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Database: PDB
Entry: 2X7J
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Original site: 2X7J 
HEADER    TRANSFERASE                             01-MAR-10   2X7J              
TITLE     STRUCTURE OF THE MENAQUINONE BIOSYNTHESIS PROTEIN MEND FROM           
TITLE    2 BACILLUS SUBTILIS                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-SUCCINYL-5-ENOLPYRUVYL-6-HYDROXY-3-CYCLOHEXENE           
COMPND   3  -1-CARBOXYLATE SYNTHASE;                                            
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 SYNONYM: MENAQUINONE BIOSYNTHESIS PROTEIN MEND, SEPHCHC SYNTHASE,    
COMPND   6  MEND;                                                               
COMPND   7 EC: 2.2.1.9;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 ATCC: 23857;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET15BTEV_BSMEND                          
KEYWDS    TRANSFERASE, METAL-BINDING                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.DAWSON,M.CHEN,P.K.FYFE,Z.GUO,W.N.HUNTER                             
REVDAT   2   04-AUG-10 2X7J    1       JRNL   REMARK DBREF  SEQADV              
REVDAT   1   14-JUL-10 2X7J    0                                                
JRNL        AUTH   A.DAWSON,M.CHEN,P.K.FYFE,Z.GUO,W.N.HUNTER                    
JRNL        TITL   STRUCTURE AND REACTIVITY OF BACILLUS SUBTILIS MEND           
JRNL        TITL 2 CATALYZING THE FIRST COMMITTED STEP IN MENAQUINONE           
JRNL        TITL 3 BIOSYNTHESIS.                                                
JRNL        REF    J.MOL.BIOL.                   V. 401   253 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20600129                                                     
JRNL        DOI    10.1016/J.JMB.2010.06.025                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 62.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.96                          
REMARK   3   NUMBER OF REFLECTIONS             : 96752                          
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) : 0.17522                         
REMARK   3   R VALUE            (WORKING SET) : 0.17243                         
REMARK   3   FREE R VALUE                     : 0.22803                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) :  5.0                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 5118                            
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) : 2.350                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.411                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7105                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.207                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 344                          
REMARK   3   BIN FREE R VALUE                    : 0.271                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18114                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 168                                     
REMARK   3   SOLVENT ATOMS            : 1074                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.9                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.448                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.64                                                
REMARK   3    B22 (A**2) : -0.02                                                
REMARK   3    B33 (A**2) : 1.66                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : -0.00                                                
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.413         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.244         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.169         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.104         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 18706 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 25431 ; 1.324 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2334 ; 6.952 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   853 ;35.287 ;23.763       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3070 ;17.151 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   132 ;19.049 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2811 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 14324 ; 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): 11589 ; 0.682 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 18752 ; 1.211 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7117 ; 0.653 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6667 ; 1.032 ; 3.000       
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   : 1.20                                          
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          
REMARK   3   RIDING POSITIONS.U VALUES REFINED INDIVIDUALLY.                    
REMARK   3   STRUCTURE WAS SOLVED USING SAD ON A SEMET DERIVATISED              
REMARK   3   PROTEIN. THE SEMET REFINEMENT WAS NOT COMPLETED OR                 
REMARK   3   SUBMITTED.                                                         
REMARK   4                                                                      
REMARK   4 2X7J COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-MAR-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-43067.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-SEP-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00640                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 101958                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.35                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 68.84                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.1                                
REMARK 200  R MERGE                    (I) : 0.11                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.30                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.39                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.10                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.8                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN BUFFER CONTAINED 20 MM           
REMARK 280  TRIS, 50 MM NACL, PH 7.5. CRYSTALLISATION CONDITION                 
REMARK 280  CONTAINED 35% PEG 1.5K, 0.1 M TRIS PH 8, 0.25 M AMMONIUM            
REMARK 280  SULFATE                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       50.09000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       79.24950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       76.49500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       79.24950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       50.09000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       76.49500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 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                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 29360 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 69090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -306.8 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -23                                                      
REMARK 465     GLY A   -22                                                      
REMARK 465     SER A   -21                                                      
REMARK 465     SER A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     SER A   -13                                                      
REMARK 465     SER A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     GLU A   -10                                                      
REMARK 465     ASN A    -9                                                      
REMARK 465     LEU A    -8                                                      
REMARK 465     TYR A    -7                                                      
REMARK 465     PHE A    -6                                                      
REMARK 465     GLN A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     MET A    -2                                                      
REMARK 465     LEU A    -1                                                      
REMARK 465     GLU A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     MET B   -23                                                      
REMARK 465     GLY B   -22                                                      
REMARK 465     SER B   -21                                                      
REMARK 465     SER B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     SER B   -13                                                      
REMARK 465     SER B   -12                                                      
REMARK 465     GLY B   -11                                                      
REMARK 465     GLU B   -10                                                      
REMARK 465     ASN B    -9                                                      
REMARK 465     LEU B    -8                                                      
REMARK 465     TYR B    -7                                                      
REMARK 465     PHE B    -6                                                      
REMARK 465     GLN B    -5                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     MET B    -2                                                      
REMARK 465     LEU B    -1                                                      
REMARK 465     GLU B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     MET C   -23                                                      
REMARK 465     GLY C   -22                                                      
REMARK 465     SER C   -21                                                      
REMARK 465     SER C   -20                                                      
REMARK 465     HIS C   -19                                                      
REMARK 465     HIS C   -18                                                      
REMARK 465     HIS C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     SER C   -13                                                      
REMARK 465     SER C   -12                                                      
REMARK 465     GLY C   -11                                                      
REMARK 465     GLU C   -10                                                      
REMARK 465     ASN C    -9                                                      
REMARK 465     LEU C    -8                                                      
REMARK 465     TYR C    -7                                                      
REMARK 465     PHE C    -6                                                      
REMARK 465     GLN C    -5                                                      
REMARK 465     GLY C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     MET C    -2                                                      
REMARK 465     LEU C    -1                                                      
REMARK 465     GLU C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C   579                                                      
REMARK 465     LEU C   580                                                      
REMARK 465     MET D   -23                                                      
REMARK 465     GLY D   -22                                                      
REMARK 465     SER D   -21                                                      
REMARK 465     SER D   -20                                                      
REMARK 465     HIS D   -19                                                      
REMARK 465     HIS D   -18                                                      
REMARK 465     HIS D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     SER D   -13                                                      
REMARK 465     SER D   -12                                                      
REMARK 465     GLY D   -11                                                      
REMARK 465     GLU D   -10                                                      
REMARK 465     ASN D    -9                                                      
REMARK 465     LEU D    -8                                                      
REMARK 465     TYR D    -7                                                      
REMARK 465     PHE D    -6                                                      
REMARK 465     GLN D    -5                                                      
REMARK 465     GLY D    -4                                                      
REMARK 465     HIS D    -3                                                      
REMARK 465     MET D    -2                                                      
REMARK 465     LEU D    -1                                                      
REMARK 465     GLU D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU A   356     O    HOH A  2189              2.00            
REMARK 500   OE1  GLU A   378     O    HOH A  2195              2.05            
REMARK 500   OG1  THR B    77     O2   EDO B   603              2.19            
REMARK 500   NZ   LYS B   276     O    HOH B  2120              2.14            
REMARK 500   O    THR B   349     N    ALA B   351              2.04            
REMARK 500   OXT  LEU B   580     O    HOH B  2237              2.19            
REMARK 500   O    VAL D   261     O    HOH D  2138              2.14            
REMARK 500   NZ   LYS D   276     O    HOH D  2145              2.17            
REMARK 500   O    LYS D   499     O    HOH D  2251              2.15            
REMARK 500   O    HOH A  2023     O    HOH A  2024              2.18            
REMARK 500   O    HOH A  2211     O    HOH A  2224              1.92            
REMARK 500   O    HOH C  2186     O    HOH C  2196              2.14            
REMARK 500   O    HOH D  2114     O    HOH D  2119              2.08            
REMARK 500   O    HOH D  2129     O    HOH D  2131              2.20            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 163   C   -  N   -  CA  ANGL. DEV. =  12.8 DEGREES          
REMARK 500    PRO A 163   C   -  N   -  CD  ANGL. DEV. = -30.3 DEGREES          
REMARK 500    PRO A 176   C   -  N   -  CA  ANGL. DEV. =  21.6 DEGREES          
REMARK 500    PRO A 176   C   -  N   -  CD  ANGL. DEV. = -32.6 DEGREES          
REMARK 500    PRO A 176   N   -  CA  -  C   ANGL. DEV. = -19.7 DEGREES          
REMARK 500    PRO B 163   C   -  N   -  CA  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    PRO B 163   C   -  N   -  CD  ANGL. DEV. = -29.9 DEGREES          
REMARK 500    PRO B 176   C   -  N   -  CA  ANGL. DEV. =  16.5 DEGREES          
REMARK 500    PRO B 176   C   -  N   -  CD  ANGL. DEV. = -24.2 DEGREES          
REMARK 500    PRO B 176   N   -  CA  -  C   ANGL. DEV. = -19.1 DEGREES          
REMARK 500    PRO C 163   C   -  N   -  CA  ANGL. DEV. =  11.1 DEGREES          
REMARK 500    PRO C 163   C   -  N   -  CD  ANGL. DEV. = -32.8 DEGREES          
REMARK 500    PRO C 176   C   -  N   -  CA  ANGL. DEV. =  13.3 DEGREES          
REMARK 500    PRO C 176   C   -  N   -  CD  ANGL. DEV. = -29.5 DEGREES          
REMARK 500    PRO D 163   C   -  N   -  CA  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    PRO D 163   C   -  N   -  CD  ANGL. DEV. = -29.6 DEGREES          
REMARK 500    PRO D 176   C   -  N   -  CA  ANGL. DEV. =  21.0 DEGREES          
REMARK 500    PRO D 176   C   -  N   -  CD  ANGL. DEV. = -33.1 DEGREES          
REMARK 500    PRO D 176   N   -  CA  -  C   ANGL. DEV. = -19.3 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    GLN A 117       10.26     80.15                                   
REMARK 500    PRO A 163       93.16     16.27                                   
REMARK 500    HIS A 230      -39.02   -130.50                                   
REMARK 500    SER A 298      109.11    -56.66                                   
REMARK 500    ASP A 324       84.92   -162.28                                   
REMARK 500    GLN A 327       12.79     54.51                                   
REMARK 500    SER A 405     -131.95     73.70                                   
REMARK 500    GLU A 498       66.36    -58.10                                   
REMARK 500    THR A 508       61.36     38.85                                   
REMARK 500    ALA A 539       69.88   -155.08                                   
REMARK 500    ALA A 542       37.82   -142.52                                   
REMARK 500    PRO B 163       82.36     33.78                                   
REMARK 500    GLU B 184       74.10     36.31                                   
REMARK 500    ASP B 324       88.41   -172.60                                   
REMARK 500    ALA B 350       14.83    -27.68                                   
REMARK 500    ALA B 351       37.43    -68.21                                   
REMARK 500    THR B 352      -67.90     49.84                                   
REMARK 500    ARG B 353      133.96    104.80                                   
REMARK 500    SER B 405     -135.85     70.74                                   
REMARK 500    LYS B 448       15.61     52.93                                   
REMARK 500    ASP B 485       72.05     40.31                                   
REMARK 500    THR B 508       69.84     32.22                                   
REMARK 500    PRO B 545      156.88    -48.61                                   
REMARK 500    GLN B 577        2.92    -61.70                                   
REMARK 500    PRO C 163       87.14     23.76                                   
REMARK 500    PRO C 176       94.71     37.40                                   
REMARK 500    LYS C 221       77.10   -101.05                                   
REMARK 500    GLU C 228      130.03    -36.47                                   
REMARK 500    ASN C 259       85.03   -158.99                                   
REMARK 500    LEU C 275        5.32    -68.12                                   
REMARK 500    ASP C 324       87.08   -172.11                                   
REMARK 500    GLN C 327       13.10     59.14                                   
REMARK 500    ALA C 351       87.21    -50.91                                   
REMARK 500    ASP C 379      105.96    -58.09                                   
REMARK 500    SER C 405     -146.35     68.10                                   
REMARK 500    SER C 426      148.88   -171.73                                   
REMARK 500    ALA C 539       69.74   -152.71                                   
REMARK 500    PRO C 545      157.18    -44.79                                   
REMARK 500    GLN C 577      -18.31    -47.53                                   
REMARK 500    ARG D 162      158.41    -48.89                                   
REMARK 500    PRO D 163       77.29     29.39                                   
REMARK 500    GLU D 228      125.74    -39.44                                   
REMARK 500    ASP D 324       87.50   -163.96                                   
REMARK 500    GLN D 327       13.16     59.26                                   
REMARK 500    SER D 405     -145.88     69.31                                   
REMARK 500    GLN D 495        0.85    -63.62                                   
REMARK 500    GLU D 498       71.91    -69.01                                   
REMARK 500    THR D 508       74.25     33.48                                   
REMARK 500    ALA D 542       17.36   -140.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG A  162     PRO A  163                 -103.25                    
REMARK 500 GLU A  175     PRO A  176                   90.97                    
REMARK 500 ARG B  162     PRO B  163                 -110.96                    
REMARK 500 GLU B  175     PRO B  176                   91.15                    
REMARK 500 ARG C  162     PRO C  163                 -106.87                    
REMARK 500 GLU C  175     PRO C  176                 -107.85                    
REMARK 500 ARG D  162     PRO D  163                 -112.72                    
REMARK 500 GLU D  175     PRO D  176                   95.25                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PRO A 176        48.0      L          L   OUTSIDE RANGE           
REMARK 500    PRO B 176        47.8      L          L   OUTSIDE RANGE           
REMARK 500    PRO D 176        48.0      L          L   OUTSIDE RANGE           
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                              MN A 602  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 457   OD1                                                    
REMARK 620 2 ASN A 484   OD1  86.9                                              
REMARK 620 3 GLY A 486   O   104.2  79.7                                        
REMARK 620 4 TPP A 601   O1A  87.3 170.8  94.9                                  
REMARK 620 5 TPP A 601   O3B 161.8  89.2  92.5  98.5                            
REMARK 620 6 HOH A2237   O    82.5  82.7 160.7 103.5  79.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 602  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 484   OD1                                                    
REMARK 620 2 TPP B 601   O1B  92.4                                              
REMARK 620 3 HOH B2239   O    91.5  77.1                                        
REMARK 620 4 ASP B 457   OD1  93.1 159.1  82.5                                  
REMARK 620 5 GLY B 486   O    83.6 103.4 175.1  97.3                            
REMARK 620 6 TPP B 601   O1A 170.7  93.2  97.0  84.3  87.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 602  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C2253   O                                                      
REMARK 620 2 ASP C 457   OD1  81.4                                              
REMARK 620 3 ASN C 484   OD1  91.9  81.2                                        
REMARK 620 4 GLY C 486   O   171.9 106.6  88.1                                  
REMARK 620 5 TPP C 601   O1A  82.9  90.4 170.7  98.1                            
REMARK 620 6 TPP C 601   O3B  77.1 158.5 100.9  94.9  85.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 602  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY D 486   O                                                      
REMARK 620 2 ASN D 484   OD1  87.4                                              
REMARK 620 3 TPP D 601   O1B  93.5  95.7                                        
REMARK 620 4 HOH D2292   O   172.4  86.4  82.8                                  
REMARK 620 5 ASP D 457   OD1 105.6  81.8 160.5  77.8                            
REMARK 620 6 TPP D 601   O1A  90.6 177.4  86.1  95.7  97.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1581  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2022   O                                                      
REMARK 620 2 CYS A  40   O   106.6                                              
REMARK 620 3 ALA A  41   O    83.5  81.4                                        
REMARK 620 4 HIS A  43   O   162.2  88.6 108.5                                  
REMARK 620 5 ILE A  46   O    80.3  87.7 157.0  91.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B1581  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2024   O                                                      
REMARK 620 2 HOH B2022   O    67.6                                              
REMARK 620 3 ILE B  46   O    84.1  98.6                                        
REMARK 620 4 CYS B  40   O   105.2 171.2  85.3                                  
REMARK 620 5 HIS B  43   O   164.2  98.1  91.8  89.6                            
REMARK 620 6 ALA B  41   O    86.8  94.6 159.7  79.6 101.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D1581  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE D  46   O                                                      
REMARK 620 2 CYS D  40   O    97.5                                              
REMARK 620 3 ALA D  41   O   163.6  80.2                                        
REMARK 620 4 HIS D  43   O    98.2  95.9  98.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C1579  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  40   O                                                      
REMARK 620 2 HIS C  43   O    88.4                                              
REMARK 620 3 ALA C  41   O    79.6 104.3                                        
REMARK 620 4 ILE C  46   O    84.6  93.9 155.4                                  
REMARK 620 5 HOH C2015   O   173.5  96.1 103.8  90.3                            
REMARK 620 6 HOH C2018   O   110.1 161.2  83.1  84.8  65.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA D1581                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A1581                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA B1581                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA C1579                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1582                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1582                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1582                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1580                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1583                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1583                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1581                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1583                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 ADDITIONAL RESIDUES AT N-TERMINUS ARE DUE TO HEXA-HIS TAG,           
REMARK 999 TEV CLEAVAGE SITE AND THREE RESIDUES FROM CLONING                    
REMARK 999 STRATEGY.                                                            
DBREF  2X7J A    1   580  UNP    P23970   MEND_BACSU       1    580             
DBREF  2X7J B    1   580  UNP    P23970   MEND_BACSU       1    580             
DBREF  2X7J C    1   580  UNP    P23970   MEND_BACSU       1    580             
DBREF  2X7J D    1   580  UNP    P23970   MEND_BACSU       1    580             
SEQADV 2X7J MET A  -23  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLY A  -22  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J SER A  -21  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J SER A  -20  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS A  -19  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS A  -18  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS A  -17  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS A  -16  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS A  -15  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS A  -14  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J SER A  -13  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J SER A  -12  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLY A  -11  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLU A  -10  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J ASN A   -9  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J LEU A   -8  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J TYR A   -7  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J PHE A   -6  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLN A   -5  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLY A   -4  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS A   -3  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J MET A   -2  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J LEU A   -1  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLU A    0  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J MET B  -23  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLY B  -22  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J SER B  -21  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J SER B  -20  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS B  -19  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS B  -18  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS B  -17  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS B  -16  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS B  -15  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS B  -14  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J SER B  -13  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J SER B  -12  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLY B  -11  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLU B  -10  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J ASN B   -9  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J LEU B   -8  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J TYR B   -7  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J PHE B   -6  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLN B   -5  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLY B   -4  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS B   -3  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J MET B   -2  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J LEU B   -1  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLU B    0  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J MET C  -23  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLY C  -22  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J SER C  -21  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J SER C  -20  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS C  -19  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS C  -18  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS C  -17  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS C  -16  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS C  -15  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS C  -14  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J SER C  -13  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J SER C  -12  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLY C  -11  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLU C  -10  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J ASN C   -9  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J LEU C   -8  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J TYR C   -7  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J PHE C   -6  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLN C   -5  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLY C   -4  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS C   -3  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J MET C   -2  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J LEU C   -1  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLU C    0  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J MET D  -23  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLY D  -22  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J SER D  -21  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J SER D  -20  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS D  -19  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS D  -18  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS D  -17  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS D  -16  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS D  -15  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS D  -14  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J SER D  -13  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J SER D  -12  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLY D  -11  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLU D  -10  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J ASN D   -9  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J LEU D   -8  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J TYR D   -7  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J PHE D   -6  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLN D   -5  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLY D   -4  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J HIS D   -3  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J MET D   -2  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J LEU D   -1  UNP  P23970              EXPRESSION TAG                 
SEQADV 2X7J GLU D    0  UNP  P23970              EXPRESSION TAG                 
SEQRES   1 A  604  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  604  GLU ASN LEU TYR PHE GLN GLY HIS MET LEU GLU MET THR          
SEQRES   3 A  604  VAL ASN PRO ILE THR HIS TYR ILE GLY SER PHE ILE ASP          
SEQRES   4 A  604  GLU PHE ALA LEU SER GLY ILE THR ASP ALA VAL VAL CYS          
SEQRES   5 A  604  PRO GLY SER ARG SER THR PRO LEU ALA VAL LEU CYS ALA          
SEQRES   6 A  604  ALA HIS PRO ASP ILE SER VAL HIS VAL GLN ILE ASP GLU          
SEQRES   7 A  604  ARG SER ALA GLY PHE PHE ALA LEU GLY LEU ALA LYS ALA          
SEQRES   8 A  604  LYS GLN ARG PRO VAL LEU LEU ILE CYS THR SER GLY THR          
SEQRES   9 A  604  ALA ALA ALA ASN PHE TYR PRO ALA VAL VAL GLU ALA HIS          
SEQRES  10 A  604  TYR SER ARG VAL PRO ILE ILE VAL LEU THR ALA ASP ARG          
SEQRES  11 A  604  PRO HIS GLU LEU ARG GLU VAL GLY ALA PRO GLN ALA ILE          
SEQRES  12 A  604  ASN GLN HIS PHE LEU PHE GLY ASN PHE VAL LYS PHE PHE          
SEQRES  13 A  604  THR ASP SER ALA LEU PRO GLU GLU SER PRO GLN MET LEU          
SEQRES  14 A  604  ARG TYR ILE ARG THR LEU ALA SER ARG ALA ALA GLY GLU          
SEQRES  15 A  604  ALA GLN LYS ARG PRO MET GLY PRO VAL HIS VAL ASN VAL          
SEQRES  16 A  604  PRO LEU ARG GLU PRO LEU MET PRO ASP LEU SER ASP GLU          
SEQRES  17 A  604  PRO PHE GLY ARG MET ARG THR GLY ARG HIS VAL SER VAL          
SEQRES  18 A  604  LYS THR GLY THR GLN SER VAL ASP ARG GLU SER LEU SER          
SEQRES  19 A  604  ASP VAL ALA GLU MET LEU ALA GLU ALA GLU LYS GLY MET          
SEQRES  20 A  604  ILE VAL CYS GLY GLU LEU HIS SER ASP ALA ASP LYS GLU          
SEQRES  21 A  604  ASN ILE ILE ALA LEU SER LYS ALA LEU GLN TYR PRO ILE          
SEQRES  22 A  604  LEU ALA ASP PRO LEU SER ASN LEU ARG ASN GLY VAL HIS          
SEQRES  23 A  604  ASP LYS SER THR VAL ILE ASP ALA TYR ASP SER PHE LEU          
SEQRES  24 A  604  LYS ASP ASP GLU LEU LYS ARG LYS LEU ARG PRO ASP VAL          
SEQRES  25 A  604  VAL ILE ARG PHE GLY PRO MET PRO VAL SER LYS PRO VAL          
SEQRES  26 A  604  PHE LEU TRP LEU LYS ASP ASP PRO THR ILE GLN GLN ILE          
SEQRES  27 A  604  VAL ILE ASP GLU ASP GLY GLY TRP ARG ASP PRO THR GLN          
SEQRES  28 A  604  ALA SER ALA HIS MET ILE HIS CYS ASN ALA SER VAL PHE          
SEQRES  29 A  604  ALA GLU GLU ILE MET ALA GLY LEU THR ALA ALA THR ARG          
SEQRES  30 A  604  SER SER GLU TRP LEU GLU LYS TRP GLN PHE VAL ASN GLY          
SEQRES  31 A  604  ARG PHE ARG GLU HIS LEU GLN THR ILE SER SER GLU ASP          
SEQRES  32 A  604  VAL SER PHE GLU GLY ASN LEU TYR ARG ILE LEU GLN HIS          
SEQRES  33 A  604  LEU VAL PRO GLU ASN SER SER LEU PHE VAL GLY ASN SER          
SEQRES  34 A  604  MET PRO ILE ARG ASP VAL ASP THR PHE PHE GLU LYS GLN          
SEQRES  35 A  604  ASP ARG PRO PHE ARG ILE TYR SER ASN ARG GLY ALA ASN          
SEQRES  36 A  604  GLY ILE ASP GLY VAL VAL SER SER ALA MET GLY VAL CYS          
SEQRES  37 A  604  GLU GLY THR LYS ALA PRO VAL THR LEU VAL ILE GLY ASP          
SEQRES  38 A  604  LEU SER PHE TYR HIS ASP LEU ASN GLY LEU LEU ALA ALA          
SEQRES  39 A  604  LYS LYS LEU GLY ILE PRO LEU THR VAL ILE LEU VAL ASN          
SEQRES  40 A  604  ASN ASP GLY GLY GLY ILE PHE SER PHE LEU PRO GLN ALA          
SEQRES  41 A  604  SER GLU LYS THR HIS PHE GLU ASP LEU PHE GLY THR PRO          
SEQRES  42 A  604  THR GLY LEU ASP PHE LYS HIS ALA ALA ALA LEU TYR GLY          
SEQRES  43 A  604  GLY THR TYR SER CYS PRO ALA SER TRP ASP GLU PHE LYS          
SEQRES  44 A  604  THR ALA TYR ALA PRO GLN ALA ASP LYS PRO GLY LEU HIS          
SEQRES  45 A  604  LEU ILE GLU ILE LYS THR ASP ARG GLN SER ARG VAL GLN          
SEQRES  46 A  604  LEU HIS ARG ASP MET LEU ASN GLU ALA VAL ARG GLU VAL          
SEQRES  47 A  604  LYS LYS GLN TRP GLU LEU                                      
SEQRES   1 B  604  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  604  GLU ASN LEU TYR PHE GLN GLY HIS MET LEU GLU MET THR          
SEQRES   3 B  604  VAL ASN PRO ILE THR HIS TYR ILE GLY SER PHE ILE ASP          
SEQRES   4 B  604  GLU PHE ALA LEU SER GLY ILE THR ASP ALA VAL VAL CYS          
SEQRES   5 B  604  PRO GLY SER ARG SER THR PRO LEU ALA VAL LEU CYS ALA          
SEQRES   6 B  604  ALA HIS PRO ASP ILE SER VAL HIS VAL GLN ILE ASP GLU          
SEQRES   7 B  604  ARG SER ALA GLY PHE PHE ALA LEU GLY LEU ALA LYS ALA          
SEQRES   8 B  604  LYS GLN ARG PRO VAL LEU LEU ILE CYS THR SER GLY THR          
SEQRES   9 B  604  ALA ALA ALA ASN PHE TYR PRO ALA VAL VAL GLU ALA HIS          
SEQRES  10 B  604  TYR SER ARG VAL PRO ILE ILE VAL LEU THR ALA ASP ARG          
SEQRES  11 B  604  PRO HIS GLU LEU ARG GLU VAL GLY ALA PRO GLN ALA ILE          
SEQRES  12 B  604  ASN GLN HIS PHE LEU PHE GLY ASN PHE VAL LYS PHE PHE          
SEQRES  13 B  604  THR ASP SER ALA LEU PRO GLU GLU SER PRO GLN MET LEU          
SEQRES  14 B  604  ARG TYR ILE ARG THR LEU ALA SER ARG ALA ALA GLY GLU          
SEQRES  15 B  604  ALA GLN LYS ARG PRO MET GLY PRO VAL HIS VAL ASN VAL          
SEQRES  16 B  604  PRO LEU ARG GLU PRO LEU MET PRO ASP LEU SER ASP GLU          
SEQRES  17 B  604  PRO PHE GLY ARG MET ARG THR GLY ARG HIS VAL SER VAL          
SEQRES  18 B  604  LYS THR GLY THR GLN SER VAL ASP ARG GLU SER LEU SER          
SEQRES  19 B  604  ASP VAL ALA GLU MET LEU ALA GLU ALA GLU LYS GLY MET          
SEQRES  20 B  604  ILE VAL CYS GLY GLU LEU HIS SER ASP ALA ASP LYS GLU          
SEQRES  21 B  604  ASN ILE ILE ALA LEU SER LYS ALA LEU GLN TYR PRO ILE          
SEQRES  22 B  604  LEU ALA ASP PRO LEU SER ASN LEU ARG ASN GLY VAL HIS          
SEQRES  23 B  604  ASP LYS SER THR VAL ILE ASP ALA TYR ASP SER PHE LEU          
SEQRES  24 B  604  LYS ASP ASP GLU LEU LYS ARG LYS LEU ARG PRO ASP VAL          
SEQRES  25 B  604  VAL ILE ARG PHE GLY PRO MET PRO VAL SER LYS PRO VAL          
SEQRES  26 B  604  PHE LEU TRP LEU LYS ASP ASP PRO THR ILE GLN GLN ILE          
SEQRES  27 B  604  VAL ILE ASP GLU ASP GLY GLY TRP ARG ASP PRO THR GLN          
SEQRES  28 B  604  ALA SER ALA HIS MET ILE HIS CYS ASN ALA SER VAL PHE          
SEQRES  29 B  604  ALA GLU GLU ILE MET ALA GLY LEU THR ALA ALA THR ARG          
SEQRES  30 B  604  SER SER GLU TRP LEU GLU LYS TRP GLN PHE VAL ASN GLY          
SEQRES  31 B  604  ARG PHE ARG GLU HIS LEU GLN THR ILE SER SER GLU ASP          
SEQRES  32 B  604  VAL SER PHE GLU GLY ASN LEU TYR ARG ILE LEU GLN HIS          
SEQRES  33 B  604  LEU VAL PRO GLU ASN SER SER LEU PHE VAL GLY ASN SER          
SEQRES  34 B  604  MET PRO ILE ARG ASP VAL ASP THR PHE PHE GLU LYS GLN          
SEQRES  35 B  604  ASP ARG PRO PHE ARG ILE TYR SER ASN ARG GLY ALA ASN          
SEQRES  36 B  604  GLY ILE ASP GLY VAL VAL SER SER ALA MET GLY VAL CYS          
SEQRES  37 B  604  GLU GLY THR LYS ALA PRO VAL THR LEU VAL ILE GLY ASP          
SEQRES  38 B  604  LEU SER PHE TYR HIS ASP LEU ASN GLY LEU LEU ALA ALA          
SEQRES  39 B  604  LYS LYS LEU GLY ILE PRO LEU THR VAL ILE LEU VAL ASN          
SEQRES  40 B  604  ASN ASP GLY GLY GLY ILE PHE SER PHE LEU PRO GLN ALA          
SEQRES  41 B  604  SER GLU LYS THR HIS PHE GLU ASP LEU PHE GLY THR PRO          
SEQRES  42 B  604  THR GLY LEU ASP PHE LYS HIS ALA ALA ALA LEU TYR GLY          
SEQRES  43 B  604  GLY THR TYR SER CYS PRO ALA SER TRP ASP GLU PHE LYS          
SEQRES  44 B  604  THR ALA TYR ALA PRO GLN ALA ASP LYS PRO GLY LEU HIS          
SEQRES  45 B  604  LEU ILE GLU ILE LYS THR ASP ARG GLN SER ARG VAL GLN          
SEQRES  46 B  604  LEU HIS ARG ASP MET LEU ASN GLU ALA VAL ARG GLU VAL          
SEQRES  47 B  604  LYS LYS GLN TRP GLU LEU                                      
SEQRES   1 C  604  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  604  GLU ASN LEU TYR PHE GLN GLY HIS MET LEU GLU MET THR          
SEQRES   3 C  604  VAL ASN PRO ILE THR HIS TYR ILE GLY SER PHE ILE ASP          
SEQRES   4 C  604  GLU PHE ALA LEU SER GLY ILE THR ASP ALA VAL VAL CYS          
SEQRES   5 C  604  PRO GLY SER ARG SER THR PRO LEU ALA VAL LEU CYS ALA          
SEQRES   6 C  604  ALA HIS PRO ASP ILE SER VAL HIS VAL GLN ILE ASP GLU          
SEQRES   7 C  604  ARG SER ALA GLY PHE PHE ALA LEU GLY LEU ALA LYS ALA          
SEQRES   8 C  604  LYS GLN ARG PRO VAL LEU LEU ILE CYS THR SER GLY THR          
SEQRES   9 C  604  ALA ALA ALA ASN PHE TYR PRO ALA VAL VAL GLU ALA HIS          
SEQRES  10 C  604  TYR SER ARG VAL PRO ILE ILE VAL LEU THR ALA ASP ARG          
SEQRES  11 C  604  PRO HIS GLU LEU ARG GLU VAL GLY ALA PRO GLN ALA ILE          
SEQRES  12 C  604  ASN GLN HIS PHE LEU PHE GLY ASN PHE VAL LYS PHE PHE          
SEQRES  13 C  604  THR ASP SER ALA LEU PRO GLU GLU SER PRO GLN MET LEU          
SEQRES  14 C  604  ARG TYR ILE ARG THR LEU ALA SER ARG ALA ALA GLY GLU          
SEQRES  15 C  604  ALA GLN LYS ARG PRO MET GLY PRO VAL HIS VAL ASN VAL          
SEQRES  16 C  604  PRO LEU ARG GLU PRO LEU MET PRO ASP LEU SER ASP GLU          
SEQRES  17 C  604  PRO PHE GLY ARG MET ARG THR GLY ARG HIS VAL SER VAL          
SEQRES  18 C  604  LYS THR GLY THR GLN SER VAL ASP ARG GLU SER LEU SER          
SEQRES  19 C  604  ASP VAL ALA GLU MET LEU ALA GLU ALA GLU LYS GLY MET          
SEQRES  20 C  604  ILE VAL CYS GLY GLU LEU HIS SER ASP ALA ASP LYS GLU          
SEQRES  21 C  604  ASN ILE ILE ALA LEU SER LYS ALA LEU GLN TYR PRO ILE          
SEQRES  22 C  604  LEU ALA ASP PRO LEU SER ASN LEU ARG ASN GLY VAL HIS          
SEQRES  23 C  604  ASP LYS SER THR VAL ILE ASP ALA TYR ASP SER PHE LEU          
SEQRES  24 C  604  LYS ASP ASP GLU LEU LYS ARG LYS LEU ARG PRO ASP VAL          
SEQRES  25 C  604  VAL ILE ARG PHE GLY PRO MET PRO VAL SER LYS PRO VAL          
SEQRES  26 C  604  PHE LEU TRP LEU LYS ASP ASP PRO THR ILE GLN GLN ILE          
SEQRES  27 C  604  VAL ILE ASP GLU ASP GLY GLY TRP ARG ASP PRO THR GLN          
SEQRES  28 C  604  ALA SER ALA HIS MET ILE HIS CYS ASN ALA SER VAL PHE          
SEQRES  29 C  604  ALA GLU GLU ILE MET ALA GLY LEU THR ALA ALA THR ARG          
SEQRES  30 C  604  SER SER GLU TRP LEU GLU LYS TRP GLN PHE VAL ASN GLY          
SEQRES  31 C  604  ARG PHE ARG GLU HIS LEU GLN THR ILE SER SER GLU ASP          
SEQRES  32 C  604  VAL SER PHE GLU GLY ASN LEU TYR ARG ILE LEU GLN HIS          
SEQRES  33 C  604  LEU VAL PRO GLU ASN SER SER LEU PHE VAL GLY ASN SER          
SEQRES  34 C  604  MET PRO ILE ARG ASP VAL ASP THR PHE PHE GLU LYS GLN          
SEQRES  35 C  604  ASP ARG PRO PHE ARG ILE TYR SER ASN ARG GLY ALA ASN          
SEQRES  36 C  604  GLY ILE ASP GLY VAL VAL SER SER ALA MET GLY VAL CYS          
SEQRES  37 C  604  GLU GLY THR LYS ALA PRO VAL THR LEU VAL ILE GLY ASP          
SEQRES  38 C  604  LEU SER PHE TYR HIS ASP LEU ASN GLY LEU LEU ALA ALA          
SEQRES  39 C  604  LYS LYS LEU GLY ILE PRO LEU THR VAL ILE LEU VAL ASN          
SEQRES  40 C  604  ASN ASP GLY GLY GLY ILE PHE SER PHE LEU PRO GLN ALA          
SEQRES  41 C  604  SER GLU LYS THR HIS PHE GLU ASP LEU PHE GLY THR PRO          
SEQRES  42 C  604  THR GLY LEU ASP PHE LYS HIS ALA ALA ALA LEU TYR GLY          
SEQRES  43 C  604  GLY THR TYR SER CYS PRO ALA SER TRP ASP GLU PHE LYS          
SEQRES  44 C  604  THR ALA TYR ALA PRO GLN ALA ASP LYS PRO GLY LEU HIS          
SEQRES  45 C  604  LEU ILE GLU ILE LYS THR ASP ARG GLN SER ARG VAL GLN          
SEQRES  46 C  604  LEU HIS ARG ASP MET LEU ASN GLU ALA VAL ARG GLU VAL          
SEQRES  47 C  604  LYS LYS GLN TRP GLU LEU                                      
SEQRES   1 D  604  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  604  GLU ASN LEU TYR PHE GLN GLY HIS MET LEU GLU MET THR          
SEQRES   3 D  604  VAL ASN PRO ILE THR HIS TYR ILE GLY SER PHE ILE ASP          
SEQRES   4 D  604  GLU PHE ALA LEU SER GLY ILE THR ASP ALA VAL VAL CYS          
SEQRES   5 D  604  PRO GLY SER ARG SER THR PRO LEU ALA VAL LEU CYS ALA          
SEQRES   6 D  604  ALA HIS PRO ASP ILE SER VAL HIS VAL GLN ILE ASP GLU          
SEQRES   7 D  604  ARG SER ALA GLY PHE PHE ALA LEU GLY LEU ALA LYS ALA          
SEQRES   8 D  604  LYS GLN ARG PRO VAL LEU LEU ILE CYS THR SER GLY THR          
SEQRES   9 D  604  ALA ALA ALA ASN PHE TYR PRO ALA VAL VAL GLU ALA HIS          
SEQRES  10 D  604  TYR SER ARG VAL PRO ILE ILE VAL LEU THR ALA ASP ARG          
SEQRES  11 D  604  PRO HIS GLU LEU ARG GLU VAL GLY ALA PRO GLN ALA ILE          
SEQRES  12 D  604  ASN GLN HIS PHE LEU PHE GLY ASN PHE VAL LYS PHE PHE          
SEQRES  13 D  604  THR ASP SER ALA LEU PRO GLU GLU SER PRO GLN MET LEU          
SEQRES  14 D  604  ARG TYR ILE ARG THR LEU ALA SER ARG ALA ALA GLY GLU          
SEQRES  15 D  604  ALA GLN LYS ARG PRO MET GLY PRO VAL HIS VAL ASN VAL          
SEQRES  16 D  604  PRO LEU ARG GLU PRO LEU MET PRO ASP LEU SER ASP GLU          
SEQRES  17 D  604  PRO PHE GLY ARG MET ARG THR GLY ARG HIS VAL SER VAL          
SEQRES  18 D  604  LYS THR GLY THR GLN SER VAL ASP ARG GLU SER LEU SER          
SEQRES  19 D  604  ASP VAL ALA GLU MET LEU ALA GLU ALA GLU LYS GLY MET          
SEQRES  20 D  604  ILE VAL CYS GLY GLU LEU HIS SER ASP ALA ASP LYS GLU          
SEQRES  21 D  604  ASN ILE ILE ALA LEU SER LYS ALA LEU GLN TYR PRO ILE          
SEQRES  22 D  604  LEU ALA ASP PRO LEU SER ASN LEU ARG ASN GLY VAL HIS          
SEQRES  23 D  604  ASP LYS SER THR VAL ILE ASP ALA TYR ASP SER PHE LEU          
SEQRES  24 D  604  LYS ASP ASP GLU LEU LYS ARG LYS LEU ARG PRO ASP VAL          
SEQRES  25 D  604  VAL ILE ARG PHE GLY PRO MET PRO VAL SER LYS PRO VAL          
SEQRES  26 D  604  PHE LEU TRP LEU LYS ASP ASP PRO THR ILE GLN GLN ILE          
SEQRES  27 D  604  VAL ILE ASP GLU ASP GLY GLY TRP ARG ASP PRO THR GLN          
SEQRES  28 D  604  ALA SER ALA HIS MET ILE HIS CYS ASN ALA SER VAL PHE          
SEQRES  29 D  604  ALA GLU GLU ILE MET ALA GLY LEU THR ALA ALA THR ARG          
SEQRES  30 D  604  SER SER GLU TRP LEU GLU LYS TRP GLN PHE VAL ASN GLY          
SEQRES  31 D  604  ARG PHE ARG GLU HIS LEU GLN THR ILE SER SER GLU ASP          
SEQRES  32 D  604  VAL SER PHE GLU GLY ASN LEU TYR ARG ILE LEU GLN HIS          
SEQRES  33 D  604  LEU VAL PRO GLU ASN SER SER LEU PHE VAL GLY ASN SER          
SEQRES  34 D  604  MET PRO ILE ARG ASP VAL ASP THR PHE PHE GLU LYS GLN          
SEQRES  35 D  604  ASP ARG PRO PHE ARG ILE TYR SER ASN ARG GLY ALA ASN          
SEQRES  36 D  604  GLY ILE ASP GLY VAL VAL SER SER ALA MET GLY VAL CYS          
SEQRES  37 D  604  GLU GLY THR LYS ALA PRO VAL THR LEU VAL ILE GLY ASP          
SEQRES  38 D  604  LEU SER PHE TYR HIS ASP LEU ASN GLY LEU LEU ALA ALA          
SEQRES  39 D  604  LYS LYS LEU GLY ILE PRO LEU THR VAL ILE LEU VAL ASN          
SEQRES  40 D  604  ASN ASP GLY GLY GLY ILE PHE SER PHE LEU PRO GLN ALA          
SEQRES  41 D  604  SER GLU LYS THR HIS PHE GLU ASP LEU PHE GLY THR PRO          
SEQRES  42 D  604  THR GLY LEU ASP PHE LYS HIS ALA ALA ALA LEU TYR GLY          
SEQRES  43 D  604  GLY THR TYR SER CYS PRO ALA SER TRP ASP GLU PHE LYS          
SEQRES  44 D  604  THR ALA TYR ALA PRO GLN ALA ASP LYS PRO GLY LEU HIS          
SEQRES  45 D  604  LEU ILE GLU ILE LYS THR ASP ARG GLN SER ARG VAL GLN          
SEQRES  46 D  604  LEU HIS ARG ASP MET LEU ASN GLU ALA VAL ARG GLU VAL          
SEQRES  47 D  604  LYS LYS GLN TRP GLU LEU                                      
HET    TPP  A 601      26                                                       
HET     MN  A 602       1                                                       
HET    EDO  A 603       4                                                       
HET    TPP  B 601      26                                                       
HET     MN  B 602       1                                                       
HET    EDO  B 603       4                                                       
HET    TPP  C 601      26                                                       
HET     MN  C 602       1                                                       
HET    EDO  C 603       4                                                       
HET    TPP  D 601      26                                                       
HET     MN  D 602       1                                                       
HET    EDO  D 603       4                                                       
HET     NA  D1581       1                                                       
HET     NA  A1581       1                                                       
HET     NA  B1581       1                                                       
HET     NA  C1579       1                                                       
HET    SO4  A1582       5                                                       
HET    SO4  B1582       5                                                       
HET    SO4  D1582       5                                                       
HET    SO4  C1580       5                                                       
HET    SO4  A1583       5                                                       
HET    SO4  B1583       5                                                       
HET    SO4  C1581       5                                                       
HET    SO4  D1583       5                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     SO4 SULFATE ION                                                      
HETNAM      NA SODIUM ION                                                       
HETNAM     TPP THIAMINE DIPHOSPHATE                                             
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5  EDO    4(C2 H6 O2)                                                  
FORMUL   6   MN    4(MN 2+)                                                     
FORMUL   7  SO4    8(O4 S 2-)                                                   
FORMUL   8   NA    4(NA 1+)                                                     
FORMUL   9  TPP    4(C12 H19 N4 O7 P2 S 1+)                                     
FORMUL  10  HOH   *1074(H2 O)                                                   
HELIX    1   1 PRO A    5  GLY A   21  1                                  17    
HELIX    2   2 SER A   33  HIS A   43  1                                  11    
HELIX    3   3 ASP A   53  GLN A   69  1                                  17    
HELIX    4   4 GLY A   79  ASN A   84  1                                   6    
HELIX    5   5 PHE A   85  ARG A   96  1                                  12    
HELIX    6   6 PRO A  107  ARG A  111  5                                   5    
HELIX    7   7 PHE A  125  VAL A  129  5                                   5    
HELIX    8   8 SER A  141  LYS A  161  1                                  21    
HELIX    9   9 ARG A  206  SER A  208  5                                   3    
HELIX   10  10 LEU A  209  ALA A  219  1                                  11    
HELIX   11  11 SER A  231  GLN A  246  1                                  16    
HELIX   12  12 PRO A  253  ASN A  256  5                                   4    
HELIX   13  13 ALA A  270  LEU A  275  1                                   6    
HELIX   14  14 ASP A  277  ARG A  285  1                                   9    
HELIX   15  15 SER A  298  ASP A  308  1                                  11    
HELIX   16  16 ASN A  336  GLY A  347  1                                  12    
HELIX   17  17 SER A  355  THR A  374  1                                  20    
HELIX   18  18 PHE A  382  VAL A  394  1                                  13    
HELIX   19  19 SER A  405  PHE A  415  1                                  11    
HELIX   20  20 GLY A  435  LYS A  448  1                                  14    
HELIX   21  21 ASP A  457  ASP A  463  1                                   7    
HELIX   22  22 LEU A  464  GLY A  466  5                                   3    
HELIX   23  23 LEU A  467  GLY A  474  1                                   8    
HELIX   24  24 GLY A  487  LEU A  493  5                                   7    
HELIX   25  25 LEU A  493  SER A  497  5                                   5    
HELIX   26  26 GLU A  498  PHE A  506  1                                   9    
HELIX   27  27 PHE A  514  TYR A  521  1                                   8    
HELIX   28  28 SER A  530  TYR A  538  1                                   9    
HELIX   29  29 ASP A  555  LEU A  580  1                                  26    
HELIX   30  30 PRO B    5  SER B   20  1                                  16    
HELIX   31  31 SER B   33  HIS B   43  1                                  11    
HELIX   32  32 ASP B   53  GLN B   69  1                                  17    
HELIX   33  33 GLY B   79  ASN B   84  1                                   6    
HELIX   34  34 PHE B   85  ARG B   96  1                                  12    
HELIX   35  35 PRO B  107  ARG B  111  5                                   5    
HELIX   36  36 SER B  141  LYS B  161  1                                  21    
HELIX   37  37 ASP B  205  ALA B  219  1                                  15    
HELIX   38  38 SER B  231  GLN B  246  1                                  16    
HELIX   39  39 PRO B  253  ASN B  256  5                                   4    
HELIX   40  40 ALA B  270  LEU B  275  1                                   6    
HELIX   41  41 ASP B  277  LEU B  284  1                                   8    
HELIX   42  42 SER B  298  ASP B  308  1                                  11    
HELIX   43  43 ASN B  336  GLY B  347  1                                  12    
HELIX   44  44 SER B  355  THR B  374  1                                  20    
HELIX   45  45 PHE B  382  GLN B  391  1                                  10    
HELIX   46  46 SER B  405  PHE B  415  1                                  11    
HELIX   47  47 GLY B  435  LYS B  448  1                                  14    
HELIX   48  48 ASP B  457  ASP B  463  1                                   7    
HELIX   49  49 LEU B  464  GLY B  466  5                                   3    
HELIX   50  50 LEU B  467  LEU B  473  1                                   7    
HELIX   51  51 GLY B  487  LEU B  493  5                                   7    
HELIX   52  52 LEU B  493  GLU B  498  5                                   6    
HELIX   53  53 HIS B  501  PHE B  506  1                                   6    
HELIX   54  54 PHE B  514  TYR B  521  1                                   8    
HELIX   55  55 SER B  530  TYR B  538  1                                   9    
HELIX   56  56 ASP B  555  LYS B  576  1                                  22    
HELIX   57  57 GLN B  577  GLU B  579  5                                   3    
HELIX   58  58 PRO C    5  SER C   20  1                                  16    
HELIX   59  59 SER C   33  HIS C   43  1                                  11    
HELIX   60  60 ASP C   53  GLN C   69  1                                  17    
HELIX   61  61 GLY C   79  ASN C   84  1                                   6    
HELIX   62  62 PHE C   85  ARG C   96  1                                  12    
HELIX   63  63 PRO C  107  ARG C  111  5                                   5    
HELIX   64  64 PHE C  125  VAL C  129  5                                   5    
HELIX   65  65 SER C  141  LYS C  161  1                                  21    
HELIX   66  66 ARG C  206  SER C  208  5                                   3    
HELIX   67  67 LEU C  209  GLU C  218  1                                  10    
HELIX   68  68 SER C  231  GLN C  246  1                                  16    
HELIX   69  69 PRO C  253  ASN C  256  5                                   4    
HELIX   70  70 ALA C  270  LEU C  275  1                                   6    
HELIX   71  71 ASP C  277  LEU C  284  1                                   8    
HELIX   72  72 SER C  298  ASP C  308  1                                  11    
HELIX   73  73 ASN C  336  ALA C  346  1                                  11    
HELIX   74  74 SER C  355  THR C  374  1                                  20    
HELIX   75  75 PHE C  382  VAL C  394  1                                  13    
HELIX   76  76 SER C  405  PHE C  415  1                                  11    
HELIX   77  77 GLY C  435  LYS C  448  1                                  14    
HELIX   78  78 ASP C  457  ASP C  463  1                                   7    
HELIX   79  79 LEU C  464  GLY C  466  5                                   3    
HELIX   80  80 LEU C  467  GLY C  474  1                                   8    
HELIX   81  81 GLY C  487  LEU C  493  5                                   7    
HELIX   82  82 LEU C  493  SER C  497  5                                   5    
HELIX   83  83 GLU C  498  PHE C  506  1                                   9    
HELIX   84  84 PHE C  514  TYR C  521  1                                   8    
HELIX   85  85 SER C  530  TYR C  538  1                                   9    
HELIX   86  86 ASP C  555  TRP C  578  1                                  24    
HELIX   87  87 PRO D    5  SER D   20  1                                  16    
HELIX   88  88 SER D   33  HIS D   43  1                                  11    
HELIX   89  89 ASP D   53  GLN D   69  1                                  17    
HELIX   90  90 GLY D   79  ASN D   84  1                                   6    
HELIX   91  91 PHE D   85  ARG D   96  1                                  12    
HELIX   92  92 PRO D  107  ARG D  111  5                                   5    
HELIX   93  93 PHE D  125  VAL D  129  5                                   5    
HELIX   94  94 SER D  141  LYS D  161  1                                  21    
HELIX   95  95 LEU D  209  ALA D  219  1                                  11    
HELIX   96  96 SER D  231  GLN D  246  1                                  16    
HELIX   97  97 PRO D  253  ASN D  256  5                                   4    
HELIX   98  98 ALA D  270  LEU D  275  1                                   6    
HELIX   99  99 ASP D  277  ARG D  285  1                                   9    
HELIX  100 100 SER D  298  ASP D  308  1                                  11    
HELIX  101 101 ASN D  336  LEU D  348  1                                  13    
HELIX  102 102 SER D  355  THR D  374  1                                  20    
HELIX  103 103 PHE D  382  GLN D  391  1                                  10    
HELIX  104 104 SER D  405  PHE D  415  1                                  11    
HELIX  105 105 GLY D  435  LYS D  448  1                                  14    
HELIX  106 106 ASP D  457  ASP D  463  1                                   7    
HELIX  107 107 LEU D  464  GLY D  466  5                                   3    
HELIX  108 108 LEU D  467  LEU D  473  1                                   7    
HELIX  109 109 GLY D  487  LEU D  493  5                                   7    
HELIX  110 110 LEU D  493  SER D  497  5                                   5    
HELIX  111 111 GLU D  498  PHE D  506  1                                   9    
HELIX  112 112 PHE D  514  TYR D  521  1                                   8    
HELIX  113 113 SER D  530  TYR D  538  1                                   9    
HELIX  114 114 ASP D  555  LEU D  580  1                                  26    
SHEET    1  AA 6 SER A  47  VAL A  50  0                                        
SHEET    2  AA 6 ASP A  24  VAL A  27  1  O  ALA A  25   N  HIS A  49           
SHEET    3  AA 6 VAL A  72  CYS A  76  1  O  LEU A  73   N  VAL A  26           
SHEET    4  AA 6 ILE A  99  ASP A 105  1  O  ILE A 100   N  LEU A  74           
SHEET    5  AA 6 PRO A 166  PRO A 172  1  O  VAL A 167   N  VAL A 101           
SHEET    6  AA 6 PHE A 132  ASP A 134  1  O  THR A 133   N  ASN A 170           
SHEET    1  AB 7 SER A 196  LYS A 198  0                                        
SHEET    2  AB 7 HIS D 331  ILE D 333  1  O  MET D 332   N  LYS A 198           
SHEET    3  AB 7 GLN D 312  ILE D 316  1  O  VAL D 315   N  ILE D 333           
SHEET    4  AB 7 VAL D 288  PHE D 292  1  O  VAL D 289   N  ILE D 314           
SHEET    5  AB 7 GLY D 222  CYS D 226  1  O  MET D 223   N  ILE D 290           
SHEET    6  AB 7 ILE D 249  ALA D 251  1  O  LEU D 250   N  CYS D 226           
SHEET    7  AB 7 VAL D 267  ILE D 268  1  O  ILE D 268   N  ALA D 251           
SHEET    1  AC 2 THR A 201  SER A 203  0                                        
SHEET    2  AC 2 THR D 201  SER D 203 -1  O  THR D 201   N  SER A 203           
SHEET    1  AD 7 VAL A 267  ILE A 268  0                                        
SHEET    2  AD 7 ILE A 249  ALA A 251  1  O  ILE A 249   N  ILE A 268           
SHEET    3  AD 7 GLY A 222  CYS A 226  1  O  ILE A 224   N  LEU A 250           
SHEET    4  AD 7 VAL A 288  PHE A 292  1  O  VAL A 288   N  MET A 223           
SHEET    5  AD 7 GLN A 312  ILE A 316  1  O  GLN A 312   N  VAL A 289           
SHEET    6  AD 7 HIS A 331  ILE A 333  1  O  HIS A 331   N  VAL A 315           
SHEET    7  AD 7 SER D 196  LYS D 198  1  O  SER D 196   N  MET A 332           
SHEET    1  AE 6 ARG A 423  TYR A 425  0                                        
SHEET    2  AE 6 SER A 399  VAL A 402  1  O  LEU A 400   N  TYR A 425           
SHEET    3  AE 6 VAL A 451  GLY A 456  1  O  THR A 452   N  PHE A 401           
SHEET    4  AE 6 LEU A 477  ASN A 483  1  O  THR A 478   N  LEU A 453           
SHEET    5  AE 6 LEU A 547  LYS A 553  1  O  HIS A 548   N  VAL A 479           
SHEET    6  AE 6 THR A 524  SER A 526  1  O  THR A 524   N  LEU A 549           
SHEET    1  BA 6 SER B  47  VAL B  50  0                                        
SHEET    2  BA 6 ASP B  24  VAL B  27  1  O  ALA B  25   N  HIS B  49           
SHEET    3  BA 6 VAL B  72  CYS B  76  1  O  LEU B  73   N  VAL B  26           
SHEET    4  BA 6 ILE B  99  ASP B 105  1  O  ILE B 100   N  LEU B  74           
SHEET    5  BA 6 PRO B 166  PRO B 172  1  O  VAL B 167   N  VAL B 101           
SHEET    6  BA 6 PHE B 132  ASP B 134  1  O  THR B 133   N  ASN B 170           
SHEET    1  BB 7 SER B 196  LYS B 198  0                                        
SHEET    2  BB 7 HIS C 331  ILE C 333  1  O  MET C 332   N  LYS B 198           
SHEET    3  BB 7 GLN C 312  ILE C 316  1  O  VAL C 315   N  ILE C 333           
SHEET    4  BB 7 VAL C 288  PHE C 292  1  O  VAL C 289   N  ILE C 314           
SHEET    5  BB 7 GLY C 222  CYS C 226  1  O  MET C 223   N  ILE C 290           
SHEET    6  BB 7 ILE C 249  ALA C 251  1  O  LEU C 250   N  CYS C 226           
SHEET    7  BB 7 VAL C 267  ILE C 268  1  O  ILE C 268   N  ALA C 251           
SHEET    1  BC 2 THR B 201  SER B 203  0                                        
SHEET    2  BC 2 THR C 201  SER C 203 -1  O  THR C 201   N  SER B 203           
SHEET    1  BD 7 VAL B 267  ILE B 268  0                                        
SHEET    2  BD 7 ILE B 249  ALA B 251  1  O  ILE B 249   N  ILE B 268           
SHEET    3  BD 7 GLY B 222  CYS B 226  1  O  ILE B 224   N  LEU B 250           
SHEET    4  BD 7 VAL B 288  PHE B 292  1  O  VAL B 288   N  MET B 223           
SHEET    5  BD 7 GLN B 312  ILE B 316  1  O  GLN B 312   N  VAL B 289           
SHEET    6  BD 7 HIS B 331  ILE B 333  1  O  HIS B 331   N  VAL B 315           
SHEET    7  BD 7 SER C 196  LYS C 198  1  O  SER C 196   N  MET B 332           
SHEET    1  BE 6 ARG B 423  TYR B 425  0                                        
SHEET    2  BE 6 SER B 399  VAL B 402  1  O  LEU B 400   N  TYR B 425           
SHEET    3  BE 6 VAL B 451  GLY B 456  1  O  THR B 452   N  PHE B 401           
SHEET    4  BE 6 LEU B 477  ASN B 483  1  O  THR B 478   N  LEU B 453           
SHEET    5  BE 6 LEU B 547  LYS B 553  1  O  HIS B 548   N  VAL B 479           
SHEET    6  BE 6 THR B 524  SER B 526  1  O  THR B 524   N  LEU B 549           
SHEET    1  CA 6 SER C  47  VAL C  50  0                                        
SHEET    2  CA 6 ASP C  24  VAL C  27  1  O  ALA C  25   N  HIS C  49           
SHEET    3  CA 6 VAL C  72  CYS C  76  1  O  LEU C  73   N  VAL C  26           
SHEET    4  CA 6 ILE C  99  ASP C 105  1  O  ILE C 100   N  LEU C  74           
SHEET    5  CA 6 PRO C 166  PRO C 172  1  O  VAL C 167   N  VAL C 101           
SHEET    6  CA 6 PHE C 132  ASP C 134  1  O  THR C 133   N  ASN C 170           
SHEET    1  CB 6 ARG C 423  SER C 426  0                                        
SHEET    2  CB 6 SER C 399  VAL C 402  1  O  LEU C 400   N  TYR C 425           
SHEET    3  CB 6 VAL C 451  GLY C 456  1  O  THR C 452   N  PHE C 401           
SHEET    4  CB 6 LEU C 477  ASN C 483  1  O  THR C 478   N  LEU C 453           
SHEET    5  CB 6 LEU C 547  LYS C 553  1  O  HIS C 548   N  VAL C 479           
SHEET    6  CB 6 THR C 524  SER C 526  1  O  THR C 524   N  LEU C 549           
SHEET    1  DA 6 SER D  47  VAL D  50  0                                        
SHEET    2  DA 6 ASP D  24  VAL D  27  1  O  ALA D  25   N  HIS D  49           
SHEET    3  DA 6 VAL D  72  CYS D  76  1  O  LEU D  73   N  VAL D  26           
SHEET    4  DA 6 ILE D  99  ASP D 105  1  O  ILE D 100   N  LEU D  74           
SHEET    5  DA 6 PRO D 166  PRO D 172  1  O  VAL D 167   N  VAL D 101           
SHEET    6  DA 6 PHE D 132  ASP D 134  1  O  THR D 133   N  ASN D 170           
SHEET    1  DB 6 ARG D 423  TYR D 425  0                                        
SHEET    2  DB 6 SER D 399  VAL D 402  1  O  LEU D 400   N  TYR D 425           
SHEET    3  DB 6 VAL D 451  GLY D 456  1  O  THR D 452   N  PHE D 401           
SHEET    4  DB 6 LEU D 477  ASN D 483  1  O  THR D 478   N  LEU D 453           
SHEET    5  DB 6 LEU D 547  LYS D 553  1  O  HIS D 548   N  VAL D 479           
SHEET    6  DB 6 THR D 524  SER D 526  1  O  THR D 524   N  LEU D 549           
LINK        MN    MN A 602                 OD1 ASP A 457     1555   1555  2.15  
LINK        MN    MN A 602                 OD1 ASN A 484     1555   1555  2.24  
LINK        MN    MN A 602                 O   GLY A 486     1555   1555  2.22  
LINK        MN    MN A 602                 O1A TPP A 601     1555   1555  2.04  
LINK        MN    MN A 602                 O3B TPP A 601     1555   1555  1.98  
LINK        MN    MN A 602                 O   HOH A2237     1555   1555  2.43  
LINK        NA    NA A1581                 O   HOH A2022     1555   1555  3.18  
LINK        NA    NA A1581                 O   CYS A  40     1555   1555  2.68  
LINK        NA    NA A1581                 O   ALA A  41     1555   1555  2.41  
LINK        NA    NA A1581                 O   HIS A  43     1555   1555  2.34  
LINK        NA    NA A1581                 O   ILE A  46     1555   1555  2.53  
LINK        MN    MN B 602                 O1A TPP B 601     1555   1555  2.19  
LINK        MN    MN B 602                 OD1 ASN B 484     1555   1555  2.25  
LINK        MN    MN B 602                 O1B TPP B 601     1555   1555  1.99  
LINK        MN    MN B 602                 O   HOH B2239     1555   1555  2.49  
LINK        MN    MN B 602                 OD1 ASP B 457     1555   1555  2.15  
LINK        MN    MN B 602                 O   GLY B 486     1555   1555  2.08  
LINK        NA    NA B1581                 O   ALA B  41     1555   1555  2.74  
LINK        NA    NA B1581                 O   HIS B  43     1555   1555  2.43  
LINK        NA    NA B1581                 O   CYS B  40     1555   1555  2.74  
LINK        NA    NA B1581                 O   ILE B  46     1555   1555  2.23  
LINK        NA    NA B1581                 O   HOH B2022     1555   1555  2.41  
LINK        NA    NA B1581                 O   HOH B2024     1555   1555  2.98  
LINK        MN    MN C 602                 O   HOH C2253     1555   1555  2.05  
LINK        MN    MN C 602                 OD1 ASP C 457     1555   1555  2.23  
LINK        MN    MN C 602                 OD1 ASN C 484     1555   1555  2.06  
LINK        MN    MN C 602                 O   GLY C 486     1555   1555  2.10  
LINK        MN    MN C 602                 O3B TPP C 601     1555   1555  2.15  
LINK        MN    MN C 602                 O1A TPP C 601     1555   1555  2.10  
LINK        NA    NA C1579                 O   HOH C2018     1555   1555  3.10  
LINK        NA    NA C1579                 O   HOH C2015     1555   1555  2.33  
LINK        NA    NA C1579                 O   ILE C  46     1555   1555  2.54  
LINK        NA    NA C1579                 O   ALA C  41     1555   1555  2.41  
LINK        NA    NA C1579                 O   CYS C  40     1555   1555  2.73  
LINK        NA    NA C1579                 O   HIS C  43     1555   1555  2.43  
LINK        MN    MN D 602                 O1A TPP D 601     1555   1555  2.07  
LINK        MN    MN D 602                 OD1 ASP D 457     1555   1555  2.23  
LINK        MN    MN D 602                 O   HOH D2292     1555   1555  2.29  
LINK        MN    MN D 602                 O1B TPP D 601     1555   1555  2.03  
LINK        MN    MN D 602                 OD1 ASN D 484     1555   1555  2.22  
LINK        MN    MN D 602                 O   GLY D 486     1555   1555  2.20  
LINK        NA    NA D1581                 O   HIS D  43     1555   1555  2.30  
LINK        NA    NA D1581                 O   ALA D  41     1555   1555  2.62  
LINK        NA    NA D1581                 O   CYS D  40     1555   1555  2.55  
LINK        NA    NA D1581                 O   ILE D  46     1555   1555  2.24  
SITE     1 AC1 23 SER A 405  MET A 406  ASN A 431  ILE A 433                    
SITE     2 AC1 23 ASP A 434  GLY A 456  ASP A 457  LEU A 458                    
SITE     3 AC1 23 SER A 459  ASN A 484  GLY A 486  GLY A 487                    
SITE     4 AC1 23 GLY A 488  ILE A 489  PHE A 490   MN A 602                    
SITE     5 AC1 23 HOH A2200  HOH A2213  HOH A2237  HOH A2282                    
SITE     6 AC1 23 GLU B  54  GLN B 117  EDO B 603                               
SITE     1 AC2  5 ASP A 457  ASN A 484  GLY A 486  TPP A 601                    
SITE     2 AC2  5 HOH A2237                                                     
SITE     1 AC3  8 GLY A  30  SER A  31  ARG A  32  THR A  77                    
SITE     2 AC3  8 ARG A 106  GLN A 117  PHE B 490  TPP B 601                    
SITE     1 AC4 21 GLU A  54  GLN A 117  EDO A 603  SER B 405                    
SITE     2 AC4 21 MET B 406  ASN B 431  ILE B 433  ASP B 434                    
SITE     3 AC4 21 GLY B 456  ASP B 457  LEU B 458  SER B 459                    
SITE     4 AC4 21 ASN B 484  GLY B 486  GLY B 487  GLY B 488                    
SITE     5 AC4 21 ILE B 489   MN B 602  HOH B2155  HOH B2238                    
SITE     6 AC4 21 HOH B2239                                                     
SITE     1 AC5  5 ASP B 457  ASN B 484  GLY B 486  TPP B 601                    
SITE     2 AC5  5 HOH B2239                                                     
SITE     1 AC6  7 PHE A 490  TPP A 601  GLY B  30  SER B  31                    
SITE     2 AC6  7 ARG B  32  THR B  77  GLN B 117                               
SITE     1 AC7 26 SER C 405  MET C 406  PRO C 407  ASN C 431                    
SITE     2 AC7 26 GLY C 432  ILE C 433  ASP C 434  GLY C 456                    
SITE     3 AC7 26 ASP C 457  LEU C 458  SER C 459  ASN C 484                    
SITE     4 AC7 26 GLY C 486  GLY C 487  GLY C 488  ILE C 489                    
SITE     5 AC7 26 PHE C 490   MN C 602  HOH C2251  HOH C2252                    
SITE     6 AC7 26 HOH C2253  PRO D  29  GLU D  54  THR D  80                    
SITE     7 AC7 26 GLN D 117  EDO D 603                                          
SITE     1 AC8  5 ASP C 457  ASN C 484  GLY C 486  TPP C 601                    
SITE     2 AC8  5 HOH C2253                                                     
SITE     1 AC9  7 GLY C  30  SER C  31  ARG C  32  THR C  77                    
SITE     2 AC9  7 GLN C 117  PHE D 490  TPP D 601                               
SITE     1 BC1 25 PRO C  29  GLU C  54  THR C  80  GLN C 117                    
SITE     2 BC1 25 EDO C 603  SER D 405  MET D 406  ASN D 431                    
SITE     3 BC1 25 ILE D 433  ASP D 434  GLY D 456  ASP D 457                    
SITE     4 BC1 25 LEU D 458  SER D 459  ASN D 484  GLY D 486                    
SITE     5 BC1 25 GLY D 487  GLY D 488  ILE D 489  PHE D 490                    
SITE     6 BC1 25  MN D 602  HOH D2206  HOH D2290  HOH D2291                    
SITE     7 BC1 25 HOH D2292                                                     
SITE     1 BC2  5 ASP D 457  ASN D 484  GLY D 486  TPP D 601                    
SITE     2 BC2  5 HOH D2292                                                     
SITE     1 BC3  7 PHE C 490  TPP C 601  GLY D  30  SER D  31                    
SITE     2 BC3  7 ARG D  32  THR D  77  GLN D 117                               
SITE     1 BC4  4 CYS D  40  ALA D  41  HIS D  43  ILE D  46                    
SITE     1 BC5  4 CYS A  40  ALA A  41  HIS A  43  ILE A  46                    
SITE     1 BC6  6 CYS B  40  ALA B  41  HIS B  43  ILE B  46                    
SITE     2 BC6  6 HOH B2022  HOH B2024                                          
SITE     1 BC7  5 CYS C  40  ALA C  41  HIS C  43  ILE C  46                    
SITE     2 BC7  5 HOH C2015                                                     
SITE     1 BC8  7 ARG A  32  PRO A 107  LEU A 110  LEU A 173                    
SITE     2 BC8  7 ARG A 174  GLU A 175  HOH A2283                               
SITE     1 BC9  6 ARG B  32  PRO B 107  LEU B 110  LEU B 173                    
SITE     2 BC9  6 ARG B 174  GLU B 175                                          
SITE     1 CC1  7 ARG D  32  PRO D 107  LEU D 110  ARG D 174                    
SITE     2 CC1  7 GLU D 175  HOH D2041  HOH D2293                               
SITE     1 CC2  9 ARG C  32  PRO C 107  GLU C 109  LEU C 110                    
SITE     2 CC2  9 LEU C 173  ARG C 174  GLU C 175  HOH C2254                    
SITE     3 CC2  9 HOH C2255                                                     
SITE     1 CC3  4 LYS A 276  ARG A 564  HOH A2284  HOH A2285                    
SITE     1 CC4  3 LYS B 276  ARG B 564  HOH B2121                               
SITE     1 CC5  4 LYS C 276  PHE C 492  ARG C 564  HOH C2256                    
SITE     1 CC6  3 LYS D 276  PHE D 492  ARG D 564                               
CRYST1  100.180  152.990  158.499  90.00  90.00  90.00 P 21 21 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      0.009982  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006536  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006309        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system