREF  1A0E D    1   443  UNP    P45687   XYLA_THENE       2    444             
SEQRES   1 A  443  ALA GLU PHE PHE PRO GLU ILE PRO LYS VAL GLN PHE GLU          
SEQRES   2 A  443  GLY LYS GLU SER THR ASN PRO LEU ALA PHE LYS PHE TYR          
SEQRES   3 A  443  ASP PRO GLU GLU ILE ILE ASP GLY LYS PRO LEU LYS ASP          
SEQRES   4 A  443  HIS LEU LYS PHE SER VAL ALA PHE TRP HIS THR PHE VAL          
SEQRES   5 A  443  ASN GLU GLY ARG ASP PRO PHE GLY ASP PRO THR ALA ASP          
SEQRES   6 A  443  ARG PRO TRP ASN ARG TYR THR ASP PRO MET ASP LYS ALA          
SEQRES   7 A  443  PHE ALA ARG VAL ASP ALA LEU PHE GLU PHE CYS GLU LYS          
SEQRES   8 A  443  LEU ASN ILE GLU TYR PHE CYS PHE HIS ASP ARG ASP ILE          
SEQRES   9 A  443  ALA PRO GLU GLY LYS THR LEU ARG GLU THR ASN LYS ILE          
SEQRES  10 A  443  LEU ASP LYS VAL VAL GLU ARG ILE LYS GLU ARG MET LYS          
SEQRES  11 A  443  ASP SER ASN VAL LYS LEU LEU TRP GLY THR ALA ASN LEU          
SEQRES  12 A  443  PHE SER HIS PRO ARG TYR MET HIS GLY ALA ALA THR THR          
SEQRES  13 A  443  CYS SER ALA ASP VAL PHE ALA TYR ALA ALA ALA GLN VAL          
SEQRES  14 A  443  LYS LYS ALA LEU GLU ILE THR LYS GLU LEU GLY GLY GLU          
SEQRES  15 A  443  GLY TYR VAL PHE TRP GLY GLY ARG GLU GLY TYR GLU THR          
SEQRES  16 A  443  LEU LEU ASN THR ASP LEU GLY PHE GLU LEU GLU ASN LEU          
SEQRES  17 A  443  ALA ARG PHE LEU ARG MET ALA VAL ASP TYR ALA LYS ARG          
SEQRES  18 A  443  ILE GLY PHE THR GLY GLN PHE LEU ILE GLU PRO LYS PRO          
SEQRES  19 A  443  LYS GLU PRO THR LYS HIS GLN TYR ASP PHE ASP VAL ALA          
SEQRES  20 A  443  THR ALA TYR ALA PHE LEU LYS SER HIS GLY LEU ASP GLU          
SEQRES  21 A  443  TYR PHE LYS PHE ASN ILE GLU ALA ASN HIS ALA THR LEU          
SEQRES  22 A  443  ALA GLY HIS THR PHE GLN HIS GLU LEU ARG MET ALA ARG          
SEQRES  23 A  443  ILE LEU GLY LYS LEU GLY SER ILE ASP ALA ASN GLN GLY          
SEQRES  24 A  443  ASP LEU LEU LEU GLY TRP ASP THR ASP GLN PHE PRO THR          
SEQRES  25 A  443  ASN VAL TYR ASP THR THR LEU ALA MET TYR GLU VAL ILE          
SEQRES  26 A  443  LYS ALA GLY GLY PHE THR LYS GLY GLY LEU ASN PHE ASP          
SEQRES  27 A  443  ALA LYS VAL ARG ARG ALA SER TYR LYS VAL GLU ASP LEU          
SEQRES  28 A  443  PHE ILE GLY HIS ILE ALA GLY MET ASP THR PHE ALA LEU          
SEQRES  29 A  443  GLY PHE LYS VAL ALA TYR LYS LEU VAL LYS ASP GLY VAL          
SEQRES  30 A  443  LEU ASP LYS PHE ILE GLU GLU LYS TYR ARG SER PHE ARG          
SEQRES  31 A  443  GLU GLY ILE GLY ARG ASP ILE VAL GLU GLY LYS VAL ASP          
SEQRES  32 A  443  PHE GLU LYS LEU GLU GLU TYR ILE ILE ASP LYS GLU THR          
SEQRES  33 A  443  ILE GLU LEU PRO SER GLY LYS GLN GLU TYR LEU GLU SER          
SEQRES  34 A  443  LEU ILE ASN SER TYR ILE VAL LYS THR ILE LEU GLU LEU          
SEQRES  35 A  443  ARG                                                          
SEQRES   1 D  443  ALA GLU PHE PHE PRO GLU ILE PRO LYS VAL GLN PHE GLU          
SEQRES   2 D  443  GLY LYS GLU SER THR ASN PRO LEU ALA PHE LYS PHE TYR          
SEQRES   3 D  443  ASP PRO GLU GLU ILE ILE ASP GLY LYS PRO LEU LYS ASP          
SEQRES   4 D  443  HIS LEU LYS PHE SER VAL ALA PHE TRP HIS THR PHE VAL          
SEQRES   5 D  443  ASN GLU GLY ARG ASP PRO PHE GLY ASP PRO THR ALA ASP          
SEQRES   6 D  443  ARG PRO TRP ASN ARG TYR THR ASP PRO MET ASP LYS ALA          
SEQRES   7 D  443  PHE ALA ARG VAL ASP ALA LEU PHE GLU PHE CYS GLU LYS          
SEQRES   8 D  443  LEU ASN ILE GLU TYR PHE CYS PHE HIS ASP ARG ASP ILE          
SEQRES   9 D  443  ALA PRO GLU GLY LYS THR LEU ARG GLU THR ASN LYS ILE          
SEQRES  10 D  443  LEU ASP LYS VAL VAL GLU ARG ILE LYS GLU ARG MET LYS          
SEQRES  11 D  443  ASP SER ASN VAL LYS LEU LEU TRP GLY THR ALA ASN LEU          
SEQRES  12 D  443  PHE SER HIS PRO ARG TYR MET HIS GLY ALA ALA THR THR          
SEQRES  13 D  443  CYS SER ALA ASP VAL PHE ALA TYR ALA ALA ALA GLN VAL          
SEQRES  14 D  443  LYS LYS ALA LEU GLU ILE THR LYS GLU LEU GLY GLY GLU          
SEQRES  15 D  443  GLY TYR VAL PHE TRP GLY GLY ARG GLU GLY TYR GLU THR          
SEQRES  16 D  443  LEU LEU ASN THR ASP LEU GLY PHE GLU LEU GLU ASN LEU          
SEQRES  17 D  443  ALA ARG PHE LEU ARG MET ALA VAL ASP TYR ALA LYS ARG          
SEQRES  18 D  443  ILE GLY PHE THR GLY GLN PHE LEU ILE GLU PRO LYS PRO          
SEQRES  19 D  443  LYS GLU PRO THR LYS HIS GLN TYR ASP PHE ASP VAL ALA          
SEQRES  20 D  443  THR ALA TYR ALA PHE LEU LYS SER HIS GLY LEU ASP GLU          
SEQRES  21 D  443  TYR PHE LYS PHE ASN ILE GLU ALA ASN HIS ALA THR LEU          
SEQRES  22 D  443  ALA GLY HIS THR PHE GLN HIS GLU LEU ARG MET ALA ARG          
SEQRES  23 D  443  ILE LEU GLY LYS LEU GLY SER ILE ASP ALA ASN GLN GLY          
SEQRES  24 D  443  ASP LEU LEU LEU GLY TRP ASP THR ASP GLN PHE PRO THR          
SEQRES  25 D  443  ASN VAL TYR ASP THR THR LEU ALA MET TYR GLU VAL ILE          
SEQRES  26 D  443  LYS ALA GLY GLY PHE THR LYS GLY GLY LEU ASN PHE ASP          
SEQRES  27 D  443  ALA LYS VAL ARG ARG ALA SER TYR LYS VAL GLU ASP LEU          
SEQRES  28 D  443  PHE ILE GLY HIS ILE ALA GLY MET ASP THR PHE ALA LEU          
SEQRES  29 D  443  GLY PHE LYS VAL ALA TYR LYS LEU VAL LYS ASP GLY VAL          
SEQRES  30 D  443  LEU ASP LYS PHE ILE GLU GLU LYS TYR ARG SER PHE ARG          
SEQRES  31 D  443  GLU GLY ILE GLY ARG ASP ILE VAL GLU GLY LYS VAL ASP          
SEQRES  32 D  443  PHE GLU LYS LEU GLU GLU TYR ILE ILE ASP LYS GLU THR          
SEQRES  33 D  443  ILE GLU LEU PRO SER GLY LYS GLN GLU TYR LEU GLU SER          
SEQRES  34 D  443  LEU ILE ASN SER TYR ILE VAL LYS THR ILE LEU GLU LEU          
SEQRES  35 D  443  ARG                                                          
HET     CO  A 491       1                                                       
HET     CO  A 492       1                                                       
HET     CO  A 493       1                                                       
HET     CO  D 491       1                                                       
HET     CO  D 492       1                                                       
HET     CO  D 493       1                                                       
HETNAM      CO COBALT (II) ION                                                  
FORMUL   3   CO    6(CO 2+)                                                     
FORMUL   9  HOH   *256(H2 O)                                                    
HELIX    1   1 LEU A   37  LEU A   41  1                                   5    
HELIX    2   2 PHE A   47  THR A   50  1                                   4    
HELIX    3   3 PRO A   67  ASN A   69  5                                   3    
HELIX    4   4 PRO A   74  LEU A   92  1                                  19    
HELIX    5   5 ASP A  101  ILE A  104  1                                   4    
HELIX    6   6 LEU A  111  ASP A  131  1                                  21    
HELIX    7   7 PRO A  147  TYR A  149  5                                   3    
HELIX    8   8 ALA A  159  GLU A  178  1                                  20    
HELIX    9   9 LEU A  201  ILE A  222  1                                  22    
HELIX   10  10 VAL A  246  HIS A  256  1                                  11    
HELIX   11  11 ASP A  259  TYR A  261  5                                   3    
HELIX   12  12 ALA A  268  LEU A  273  1                                   6    
HELIX   13  13 PHE A  278  ILE A  287  1                                  10    
HELIX   14  14 VAL A  314  ALA A  327  1                                  14    
HELIX   15  15 VAL A  348  ASP A  375  1                                  28    
HELIX   16  16 VAL A  377  LYS A  385  1                                   9    
HELIX   17  17 ARG A  387  PHE A  389  5                                   3    
HELIX   18  18 GLY A  392  GLU A  399  1                                   8    
HELIX   19  19 PHE A  404  ILE A  411  1                                   8    
HELIX   20  20 GLN A  424  GLU A  441  1                                  18    
HELIX   21  21 LEU D   37  LEU D   41  1                                   5    
HELIX   22  22 PHE D   47  THR D   50  1                                   4    
HELIX   23  23 PRO D   67  ASN D   69  5                                   3    
HELIX   24  24 PRO D   74  LEU D   92  1                                  19    
HELIX   25  25 ASP D  101  ILE D  104  1                                   4    
HELIX   26  26 LEU D  111  ASP D  131  1                                  21    
HELIX   27  27 PRO D  147  TYR D  149  5                                   3    
HELIX   28  28 ALA D  159  GLU D  178  1                                  20    
HELIX   29  29 LEU D  201  ILE D  222  1                                  22    
HELIX   30  30 VAL D  246  HIS D  256  1                                  11    
HELIX   31  31 ASP D  259  TYR D  261  5                                   3    
HELIX   32  32 ALA D  268  LEU D  273  1                                   6    
HELIX   33  33 PHE D  278  ILE D  287  1                                  10    
HELIX   34  34 VAL D  314  ALA D  327  1                                  14    
HELIX   35  35 VAL D  348  ASP D  375  1                                  28    
HELIX   36  36 VAL D  377  LYS D  385  1                                   9    
HELIX   37  37 ARG D  387  PHE D  389  5                                   3    
HELIX   38  38 GLY D  392  GLU D  399  1                                   8    
HELIX   39  39 PHE D  404  ILE D  411  1                                   8    
HELIX   40  40 GLN D  424  GLU D  441  1                                  18    
SHEET    1   A 5 TRP A 138  THR A 140  0                                        
SHEET    2   A 5 GLY A 183  PHE A 186  1  N  GLY A 183   O  GLY A 139           
SHEET    3   A 5 GLN A 227  ILE A 230  1  N  GLN A 227   O  TYR A 184           
SHEET    4   A 5 PHE A 262  GLU A 267  1  N  LYS A 263   O  PHE A 228           
SHEET    5   A 5 LEU A 291  ASP A 295  1  N  GLY A 292   O  PHE A 264           
SHEET    1   B 5 TRP D 138  THR D 140  0                                        
SHEET    2   B 5 GLY D 183  PHE D 186  1  N  GLY D 183   O  GLY D 139           
SHEET    3   B 5 GLN D 227  ILE D 230  1  N  GLN D 227   O  TYR D 184           
SHEET    4   B 5 PHE D 262  GLU D 267  1  N  LYS D 263   O  PHE D 228           
SHEET    5   B 5 LEU D 291  ASP D 295  1  N  GLY D 292   O  PHE D 264           
LINK        CO    CO A 491                 OE2 GLU A 231     1555   1555  1.99  
LINK        CO    CO A 491                 OE1 GLU A 267     1555   1555  2.12  
LINK        CO    CO A 491                 OD2 ASP A 295     1555   1555  2.16  
LINK        CO    CO A 491                 OD2 ASP A 338     1555   1555  1.94  
LINK        CO    CO A 492                 OE2 GLU A 267     1555   1555  1.94  
LINK        CO    CO A 492                 NE2 HIS A 270     1555   1555  2.39  
LINK        CO    CO A 493                 OE2 GLU A   2     1555   1555  2.01  
LINK        CO    CO D 491                 OE2 GLU D 231     1555   1555  1.99  
LINK        CO    CO D 491                 OE1 GLU D 267     1555   1555  2.12  
LINK        CO    CO D 491                 OD2 ASP D 295     1555   1555  2.16  
LINK        CO    CO D 491                 OD2 ASP D 338     1555   1555  1.94  
LINK        CO    CO D 492                 OE2 GLU D 267     1555   1555  1.94  
LINK        CO    CO D 492                 NE2 HIS D 270     1555   1555  2.39  
LINK        CO    CO D 493                 OE2 GLU D   2     1555   1555  2.01  
LINK        CO    CO A 491                 O   HOH A 613     1555   1555  2.51  
LINK        CO    CO A 492                 O   HOH A 613     1555   1555  2.05  
LINK        CO    CO A 492                 O   HOH A 615     1555   1555  2.64  
LINK        CO    CO A 492                 O   HOH A 616     1555   1555  2.41  
LINK        CO    CO D 491                 O   HOH D 618     1555   1555  2.51  
LINK        CO    CO D 492                 O   HOH D 620     1555   1555  2.64  
LINK        CO    CO D 492                 O   HOH D 621     1555   1555  2.41  
LINK        CO    CO D 492                 O   HOH D 618     1555   1555  2.05  
LINK        CO    CO A 493                 OE2 GLU A   2     1555   3655  2.24  
LINK        CO    CO D 493                 OE2 GLU D   2     1555   3555  1.67  
CISPEP   1 GLU A  236    PRO A  237          0         1.04                     
CISPEP   2 GLU D  236    PRO D  237          0         1.07                     
SITE     1 CO1  5 GLU A 231  GLU A 267  ASP A 295  ASP A 338                    
SITE     2 CO1  5 HOH A 614                                                     
SITE     1 CO2  5 GLU A 267  HIS A 270  HOH A 614  HOH A 615                    
SITE     2 CO2  5 HOH A 616                                                     
SITE     1 CO3  1 GLU A   2                                                     
SITE     1 CO4  5 GLU D 231  GLU D 267  ASP D 295  ASP D 338                    
SITE     2 CO4  5 HOH D 619                                                     
SITE     1 CO5  5 GLU D 267  HIS D 270  HOH D 619  HOH D 620                    
SITE     2 CO5  5 HOH D 621                                                     
SITE     1 CO6  1 GLU D   2                                                     
SITE     1 AC1  5 GLU A 231  GLU A 267  ASP A 295  ASP A 338                    
SITE     2 AC1  5 HOH A 613                                                     
SITE     1 AC2  8 GLU A 267  HIS A 270  ASP A 306  ASP A 308                    
SITE     2 AC2  8 HOH A 613  HOH A 614  HOH A 615  HOH A 616                    
SITE     1 AC3  1 GLU A   2                                                     
SITE     1 AC4  5 GLU D 231  GLU D 267  ASP D 295  ASP D 338                    
SITE     2 AC4  5 HOH D 618                                                     
SITE     1 AC5  8 GLU D 267  HIS D 270  ASP D 306  ASP D 308                    
SITE     2 AC5  8 HOH D 618  HOH D 619  HOH D 620  HOH D 621                    
SITE     1 AC6  1 GLU D   2                                                     
CRYST1  161.790  121.870   98.860  90.00  90.00  90.00 C 2 2 21     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006181  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008205  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010115        0.00000                         
MTRIX1   1 -0.999990  0.002980  0.002100       80.53531    1                    
MTRIX2   1 -0.002590 -0.985770  0.168110        0.16098    1                    
MTRIX3   1  0.002570  0.168100  0.985770       -0.04196    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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