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Database: PDB
Entry: 5LZJ
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Original site: 5LZJ 
HEADER    TOXIN                                   29-SEP-16   5LZJ              
TITLE     CHOLERA TOXIN EL TOR B-PENTAMER IN COMPLEX WITH INHIBITOR LAURA237    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA ENTEROTOXIN SUBUNIT B;                             
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 SYNONYM: CHOLERA ENTEROTOXIN B CHAIN,CHOLERA ENTEROTOXIN GAMMA CHAIN,
COMPND   5 CHOLERAGENOID;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE SEROTYPE O1 (STRAIN ATCC 39315  
SOURCE   3 / EL TOR INABA N16961);                                              
SOURCE   4 ORGANISM_TAXID: 243277;                                              
SOURCE   5 GENE: CTXB, TOXB, VC_1456;                                           
SOURCE   6 EXPRESSION_SYSTEM: VIBRIO SP.;                                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 678                                         
KEYWDS    CHOLERA TOXIN B-PENTAMER, INHIBITOR, TOXIN                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.HEGGELUND,U.KRENGEL                                               
REVDAT   2   07-JUN-17 5LZJ    1       JRNL                                     
REVDAT   1   31-MAY-17 5LZJ    0                                                
JRNL        AUTH   J.E.HEGGELUND,A.MACKENZIE,T.MARTINSEN,J.BENJAMIN HEIM,       
JRNL        AUTH 2 P.CHESHEV,A.BERNARDI,U.KRENGEL                               
JRNL        TITL   TOWARDS NEW CHOLERA PROPHYLACTICS AND TREATMENT: CRYSTAL     
JRNL        TITL 2 STRUCTURES OF BACTERIAL ENTEROTOXINS IN COMPLEX WITH GM1     
JRNL        TITL 3 MIMICS.                                                      
JRNL        REF    SCI REP                       V.   7  2326 2017              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   28539625                                                     
JRNL        DOI    10.1038/S41598-017-02179-0                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0155                                      
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) : 1.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 73.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 136978                         
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) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7295                            
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) : 1.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.23                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6801                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 63.23                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 360                          
REMARK   3   BIN FREE R VALUE                    : 0.3970                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4085                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 99                                      
REMARK   3   SOLVENT ATOMS            : 549                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.84000                                             
REMARK   3    B22 (A**2) : -0.64000                                             
REMARK   3    B33 (A**2) : 0.96000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.02000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.050         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.054         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.058         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.441         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4444 ; 0.021 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  4378 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6027 ; 2.154 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10142 ; 1.144 ; 3.004       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   566 ; 7.094 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   194 ;41.169 ;25.567       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   849 ;14.410 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;26.349 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   693 ; 0.129 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4915 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   964 ; 0.002 ; 0.020       
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):  2111 ; 1.764 ; 1.489       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2110 ; 1.753 ; 1.487       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2644 ; 2.681 ; 2.225       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2645 ; 2.681 ; 2.226       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2333 ; 2.395 ; 1.831       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2329 ; 2.392 ; 1.831       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3350 ; 3.666 ; 2.635       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5086 ; 5.342 ;19.036       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5086 ; 5.341 ;19.034       
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5LZJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001381.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JUL-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97239                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 144269                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.5500                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 3CHB                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6, 30% PEG 400, 3% PGA-LM,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       51.12250            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.23800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       51.12250            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.23800            
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: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13810 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 21340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   396     O    HOH D   397              1.76            
REMARK 500   O    HOH D   345     O    HOH D   368              1.97            
REMARK 500   OAD  7BT D   202     O    HOH D   301              2.11            
REMARK 500   O    HOH E   310     O    HOH E   379              2.11            
REMARK 500   O    HOH B   320     O    HOH B   374              2.12            
REMARK 500   OE1  GLU E    79     O    HOH E   301              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   344     O    HOH A   360     4455     2.11            
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    GLU E  29   CD    GLU E  29   OE2    -0.069                       
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  37   CG  -  SD  -  CE  ANGL. DEV. =  24.3 DEGREES          
REMARK 500    LYS A  81   CD  -  CE  -  NZ  ANGL. DEV. =  14.6 DEGREES          
REMARK 500    MET A 101   CG  -  SD  -  CE  ANGL. DEV. = -14.3 DEGREES          
REMARK 500    MET B 101   CG  -  SD  -  CE  ANGL. DEV. = -18.4 DEGREES          
REMARK 500    MET C 101   CG  -  SD  -  CE  ANGL. DEV. = -21.9 DEGREES          
REMARK 500    MET D 101   CG  -  SD  -  CE  ANGL. DEV. = -17.2 DEGREES          
REMARK 500    ARG E  35   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 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    GLU B  36       60.02     34.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH E 395        DISTANCE =  6.36 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7BT C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7BT D 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG E 201                 
DBREF  5LZJ A    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5LZJ B    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5LZJ C    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5LZJ D    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5LZJ E    1   103  UNP    P01556   CHTB_VIBCH      22    124             
SEQRES   1 A  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 A  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 A  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 A  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 A  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 A  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 A  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 A  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 B  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 B  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 B  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 B  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 B  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 B  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 B  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 B  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 C  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 C  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 C  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 C  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 C  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 C  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 C  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 C  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 D  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 D  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 D  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 D  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 D  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 D  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 D  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 D  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 E  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 E  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 E  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 E  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 E  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 E  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 E  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 E  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
HET    SO4  A 201       5                                                       
HET    PEG  B 201       7                                                       
HET    PGE  C 201      10                                                       
HET    7BT  C 202      30                                                       
HET    PGE  D 201      10                                                       
HET    7BT  D 202      30                                                       
HET    PEG  E 201       7                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     7BT (~{Z})-~{N}-[2-[(2~{R},3~{R},4~{R},5~{R},6~{R})-6-               
HETNAM   2 7BT  (HYDROXYMETHYL)-3,4,5-TRIS(OXIDANYL)OXAN-2-YL]ETHYL]-           
HETNAM   3 7BT  3-(3,4,5-TRIMETHOXYPHENYL)PROP-2-ENAMIDE                        
HETSYN     7BT LAURA237                                                         
FORMUL   6  SO4    O4 S 2-                                                      
FORMUL   7  PEG    2(C4 H10 O3)                                                 
FORMUL   8  PGE    2(C6 H14 O4)                                                 
FORMUL   9  7BT    2(C20 H29 N O9)                                              
FORMUL  13  HOH   *549(H2 O)                                                    
HELIX    1   1 ILE A    5  GLU A   11  1                                   7    
HELIX    2   2 ASP A   59  THR A   78  1                                  20    
HELIX    3   3 ILE B    5  GLU B   11  1                                   7    
HELIX    4   4 ASP B   59  THR B   78  5                                  20    
HELIX    5   5 ILE C    5  GLU C   11  1                                   7    
HELIX    6   6 ASP C   59  THR C   78  5                                  20    
HELIX    7   7 ILE D    5  GLU D   11  1                                   7    
HELIX    8   8 ASP D   59  THR D   78  1                                  20    
HELIX    9   9 ILE E    5  GLU E   11  1                                   7    
HELIX   10  10 ASP E   59  THR E   78  1                                  20    
SHEET    1   A 3 THR A  15  THR A  19  0                                        
SHEET    2   A 3 VAL A  82  TRP A  88 -1  N  VAL A  87   O  GLN A  16           
SHEET    3   A 3 ALA A  98  MET A 101 -1  N  SER A 100   O  GLU A  83           
SHEET    1   B 3 SER A  26  SER A  30  0                                        
SHEET    2   B 3 MET A  37  THR A  41 -1  N  THR A  41   O  SER A  26           
SHEET    3   B 3 ILE A  47  VAL A  50 -1  N  VAL A  50   O  ALA A  38           
SHEET    1   C 3 THR B  15  THR B  19  0                                        
SHEET    2   C 3 VAL B  82  TRP B  88 -1  N  VAL B  87   O  GLN B  16           
SHEET    3   C 3 ALA B  98  MET B 101 -1  N  SER B 100   O  GLU B  83           
SHEET    1   D 3 SER B  26  GLU B  29  0                                        
SHEET    2   D 3 ALA B  38  THR B  41 -1  N  THR B  41   O  SER B  26           
SHEET    3   D 3 ILE B  47  VAL B  50 -1  N  VAL B  50   O  ALA B  38           
SHEET    1   E 3 THR C  15  THR C  19  0                                        
SHEET    2   E 3 VAL C  82  TRP C  88 -1  N  VAL C  87   O  GLN C  16           
SHEET    3   E 3 ALA C  98  MET C 101 -1  N  SER C 100   O  GLU C  83           
SHEET    1   F 3 SER C  26  SER C  30  0                                        
SHEET    2   F 3 MET C  37  THR C  41 -1  N  THR C  41   O  SER C  26           
SHEET    3   F 3 ILE C  47  VAL C  50 -1  N  VAL C  50   O  ALA C  38           
SHEET    1   G 3 THR D  15  THR D  19  0                                        
SHEET    2   G 3 VAL D  82  TRP D  88 -1  N  VAL D  87   O  GLN D  16           
SHEET    3   G 3 ALA D  98  MET D 101 -1  N  SER D 100   O  GLU D  83           
SHEET    1   H 3 SER D  26  SER D  30  0                                        
SHEET    2   H 3 MET D  37  THR D  41 -1  N  THR D  41   O  SER D  26           
SHEET    3   H 3 ILE D  47  VAL D  50 -1  N  VAL D  50   O  ALA D  38           
SHEET    1   I 3 THR E  15  THR E  19  0                                        
SHEET    2   I 3 VAL E  82  TRP E  88 -1  N  VAL E  87   O  GLN E  16           
SHEET    3   I 3 ALA E  98  MET E 101 -1  N  SER E 100   O  GLU E  83           
SHEET    1   J 3 SER E  26  SER E  30  0                                        
SHEET    2   J 3 MET E  37  THR E  41 -1  N  THR E  41   O  SER E  26           
SHEET    3   J 3 ILE E  47  VAL E  50 -1  N  VAL E  50   O  ALA E  38           
SSBOND   1 CYS A    9    CYS A   86                          1555   1555  2.10  
SSBOND   2 CYS B    9    CYS B   86                          1555   1555  2.11  
SSBOND   3 CYS C    9    CYS C   86                          1555   1555  2.10  
SSBOND   4 CYS D    9    CYS D   86                          1555   1555  2.07  
SSBOND   5 CYS E    9    CYS E   86                          1555   1555  2.13  
CISPEP   1 THR A   92    PRO A   93          0       -17.15                     
CISPEP   2 THR B   92    PRO B   93          0       -14.65                     
CISPEP   3 THR C   92    PRO C   93          0        -4.32                     
CISPEP   4 THR D   92    PRO D   93          0       -10.03                     
CISPEP   5 THR D   92    PRO D   93          0        -7.53                     
CISPEP   6 THR E   92    PRO E   93          0       -14.34                     
SITE     1 AC1  9 TYR A  12  HIS A  13  TRP A  88  HOH A 301                    
SITE     2 AC1  9 HOH A 309  TYR E  12  HIS E  13  ASN E  14                    
SITE     3 AC1  9 TRP E  88                                                     
SITE     1 AC2  3 GLU B  11  TYR B  12  ARG C  35                               
SITE     1 AC3  9 THR B  78  GLU B  79  HOH B 303  HOH B 374                    
SITE     2 AC3  9 TYR C  76  LEU C  77  GLU C  79  HOH C 316                    
SITE     3 AC3  9 HOH C 341                                                     
SITE     1 AC4 19 HIS C  13  ASN C  14  GLU C  51  GLN C  56                    
SITE     2 AC4 19 HIS C  57  GLN C  61  TRP C  88  ASN C  90                    
SITE     3 AC4 19 LYS C  91  HOH C 311  HOH C 347  HOH C 349                    
SITE     4 AC4 19 HOH C 396  HOH D 378  TYR E  18  THR E  19                    
SITE     5 AC4 19 LEU E  20  ASN E  44  ALA E  46                               
SITE     1 AC5 10 THR C  78  GLU C  79  ASN C 103  LYS D  23                    
SITE     2 AC5 10 TYR D  76  LEU D  77  GLU D  79  HOH D 322                    
SITE     3 AC5 10 HOH D 337  HOH D 369                                          
SITE     1 AC6 18 ILE A  17  TYR A  18  THR A  19  ASN A  44                    
SITE     2 AC6 18 HIS D  13  ASN D  14  GLU D  51  GLN D  56                    
SITE     3 AC6 18 GLN D  61  TRP D  88  ASN D  90  LYS D  91                    
SITE     4 AC6 18 HOH D 301  HOH D 305  HOH D 318  HOH D 350                    
SITE     5 AC6 18 HOH D 382  HOH E 355                                          
SITE     1 AC7  4 GLU D  11  TYR D  12  ARG E  35  HOH E 360                    
CRYST1  102.245   66.476   82.401  90.00 116.96  90.00 C 1 2 1      20          
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      0.009780  0.000000  0.004974        0.00000                         
SCALE2      0.000000  0.015043  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013615        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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