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Database: PDB
Entry: 1V1J
LinkDB: 1V1J
Original site: 1V1J 
HEADER    LYASE                                   16-APR-04   1V1J              
TITLE     CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINTAE DEHYDRATASE FROM          
TITLE    2 STREPTOMYCES COELICOLOR IN COMPLEX WITH 3-FLUORO                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3-DEHYDROQUINATE DEHYDRATASE;                              
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   4 SYNONYM: 3-DEHYDROQUINASE, TYPE II DHQASE;                           
COMPND   5 EC: 4.2.1.10;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR;                        
SOURCE   3 ORGANISM_TAXID: 1902;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PTB361                                    
KEYWDS    DHQ, SHIKIMATE, DEHYDROQUINASE, AROMATIC AMINO ACID BIOSYNTHESIS,     
KEYWDS   2 LYASE                                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.W.ROSZAK,J.R.COGGINS,A.J.LAPTHORN                                   
REVDAT   3   28-JUN-17 1V1J    1       REMARK                                   
REVDAT   2   24-FEB-09 1V1J    1       VERSN                                    
REVDAT   1   26-JAN-05 1V1J    0                                                
JRNL        AUTH   M.FREDERICKSON,A.W.ROSZAK,J.R.COGGINS,A.J.LAPTHORN,C.ABELL   
JRNL        TITL   (1R,4S,5R)-3-FLUORO-1,4,                                     
JRNL        TITL 2 5-TRIHYDROXY-2-CYCLOHEXENE-1-CARBOXYLIC ACID: THE FLUORO     
JRNL        TITL 3 ANALOGUE OF THE ENOLATE INTERMEDIATE IN THE REACTION         
JRNL        TITL 4 CATALYZED BY TYPE II DEHYDROQUINASES                         
JRNL        REF    ORG.BIOMOL.CHEM.              V.   2  1592 2004              
JRNL        REFN                   ISSN 1477-0520                               
JRNL        PMID   15162210                                                     
JRNL        DOI    10.1039/B404535A                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 85.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 89858                          
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) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 12.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 10066                           
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13488                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 188                                     
REMARK   3   SOLVENT ATOMS            : 700                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.11                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.82000                                              
REMARK   3    B22 (A**2) : -1.15000                                             
REMARK   3    B33 (A**2) : -0.68000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.349         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.230         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.241         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.911         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1V1J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-APR-04.                  
REMARK 100 THE DEPOSITION ID IS D_1290014989.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : ENRAF-NONIUS FR591                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MACSCIENCE                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 113346                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.16000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.9700                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.77000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.850                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1GUO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, NA/K PHOSPHATE, TRIS BUFFER,   
REMARK 280  PH 7.50                                                             
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       58.23750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.96250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       69.47050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.96250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       58.23750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       69.47050            
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: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L                                  
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     0                                                      
REMARK 465     ALA A   151                                                      
REMARK 465     GLY A   152                                                      
REMARK 465     SER A   153                                                      
REMARK 465     ALA A   154                                                      
REMARK 465     ARG A   155                                                      
REMARK 465     ALA A   156                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ALA B   151                                                      
REMARK 465     GLY B   152                                                      
REMARK 465     SER B   153                                                      
REMARK 465     ALA B   154                                                      
REMARK 465     ARG B   155                                                      
REMARK 465     ALA B   156                                                      
REMARK 465     MET C     0                                                      
REMARK 465     ALA C   151                                                      
REMARK 465     GLY C   152                                                      
REMARK 465     SER C   153                                                      
REMARK 465     ALA C   154                                                      
REMARK 465     ARG C   155                                                      
REMARK 465     ALA C   156                                                      
REMARK 465     MET D     0                                                      
REMARK 465     ALA D   151                                                      
REMARK 465     GLY D   152                                                      
REMARK 465     SER D   153                                                      
REMARK 465     ALA D   154                                                      
REMARK 465     ARG D   155                                                      
REMARK 465     ALA D   156                                                      
REMARK 465     MET E     0                                                      
REMARK 465     ALA E   151                                                      
REMARK 465     GLY E   152                                                      
REMARK 465     SER E   153                                                      
REMARK 465     ALA E   154                                                      
REMARK 465     ARG E   155                                                      
REMARK 465     ALA E   156                                                      
REMARK 465     MET F     0                                                      
REMARK 465     ALA F   151                                                      
REMARK 465     GLY F   152                                                      
REMARK 465     SER F   153                                                      
REMARK 465     ALA F   154                                                      
REMARK 465     ARG F   155                                                      
REMARK 465     ALA F   156                                                      
REMARK 465     MET G     0                                                      
REMARK 465     ALA G   151                                                      
REMARK 465     GLY G   152                                                      
REMARK 465     SER G   153                                                      
REMARK 465     ALA G   154                                                      
REMARK 465     ARG G   155                                                      
REMARK 465     ALA G   156                                                      
REMARK 465     MET H     0                                                      
REMARK 465     ALA H   151                                                      
REMARK 465     GLY H   152                                                      
REMARK 465     SER H   153                                                      
REMARK 465     ALA H   154                                                      
REMARK 465     ARG H   155                                                      
REMARK 465     ALA H   156                                                      
REMARK 465     MET I     0                                                      
REMARK 465     ALA I   151                                                      
REMARK 465     GLY I   152                                                      
REMARK 465     SER I   153                                                      
REMARK 465     ALA I   154                                                      
REMARK 465     ARG I   155                                                      
REMARK 465     ALA I   156                                                      
REMARK 465     MET J     0                                                      
REMARK 465     ALA J   151                                                      
REMARK 465     GLY J   152                                                      
REMARK 465     SER J   153                                                      
REMARK 465     ALA J   154                                                      
REMARK 465     ARG J   155                                                      
REMARK 465     ALA J   156                                                      
REMARK 465     MET K     0                                                      
REMARK 465     ALA K   151                                                      
REMARK 465     GLY K   152                                                      
REMARK 465     SER K   153                                                      
REMARK 465     ALA K   154                                                      
REMARK 465     ARG K   155                                                      
REMARK 465     ALA K   156                                                      
REMARK 465     MET L     0                                                      
REMARK 465     ALA L   151                                                      
REMARK 465     GLY L   152                                                      
REMARK 465     SER L   153                                                      
REMARK 465     ALA L   154                                                      
REMARK 465     ARG L   155                                                      
REMARK 465     ALA L   156                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  26    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  26    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  26    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  26    CG   CD   OE1  OE2                                  
REMARK 470     GLU E  26    CG   CD   OE1  OE2                                  
REMARK 470     GLU F  26    CG   CD   OE1  OE2                                  
REMARK 470     GLU G  26    CG   CD   OE1  OE2                                  
REMARK 470     GLU H  26    CG   CD   OE1  OE2                                  
REMARK 470     GLU I  26    CG   CD   OE1  OE2                                  
REMARK 470     GLU J  26    CG   CD   OE1  OE2                                  
REMARK 470     GLU K  26    CG   CD   OE1  OE2                                  
REMARK 470     GLU L  26    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH D  2037     O    HOH E  2046              0.33            
REMARK 500   O    HOH I  2053     O    HOH I  2054              0.35            
REMARK 500   O    HOH G  2051     O    HOH G  2052              0.38            
REMARK 500   O    HOH L  2045     O    HOH L  2046              0.39            
REMARK 500   O    HOH F  2049     O    HOH H  2047              0.40            
REMARK 500   O    HOH C  2048     O    HOH J  2050              0.42            
REMARK 500   O    HOH E  2048     O    HOH L  2049              0.44            
REMARK 500   O    HOH G  2048     O    HOH G  2049              0.46            
REMARK 500   O    HOH G  2037     O    HOH H  2028              0.48            
REMARK 500   O    HOH I  2039     O    HOH I  2042              0.48            
REMARK 500   O    HOH D  2047     O    HOH D  2048              0.48            
REMARK 500   O    HOH F  2050     O    HOH F  2051              0.51            
REMARK 500   O    HOH I  2055     O    HOH I  2056              0.53            
REMARK 500   O    HOH H  2049     O    HOH H  2050              0.54            
REMARK 500   O    HOH K  2048     O    HOH K  2049              0.55            
REMARK 500   O    HOH A  2050     O    HOH D  2051              0.55            
REMARK 500   O    HOH I  2049     O    HOH I  2050              0.59            
REMARK 500   O    HOH A  2041     O    HOH B  2046              0.59            
REMARK 500   O    HOH A  2051     O    HOH A  2052              0.60            
REMARK 500   O    HOH E  2049     O    HOH E  2050              0.63            
REMARK 500   O    HOH J  2037     O    HOH J  2038              0.64            
REMARK 500   O    HOH D  2053     O    HOH D  2054              0.66            
REMARK 500   O    HOH L  2050     O    HOH L  2051              0.67            
REMARK 500   O    HOH A  2055     O    HOH A  2057              0.68            
REMARK 500   O    HOH I  2057     O    HOH K  2055              0.68            
REMARK 500   O    HOH B  2049     O    HOH B  2050              0.69            
REMARK 500   O    HOH C  2049     O    HOH C  2050              0.69            
REMARK 500   O    HOH F  2028     O    HOH F  2046              0.70            
REMARK 500   O    HOH B  2056     O    HOH B  2057              0.71            
REMARK 500   O    HOH F  2038     O    HOH F  2039              0.73            
REMARK 500   O    HOH K  2037     O    HOH K  2038              0.75            
REMARK 500   O    HOH J  2052     O    HOH J  2053              0.75            
REMARK 500   O    HOH A  2053     O    HOH D  2061              0.76            
REMARK 500   O    HOH L  2058     O    HOH L  2060              0.78            
REMARK 500   O    HOH I  2038     O    HOH I  2041              0.78            
REMARK 500   O    HOH F  2052     O    HOH H  2055              0.78            
REMARK 500   O    HOH D  2038     O    HOH D  2039              0.79            
REMARK 500   O    HOH H  2052     O    HOH H  2054              0.80            
REMARK 500   O    HOH E  2038     O    HOH E  2039              0.81            
REMARK 500   O    HOH C  2026     O    HOH C  2045              0.83            
REMARK 500   O    HOH J  2028     O    HOH J  2046              0.83            
REMARK 500   O    HOH A  2029     O    HOH C  2038              0.84            
REMARK 500   O    HOH B  2053     O    HOH G  2057              0.86            
REMARK 500   O    HOH F  2055     O    HOH F  2056              0.86            
REMARK 500   O    HOH A  2038     O    HOH A  2040              0.86            
REMARK 500   O    HOH G  2038     O    HOH G  2039              0.89            
REMARK 500   O    HOH C  2051     O    HOH J  2058              0.89            
REMARK 500   O    HOH H  2036     O    HOH H  2037              0.91            
REMARK 500   O    HOH L  2036     O    HOH L  2038              0.92            
REMARK 500   O    HOH A  2014     O    HOH D  2056              0.94            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      76 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A 144   CZ    ARG A 144   NH1    -0.196                       
REMARK 500    ARG A 144   CZ    ARG A 144   NH2    -0.135                       
REMARK 500    ARG E  70   CZ    ARG E  70   NH2     0.079                       
REMARK 500    ARG L  70   CZ    ARG L  70   NH2     0.085                       
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    MET A  10   CG  -  SD  -  CE  ANGL. DEV. =  12.2 DEGREES          
REMARK 500    ASP A  31   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A  70   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 144   NH1 -  CZ  -  NH2 ANGL. DEV. = -18.6 DEGREES          
REMARK 500    ARG A 144   NE  -  CZ  -  NH1 ANGL. DEV. =   7.8 DEGREES          
REMARK 500    ARG A 144   NE  -  CZ  -  NH2 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    MET B  10   CG  -  SD  -  CE  ANGL. DEV. =  12.3 DEGREES          
REMARK 500    ARG B  70   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ASP B 127   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG B 144   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    MET C  10   CG  -  SD  -  CE  ANGL. DEV. =  14.9 DEGREES          
REMARK 500    ASP C  31   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP C  35   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP C 127   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ARG C 144   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG D  70   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ASP D 127   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG D 144   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    MET E  10   CG  -  SD  -  CE  ANGL. DEV. =  11.9 DEGREES          
REMARK 500    ASP E  31   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP E  35   CB  -  CG  -  OD2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    ARG E  70   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG E  70   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ASP E 127   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG E 144   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    MET F  10   CG  -  SD  -  CE  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    ARG F  70   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG F 144   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    MET G  10   CG  -  SD  -  CE  ANGL. DEV. =  18.6 DEGREES          
REMARK 500    ARG G  70   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP G  92   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP G 127   CB  -  CG  -  OD2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ARG G 144   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ASP H  35   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP H  92   CB  -  CG  -  OD1 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ASP H 127   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG H 144   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP I  31   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG I  70   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP I 127   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG I 144   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    MET J  10   CG  -  SD  -  CE  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    ASP J  52   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP J 127   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG J 144   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    MET K  10   CG  -  SD  -  CE  ANGL. DEV. =  12.8 DEGREES          
REMARK 500    ARG K  70   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ASP K 127   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG K 144   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    MET L  10   CG  -  SD  -  CE  ANGL. DEV. =  14.4 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 ANGLE DEVIATIONS.                             
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    ASN A  16       -2.82     62.39                                   
REMARK 500    ALA A  81     -134.17     46.68                                   
REMARK 500    ARG A 113     -158.55   -110.37                                   
REMARK 500    ASN B  16       -3.04     60.31                                   
REMARK 500    ALA B  81     -132.47     43.06                                   
REMARK 500    ARG B 113     -155.93   -111.15                                   
REMARK 500    ASN C  16       -5.04     65.35                                   
REMARK 500    ALA C  81     -129.55     48.72                                   
REMARK 500    ARG C 113     -156.78   -109.19                                   
REMARK 500    ASN D  16       -6.75     65.48                                   
REMARK 500    ALA D  81     -132.61     45.73                                   
REMARK 500    ARG D 113     -155.09   -108.65                                   
REMARK 500    ASN E  16       -7.04     64.72                                   
REMARK 500    ALA E  81     -133.43     50.05                                   
REMARK 500    ARG E 113     -160.17   -107.81                                   
REMARK 500    ASN F  16       -3.54     66.92                                   
REMARK 500    ALA F  81     -128.12     45.98                                   
REMARK 500    ARG F 113     -158.46   -112.78                                   
REMARK 500    ASN G  16       -4.24     67.24                                   
REMARK 500    ALA G  81     -132.37     50.48                                   
REMARK 500    ARG G 113     -161.14   -108.76                                   
REMARK 500    ASN H  16       -3.64     68.27                                   
REMARK 500    ALA H  81     -132.16     47.43                                   
REMARK 500    ARG H 113     -158.58   -111.96                                   
REMARK 500    ASN I  16       -6.44     68.79                                   
REMARK 500    ALA I  81     -130.11     48.59                                   
REMARK 500    ARG I 113     -156.19   -111.08                                   
REMARK 500    ASN J  16       -4.58     63.72                                   
REMARK 500    ALA J  81     -128.21     46.76                                   
REMARK 500    ARG J 113     -158.84   -108.45                                   
REMARK 500    ASN K  16       -4.23     64.65                                   
REMARK 500    ALA K  81     -130.07     44.44                                   
REMARK 500    ARG K 113     -158.22   -110.69                                   
REMARK 500    ASN L  16       -2.95     62.46                                   
REMARK 500    ALA L  81     -133.44     49.38                                   
REMARK 500    ARG L 113     -158.83   -110.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 144         0.10    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FA3 A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A1151                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FA3 B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FA3 C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FA3 D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FA3 E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS E1151                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FA3 F 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FA3 G 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FA3 H 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FA3 I 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS I1151                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FA3 J 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FA3 K 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS K1151                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FA3 L 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1D0I   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINASE FROM STREPTOMYCES        
REMARK 900 COELICOLOR COMPLEXED WITH PHOSPHATE IONS                             
REMARK 900 RELATED ID: 1GTZ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF STREPTOMYCES COELICOLOR TYPE II DEHYDROQUINASE R23A     
REMARK 900 MUTANT IN COMPLEX WITH DEHYDROSHIKIMATE                              
REMARK 900 RELATED ID: 1GU0   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINASE FROM STREPTOMYCES        
REMARK 900 COELICOLOR                                                           
REMARK 900 RELATED ID: 1GU1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINASE FROM STREPTOMYCES        
REMARK 900 COELICOLOR COMPLEXED WITH 2,3-ANYDRO-QUINIC ACID                     
DBREF  1V1J A    0     0  PDB    1V1J     1V1J             0      0             
DBREF  1V1J A    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1V1J B    0     0  PDB    1V1J     1V1J             0      0             
DBREF  1V1J B    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1V1J C    0     0  PDB    1V1J     1V1J             0      0             
DBREF  1V1J C    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1V1J D    0     0  PDB    1V1J     1V1J             0      0             
DBREF  1V1J D    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1V1J E    0     0  PDB    1V1J     1V1J             0      0             
DBREF  1V1J E    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1V1J F    0     0  PDB    1V1J     1V1J             0      0             
DBREF  1V1J F    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1V1J G    0     0  PDB    1V1J     1V1J             0      0             
DBREF  1V1J G    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1V1J H    0     0  PDB    1V1J     1V1J             0      0             
DBREF  1V1J H    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1V1J I    0     0  PDB    1V1J     1V1J             0      0             
DBREF  1V1J I    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1V1J J    0     0  PDB    1V1J     1V1J             0      0             
DBREF  1V1J J    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1V1J K    0     0  PDB    1V1J     1V1J             0      0             
DBREF  1V1J K    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1V1J L    0     0  PDB    1V1J     1V1J             0      0             
DBREF  1V1J L    1   156  UNP    P15474   AROQ_STRCO       1    156             
SEQRES   1 A  157  MET PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU          
SEQRES   2 A  157  ASN GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO          
SEQRES   3 A  157  GLU ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA          
SEQRES   4 A  157  LEU CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL          
SEQRES   5 A  157  ASP PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP          
SEQRES   6 A  157  TRP ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL          
SEQRES   7 A  157  ILE ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE          
SEQRES   8 A  157  LEU ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL          
SEQRES   9 A  157  GLU VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE          
SEQRES  10 A  157  ARG HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL          
SEQRES  11 A  157  VAL ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL          
SEQRES  12 A  157  GLU ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG          
SEQRES  13 A  157  ALA                                                          
SEQRES   1 B  157  MET PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU          
SEQRES   2 B  157  ASN GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO          
SEQRES   3 B  157  GLU ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA          
SEQRES   4 B  157  LEU CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL          
SEQRES   5 B  157  ASP PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP          
SEQRES   6 B  157  TRP ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL          
SEQRES   7 B  157  ILE ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE          
SEQRES   8 B  157  LEU ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL          
SEQRES   9 B  157  GLU VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE          
SEQRES  10 B  157  ARG HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL          
SEQRES  11 B  157  VAL ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL          
SEQRES  12 B  157  GLU ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG          
SEQRES  13 B  157  ALA                                                          
SEQRES   1 C  157  MET PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU          
SEQRES   2 C  157  ASN GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO          
SEQRES   3 C  157  GLU ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA          
SEQRES   4 C  157  LEU CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL          
SEQRES   5 C  157  ASP PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP          
SEQRES   6 C  157  TRP ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL          
SEQRES   7 C  157  ILE ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE          
SEQRES   8 C  157  LEU ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL          
SEQRES   9 C  157  GLU VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE          
SEQRES  10 C  157  ARG HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL          
SEQRES  11 C  157  VAL ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL          
SEQRES  12 C  157  GLU ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG          
SEQRES  13 C  157  ALA                                                          
SEQRES   1 D  157  MET PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU          
SEQRES   2 D  157  ASN GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO          
SEQRES   3 D  157  GLU ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA          
SEQRES   4 D  157  LEU CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL          
SEQRES   5 D  157  ASP PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP          
SEQRES   6 D  157  TRP ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL          
SEQRES   7 D  157  ILE ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE          
SEQRES   8 D  157  LEU ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL          
SEQRES   9 D  157  GLU VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE          
SEQRES  10 D  157  ARG HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL          
SEQRES  11 D  157  VAL ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL          
SEQRES  12 D  157  GLU ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG          
SEQRES  13 D  157  ALA                                                          
SEQRES   1 E  157  MET PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU          
SEQRES   2 E  157  ASN GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO          
SEQRES   3 E  157  GLU ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA          
SEQRES   4 E  157  LEU CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL          
SEQRES   5 E  157  ASP PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP          
SEQRES   6 E  157  TRP ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL          
SEQRES   7 E  157  ILE ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE          
SEQRES   8 E  157  LEU ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL          
SEQRES   9 E  157  GLU VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE          
SEQRES  10 E  157  ARG HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL          
SEQRES  11 E  157  VAL ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL          
SEQRES  12 E  157  GLU ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG          
SEQRES  13 E  157  ALA                                                          
SEQRES   1 F  157  MET PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU          
SEQRES   2 F  157  ASN GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO          
SEQRES   3 F  157  GLU ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA          
SEQRES   4 F  157  LEU CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL          
SEQRES   5 F  157  ASP PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP          
SEQRES   6 F  157  TRP ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL          
SEQRES   7 F  157  ILE ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE          
SEQRES   8 F  157  LEU ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL          
SEQRES   9 F  157  GLU VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE          
SEQRES  10 F  157  ARG HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL          
SEQRES  11 F  157  VAL ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL          
SEQRES  12 F  157  GLU ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG          
SEQRES  13 F  157  ALA                                                          
SEQRES   1 G  157  MET PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU          
SEQRES   2 G  157  ASN GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO          
SEQRES   3 G  157  GLU ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA          
SEQRES   4 G  157  LEU CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL          
SEQRES   5 G  157  ASP PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP          
SEQRES   6 G  157  TRP ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL          
SEQRES   7 G  157  ILE ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE          
SEQRES   8 G  157  LEU ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL          
SEQRES   9 G  157  GLU VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE          
SEQRES  10 G  157  ARG HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL          
SEQRES  11 G  157  VAL ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL          
SEQRES  12 G  157  GLU ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG          
SEQRES  13 G  157  ALA                                                          
SEQRES   1 H  157  MET PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU          
SEQRES   2 H  157  ASN GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO          
SEQRES   3 H  157  GLU ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA          
SEQRES   4 H  157  LEU CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL          
SEQRES   5 H  157  ASP PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP          
SEQRES   6 H  157  TRP ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL          
SEQRES   7 H  157  ILE ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE          
SEQRES   8 H  157  LEU ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL          
SEQRES   9 H  157  GLU VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE          
SEQRES  10 H  157  ARG HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL          
SEQRES  11 H  157  VAL ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL          
SEQRES  12 H  157  GLU ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG          
SEQRES  13 H  157  ALA                                                          
SEQRES   1 I  157  MET PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU          
SEQRES   2 I  157  ASN GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO          
SEQRES   3 I  157  GLU ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA          
SEQRES   4 I  157  LEU CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL          
SEQRES   5 I  157  ASP PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP          
SEQRES   6 I  157  TRP ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL          
SEQRES   7 I  157  ILE ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE          
SEQRES   8 I  157  LEU ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL          
SEQRES   9 I  157  GLU VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE          
SEQRES  10 I  157  ARG HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL          
SEQRES  11 I  157  VAL ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL          
SEQRES  12 I  157  GLU ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG          
SEQRES  13 I  157  ALA                                                          
SEQRES   1 J  157  MET PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU          
SEQRES   2 J  157  ASN GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO          
SEQRES   3 J  157  GLU ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA          
SEQRES   4 J  157  LEU CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL          
SEQRES   5 J  157  ASP PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP          
SEQRES   6 J  157  TRP ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL          
SEQRES   7 J  157  ILE ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE          
SEQRES   8 J  157  LEU ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL          
SEQRES   9 J  157  GLU VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE          
SEQRES  10 J  157  ARG HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL          
SEQRES  11 J  157  VAL ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL          
SEQRES  12 J  157  GLU ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG          
SEQRES  13 J  157  ALA                                                          
SEQRES   1 K  157  MET PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU          
SEQRES   2 K  157  ASN GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO          
SEQRES   3 K  157  GLU ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA          
SEQRES   4 K  157  LEU CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL          
SEQRES   5 K  157  ASP PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP          
SEQRES   6 K  157  TRP ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL          
SEQRES   7 K  157  ILE ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE          
SEQRES   8 K  157  LEU ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL          
SEQRES   9 K  157  GLU VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE          
SEQRES  10 K  157  ARG HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL          
SEQRES  11 K  157  VAL ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL          
SEQRES  12 K  157  GLU ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG          
SEQRES  13 K  157  ALA                                                          
SEQRES   1 L  157  MET PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU          
SEQRES   2 L  157  ASN GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO          
SEQRES   3 L  157  GLU ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA          
SEQRES   4 L  157  LEU CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL          
SEQRES   5 L  157  ASP PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP          
SEQRES   6 L  157  TRP ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL          
SEQRES   7 L  157  ILE ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE          
SEQRES   8 L  157  LEU ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL          
SEQRES   9 L  157  GLU VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE          
SEQRES  10 L  157  ARG HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL          
SEQRES  11 L  157  VAL ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL          
SEQRES  12 L  157  GLU ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG          
SEQRES  13 L  157  ALA                                                          
HET    FA3  A 201      13                                                       
HET    TRS  A1151       8                                                       
HET    FA3  B 201      13                                                       
HET    FA3  C 201      13                                                       
HET    FA3  D 201      13                                                       
HET    FA3  E 201      13                                                       
HET    TRS  E1151       8                                                       
HET    FA3  F 201      13                                                       
HET    FA3  G 201      13                                                       
HET    FA3  H 201      13                                                       
HET    FA3  I 201      13                                                       
HET    TRS  I1151       8                                                       
HET    FA3  J 201      13                                                       
HET    FA3  K 201      13                                                       
HET    TRS  K1151       8                                                       
HET    FA3  L 201      13                                                       
HETNAM     FA3 2-ANHYDRO-3-FLUORO-QUINIC ACID                                   
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     TRS TRIS BUFFER                                                      
FORMUL  13  FA3    12(C7 H9 F O5)                                               
FORMUL  14  TRS    4(C4 H12 N O3 1+)                                            
FORMUL  29  HOH   *700(H2 O)                                                    
HELIX    1   1 ASN A   16  LEU A   20  5                                   5    
HELIX    2   2 GLN A   24  GLY A   29  1                                   6    
HELIX    3   3 THR A   32  ALA A   46  1                                  15    
HELIX    4   4 HIS A   58  HIS A   73  1                                  16    
HELIX    5   5 PRO A   80  THR A   86  5                                   7    
HELIX    6   6 SER A   87  CYS A   97  1                                  11    
HELIX    7   7 ASN A  109  ARG A  113  5                                   5    
HELIX    8   8 GLU A  114  HIS A  118  5                                   5    
HELIX    9   9 SER A  120  ARG A  125  5                                   6    
HELIX   10  10 VAL A  135  GLY A  150  1                                  16    
HELIX   11  11 ASN B   16  LEU B   20  5                                   5    
HELIX   12  12 GLN B   24  GLY B   29  1                                   6    
HELIX   13  13 THR B   32  ALA B   46  1                                  15    
HELIX   14  14 HIS B   58  HIS B   73  1                                  16    
HELIX   15  15 PRO B   80  THR B   86  5                                   7    
HELIX   16  16 SER B   87  ASN B   95  1                                   9    
HELIX   17  17 ASN B  109  ARG B  113  5                                   5    
HELIX   18  18 GLU B  114  HIS B  118  5                                   5    
HELIX   19  19 SER B  120  ARG B  125  5                                   6    
HELIX   20  20 VAL B  135  GLY B  150  1                                  16    
HELIX   21  21 ASN C   16  LEU C   20  5                                   5    
HELIX   22  22 GLN C   24  GLY C   29  1                                   6    
HELIX   23  23 THR C   32  ALA C   46  1                                  15    
HELIX   24  24 HIS C   58  HIS C   73  1                                  16    
HELIX   25  25 PRO C   80  HIS C   85  5                                   6    
HELIX   26  26 SER C   87  THR C   96  1                                  10    
HELIX   27  27 ASN C  109  ARG C  113  5                                   5    
HELIX   28  28 GLU C  114  HIS C  118  5                                   5    
HELIX   29  29 TYR C  121  ARG C  125  5                                   5    
HELIX   30  30 VAL C  135  GLY C  150  1                                  16    
HELIX   31  31 ASN D   16  LEU D   20  5                                   5    
HELIX   32  32 GLN D   24  GLY D   29  1                                   6    
HELIX   33  33 THR D   32  ALA D   46  1                                  15    
HELIX   34  34 HIS D   58  HIS D   73  1                                  16    
HELIX   35  35 PRO D   80  THR D   86  5                                   7    
HELIX   36  36 SER D   87  ASN D   95  1                                   9    
HELIX   37  37 ASN D  109  ARG D  113  5                                   5    
HELIX   38  38 GLU D  114  HIS D  118  5                                   5    
HELIX   39  39 SER D  120  ARG D  125  5                                   6    
HELIX   40  40 VAL D  135  GLY D  150  1                                  16    
HELIX   41  41 ASN E   16  LEU E   20  5                                   5    
HELIX   42  42 GLN E   24  GLY E   29  1                                   6    
HELIX   43  43 THR E   32  ALA E   46  1                                  15    
HELIX   44  44 HIS E   58  HIS E   73  1                                  16    
HELIX   45  45 ALA E   82  SER E   87  1                                   6    
HELIX   46  46 SER E   87  ASN E   95  1                                   9    
HELIX   47  47 ASN E  109  ARG E  113  5                                   5    
HELIX   48  48 GLU E  114  HIS E  118  5                                   5    
HELIX   49  49 SER E  120  ARG E  125  5                                   6    
HELIX   50  50 VAL E  135  GLY E  150  1                                  16    
HELIX   51  51 ASN F   16  LEU F   20  5                                   5    
HELIX   52  52 GLN F   24  GLY F   29  1                                   6    
HELIX   53  53 THR F   32  ALA F   46  1                                  15    
HELIX   54  54 HIS F   58  HIS F   73  1                                  16    
HELIX   55  55 PRO F   80  HIS F   85  5                                   6    
HELIX   56  56 SER F   87  THR F   96  1                                  10    
HELIX   57  57 ASN F  109  ARG F  113  5                                   5    
HELIX   58  58 GLU F  114  HIS F  118  5                                   5    
HELIX   59  59 TYR F  121  ARG F  125  5                                   5    
HELIX   60  60 VAL F  135  GLY F  150  1                                  16    
HELIX   61  61 ASN G   16  LEU G   20  5                                   5    
HELIX   62  62 GLN G   24  GLY G   29  1                                   6    
HELIX   63  63 THR G   32  ALA G   46  1                                  15    
HELIX   64  64 HIS G   58  HIS G   73  1                                  16    
HELIX   65  65 ALA G   82  SER G   87  1                                   6    
HELIX   66  66 SER G   87  THR G   96  1                                  10    
HELIX   67  67 ASN G  109  ARG G  113  5                                   5    
HELIX   68  68 GLU G  114  HIS G  118  5                                   5    
HELIX   69  69 TYR G  121  ARG G  125  5                                   5    
HELIX   70  70 VAL G  135  GLY G  150  1                                  16    
HELIX   71  71 ASN H   16  LEU H   20  5                                   5    
HELIX   72  72 GLN H   24  GLY H   29  1                                   6    
HELIX   73  73 THR H   32  ALA H   46  1                                  15    
HELIX   74  74 HIS H   58  HIS H   73  1                                  16    
HELIX   75  75 PRO H   80  HIS H   85  5                                   6    
HELIX   76  76 SER H   87  ASN H   95  1                                   9    
HELIX   77  77 ASN H  109  ARG H  113  5                                   5    
HELIX   78  78 GLU H  114  HIS H  118  5                                   5    
HELIX   79  79 TYR H  121  ARG H  125  5                                   5    
HELIX   80  80 VAL H  135  GLY H  150  1                                  16    
HELIX   81  81 ASN I   16  LEU I   20  5                                   5    
HELIX   82  82 GLN I   24  GLY I   29  1                                   6    
HELIX   83  83 THR I   32  ALA I   46  1                                  15    
HELIX   84  84 HIS I   58  HIS I   73  1                                  16    
HELIX   85  85 PRO I   80  HIS I   85  5                                   6    
HELIX   86  86 SER I   87  THR I   96  1                                  10    
HELIX   87  87 ASN I  109  ARG I  113  5                                   5    
HELIX   88  88 GLU I  114  HIS I  118  5                                   5    
HELIX   89  89 SER I  120  ARG I  125  5                                   6    
HELIX   90  90 VAL I  135  GLY I  150  1                                  16    
HELIX   91  91 ASN J   16  LEU J   20  5                                   5    
HELIX   92  92 GLN J   24  GLY J   29  1                                   6    
HELIX   93  93 THR J   32  ALA J   46  1                                  15    
HELIX   94  94 HIS J   58  HIS J   73  1                                  16    
HELIX   95  95 ALA J   82  SER J   87  1                                   6    
HELIX   96  96 SER J   87  ASN J   95  1                                   9    
HELIX   97  97 ASN J  109  ARG J  113  5                                   5    
HELIX   98  98 GLU J  114  HIS J  118  5                                   5    
HELIX   99  99 SER J  120  ARG J  125  5                                   6    
HELIX  100 100 VAL J  135  GLY J  150  1                                  16    
HELIX  101 101 ASN K   16  LEU K   20  5                                   5    
HELIX  102 102 GLN K   24  GLY K   29  1                                   6    
HELIX  103 103 THR K   32  ALA K   46  1                                  15    
HELIX  104 104 HIS K   58  HIS K   73  1                                  16    
HELIX  105 105 ALA K   82  SER K   87  1                                   6    
HELIX  106 106 SER K   87  ASN K   95  1                                   9    
HELIX  107 107 ASN K  109  ARG K  113  5                                   5    
HELIX  108 108 GLU K  114  HIS K  118  5                                   5    
HELIX  109 109 TYR K  121  ARG K  125  5                                   5    
HELIX  110 110 VAL K  135  GLY K  150  1                                  16    
HELIX  111 111 ASN L   16  LEU L   20  5                                   5    
HELIX  112 112 GLN L   24  GLY L   29  1                                   6    
HELIX  113 113 THR L   32  ALA L   46  1                                  15    
HELIX  114 114 HIS L   58  HIS L   73  1                                  16    
HELIX  115 115 PRO L   80  THR L   86  5                                   7    
HELIX  116 116 SER L   87  THR L   96  1                                  10    
HELIX  117 117 ASN L  109  ARG L  113  5                                   5    
HELIX  118 118 GLU L  114  HIS L  118  5                                   5    
HELIX  119 119 SER L  120  ARG L  125  5                                   6    
HELIX  120 120 VAL L  135  GLY L  150  1                                  16    
SHEET    1  AA10 VAL A  51  GLN A  55  0                                        
SHEET    2  AA10 ILE A   9  ASN A  13  1  O  ILE A   9   N  ASP A  52           
SHEET    3  AA10 GLY A  75  ASN A  79  1  O  GLY A  75   N  MET A  10           
SHEET    4  AA10 VAL A 102  HIS A 106  1  O  VAL A 103   N  ILE A  78           
SHEET    5  AA10 GLY A 128  ALA A 131  1  O  GLY A 128   N  GLU A 104           
SHEET    6  AA10 GLY D 128  ALA D 131 -1  O  VAL D 129   N  ALA A 131           
SHEET    7  AA10 VAL D 102  HIS D 106  1  O  GLU D 104   N  VAL D 130           
SHEET    8  AA10 ILE D  76  ASN D  79  1  O  ILE D  76   N  VAL D 103           
SHEET    9  AA10 ILE D   9  ASN D  13  1  O  MET D  10   N  VAL D  77           
SHEET   10  AA10 VAL D  51  GLN D  55  1  O  ASP D  52   N  ILE D  11           
SHEET    1  BA10 VAL B  51  GLN B  55  0                                        
SHEET    2  BA10 ILE B   9  ASN B  13  1  O  ILE B   9   N  ASP B  52           
SHEET    3  BA10 ILE B  76  ASN B  79  1  O  VAL B  77   N  LEU B  12           
SHEET    4  BA10 VAL B 102  HIS B 106  1  O  VAL B 103   N  ILE B  78           
SHEET    5  BA10 GLY B 128  ALA B 131  1  O  GLY B 128   N  GLU B 104           
SHEET    6  BA10 GLY G 128  ALA G 131 -1  O  VAL G 129   N  ALA B 131           
SHEET    7  BA10 VAL G 102  HIS G 106  1  O  GLU G 104   N  VAL G 130           
SHEET    8  BA10 ILE G  76  ASN G  79  1  O  ILE G  76   N  VAL G 103           
SHEET    9  BA10 ILE G   9  ASN G  13  1  O  MET G  10   N  VAL G  77           
SHEET   10  BA10 VAL G  51  GLN G  55  1  O  ASP G  52   N  ILE G  11           
SHEET    1  CA10 VAL C  51  GLN C  55  0                                        
SHEET    2  CA10 ILE C   9  ASN C  13  1  O  ILE C   9   N  ASP C  52           
SHEET    3  CA10 GLY C  75  ASN C  79  1  O  GLY C  75   N  MET C  10           
SHEET    4  CA10 VAL C 102  HIS C 106  1  O  VAL C 103   N  ILE C  78           
SHEET    5  CA10 GLY C 128  ALA C 131  1  O  GLY C 128   N  GLU C 104           
SHEET    6  CA10 GLY J 128  ALA J 131 -1  O  VAL J 129   N  ALA C 131           
SHEET    7  CA10 VAL J 102  HIS J 106  1  O  GLU J 104   N  VAL J 130           
SHEET    8  CA10 GLY J  75  ASN J  79  1  O  ILE J  76   N  VAL J 103           
SHEET    9  CA10 ILE J   9  ASN J  13  1  O  MET J  10   N  VAL J  77           
SHEET   10  CA10 VAL J  51  GLN J  55  1  O  ASP J  52   N  ILE J  11           
SHEET    1  EA10 VAL E  51  GLN E  55  0                                        
SHEET    2  EA10 ILE E   9  ASN E  13  1  O  ILE E   9   N  ASP E  52           
SHEET    3  EA10 ILE E  76  ASN E  79  1  O  VAL E  77   N  LEU E  12           
SHEET    4  EA10 VAL E 102  HIS E 106  1  O  VAL E 103   N  ILE E  78           
SHEET    5  EA10 GLY E 128  ALA E 131  1  O  GLY E 128   N  GLU E 104           
SHEET    6  EA10 GLY L 128  ALA L 131 -1  O  VAL L 129   N  ALA E 131           
SHEET    7  EA10 VAL L 102  HIS L 106  1  O  GLU L 104   N  VAL L 130           
SHEET    8  EA10 GLY L  75  ASN L  79  1  O  ILE L  76   N  VAL L 103           
SHEET    9  EA10 ILE L   9  ASN L  13  1  O  MET L  10   N  VAL L  77           
SHEET   10  EA10 VAL L  51  GLN L  55  1  O  ASP L  52   N  ILE L  11           
SHEET    1  FA10 VAL F  51  GLN F  55  0                                        
SHEET    2  FA10 ILE F   9  ASN F  13  1  O  ILE F   9   N  ASP F  52           
SHEET    3  FA10 GLY F  75  ASN F  79  1  O  GLY F  75   N  MET F  10           
SHEET    4  FA10 VAL F 102  HIS F 106  1  O  VAL F 103   N  ILE F  78           
SHEET    5  FA10 GLY F 128  ALA F 131  1  O  GLY F 128   N  GLU F 104           
SHEET    6  FA10 GLY H 128  ALA H 131 -1  O  VAL H 129   N  ALA F 131           
SHEET    7  FA10 VAL H 102  HIS H 106  1  O  GLU H 104   N  VAL H 130           
SHEET    8  FA10 GLY H  75  ASN H  79  1  O  ILE H  76   N  VAL H 103           
SHEET    9  FA10 ILE H   9  ASN H  13  1  O  MET H  10   N  VAL H  77           
SHEET   10  FA10 VAL H  51  GLN H  55  1  O  ASP H  52   N  ILE H  11           
SHEET    1  IA10 VAL I  51  GLN I  55  0                                        
SHEET    2  IA10 ILE I   9  ASN I  13  1  O  ILE I   9   N  ASP I  52           
SHEET    3  IA10 ILE I  76  ASN I  79  1  O  VAL I  77   N  LEU I  12           
SHEET    4  IA10 VAL I 102  HIS I 106  1  O  VAL I 103   N  ILE I  78           
SHEET    5  IA10 GLY I 128  ALA I 131  1  O  GLY I 128   N  GLU I 104           
SHEET    6  IA10 GLY K 128  ALA K 131 -1  O  VAL K 129   N  ALA I 131           
SHEET    7  IA10 VAL K 102  HIS K 106  1  O  GLU K 104   N  VAL K 130           
SHEET    8  IA10 GLY K  75  ASN K  79  1  O  ILE K  76   N  VAL K 103           
SHEET    9  IA10 ILE K   9  ASN K  13  1  O  MET K  10   N  VAL K  77           
SHEET   10  IA10 VAL K  51  GLN K  55  1  O  ASP K  52   N  ILE K  11           
SITE     1 AC1 10 TYR A  28  ASN A  79  ALA A  81  ALA A  82                    
SITE     2 AC1 10 HIS A  85  HIS A 106  ILE A 107  SER A 108                    
SITE     3 AC1 10 ARG A 117  ASP B  92                                          
SITE     1 AC2  8 GLU A  59  THR A  86  GLU B  59  THR B  86                    
SITE     2 AC2  8 SER B  87  GLU C  59  THR C  86  SER C  87                    
SITE     1 AC3 10 TYR B  28  ASN B  79  ALA B  81  ALA B  82                    
SITE     2 AC3 10 HIS B  85  HIS B 106  ILE B 107  SER B 108                    
SITE     3 AC3 10 ARG B 117  ASP C  92                                          
SITE     1 AC4 11 ASP A  92  HOH A2028  TYR C  28  ASN C  79                    
SITE     2 AC4 11 ALA C  81  ALA C  82  HIS C  85  HIS C 106                    
SITE     3 AC4 11 ILE C 107  SER C 108  ARG C 117                               
SITE     1 AC5 11 TYR D  28  ASN D  79  ALA D  81  ALA D  82                    
SITE     2 AC5 11 HIS D  85  HIS D 106  ILE D 107  SER D 108                    
SITE     3 AC5 11 ARG D 117  HOH D2002  ASP E  92                               
SITE     1 AC6 11 TYR E  28  ASN E  79  ALA E  81  ALA E  82                    
SITE     2 AC6 11 HIS E  85  HIS E 106  ILE E 107  SER E 108                    
SITE     3 AC6 11 ARG E 117  ASP F  92  HOH F2026                               
SITE     1 AC7  9 GLU D  59  THR D  86  SER D  87  GLU E  59                    
SITE     2 AC7  9 THR E  86  SER E  87  GLU F  59  THR F  86                    
SITE     3 AC7  9 SER F  87                                                     
SITE     1 AC8 10 ASP D  92  TYR F  28  ASN F  79  ALA F  81                    
SITE     2 AC8 10 ALA F  82  HIS F  85  HIS F 106  ILE F 107                    
SITE     3 AC8 10 SER F 108  ARG F 117                                          
SITE     1 AC9 10 TYR G  28  ASN G  79  ALA G  81  ALA G  82                    
SITE     2 AC9 10 HIS G  85  HIS G 106  ILE G 107  SER G 108                    
SITE     3 AC9 10 ARG G 117  ASP H  92                                          
SITE     1 BC1 10 TYR H  28  ASN H  79  ALA H  81  ALA H  82                    
SITE     2 BC1 10 HIS H  85  HIS H 106  ILE H 107  SER H 108                    
SITE     3 BC1 10 ARG H 117  ASP I  92                                          
SITE     1 BC2 10 ASP G  92  TYR I  28  ASN I  79  ALA I  81                    
SITE     2 BC2 10 ALA I  82  HIS I  85  HIS I 106  ILE I 107                    
SITE     3 BC2 10 SER I 108  ARG I 117                                          
SITE     1 BC3  9 GLU G  59  THR G  86  SER G  87  GLU H  59                    
SITE     2 BC3  9 THR H  86  SER H  87  GLU I  59  THR I  86                    
SITE     3 BC3  9 SER I  87                                                     
SITE     1 BC4 10 TYR J  28  ASN J  79  ALA J  81  ALA J  82                    
SITE     2 BC4 10 HIS J  85  HIS J 106  ILE J 107  SER J 108                    
SITE     3 BC4 10 ARG J 117  ASP K  92                                          
SITE     1 BC5 10 TYR K  28  ASN K  79  ALA K  81  ALA K  82                    
SITE     2 BC5 10 HIS K  85  HIS K 106  ILE K 107  SER K 108                    
SITE     3 BC5 10 ARG K 117  ASP L  92                                          
SITE     1 BC6  8 GLU J  59  THR J  86  GLU K  59  THR K  86                    
SITE     2 BC6  8 SER K  87  GLU L  59  THR L  86  SER L  87                    
SITE     1 BC7 10 ASP J  92  TYR L  28  ASN L  79  ALA L  81                    
SITE     2 BC7 10 ALA L  82  HIS L  85  HIS L 106  ILE L 107                    
SITE     3 BC7 10 SER L 108  ARG L 117                                          
CRYST1  116.475  138.941  141.925  90.00  90.00  90.00 P 21 21 21   48          
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      0.008585  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007197  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007046        0.00000                         
MTRIX1   1  0.000450  0.404460 -0.914560       51.89528    1                    
MTRIX2   1 -0.914870 -0.369090 -0.163680       82.15550    1                    
MTRIX3   1 -0.403760  0.836770  0.369860        7.52426    1                    
MTRIX1   2 -0.000490 -0.912240 -0.409670       78.43419    1                    
MTRIX2   2  0.407080 -0.374370  0.833150        3.41615    1                    
MTRIX3   2 -0.913390 -0.166360  0.371530       58.11004    1                    
MTRIX1   3 -0.999980 -0.001580 -0.005400       62.43271    1                    
MTRIX2   3 -0.005060  0.671590  0.740910      -16.75690    1                    
MTRIX3   3  0.002450  0.740920 -0.671590       38.04821    1                    
MTRIX1   4  0.003310 -0.402490  0.915420        9.98314    1                    
MTRIX2   4 -0.913710  0.370770  0.166320       43.82185    1                    
MTRIX3   4 -0.406350 -0.836980 -0.366530       93.83305    1                    
MTRIX1   5 -0.003160  0.914090  0.405500      -16.11196    1                    
MTRIX2   5 -0.402760 -0.372320  0.836160       28.32615    1                    
MTRIX3   5  0.915300 -0.160680  0.369340        1.31071    1                    
MTRIX1   6 -0.003400 -0.405920  0.913900       10.32446    1                    
MTRIX2   6  0.914390 -0.371230 -0.161480       25.43354    1                    
MTRIX3   6  0.404810  0.835110  0.372440      -17.56244    1                    
MTRIX1   7  0.003290  0.912820  0.408340      -16.36827    1                    
MTRIX2   7  0.403320  0.372450 -0.835830       41.22469    1                    
MTRIX3   7 -0.915050  0.167440 -0.366940       74.78658    1                    
MTRIX1   8 -0.999990  0.003850 -0.001190       61.97967    1                    
MTRIX2   8 -0.001700 -0.670580 -0.741840       86.44312    1                    
MTRIX3   8 -0.003660 -0.741830  0.670580       38.55089    1                    
MTRIX1   9 -0.003340 -0.914430 -0.404730       78.41739    1                    
MTRIX2   9 -0.406170  0.371090 -0.835060       66.30820    1                    
MTRIX3   9  0.913790  0.161600 -0.372650       18.52069    1                    
MTRIX1  10  0.999990  0.001640  0.004880       -0.21171    1                    
MTRIX2  10  0.001650 -1.000000 -0.001500       69.54708    1                    
MTRIX3  10  0.004870  0.001510 -0.999990       76.21187    1                    
MTRIX1  11 -0.002880  0.406910 -0.913460       51.92285    1                    
MTRIX2  11  0.915280  0.369020  0.161500      -12.54626    1                    
MTRIX3  11  0.402800 -0.835610 -0.373500       69.01919    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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