GenomeNet

Database: PDB
Entry: 5FTV
LinkDB: 5FTV
Original site: 5FTV 
HEADER    TRANSFERASE                             18-JAN-16   5FTV              
TITLE     PSEUDOMONAS AERUGINOSA RMLA IN COMPLEX WITH ALLOSTERIC INHIBITOR      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE;                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 2.7.7.24;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    THYMIDYLYL, TRANSFERASE, ALLOSTERIC, INHIBITOR, PSEUDOMONAS           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.S.ALPHEY,F.TRAN,N.J.WESTWOOD,J.H.NAISMITH                           
REVDAT   2   05-JUL-17 5FTV    1       REMARK                                   
REVDAT   1   22-FEB-17 5FTV    0                                                
JRNL        AUTH   F.TRAN,M.S.ALPHEY,N.J.WESTWOOD,J.H.NAISMITH                  
JRNL        TITL   ALLOSTERIC COMPETITIVE INHIBITORS OF THE GLUCOSE-1-PHOSPHATE 
JRNL        TITL 2 THYMIDYLYLTRANSFERASE (RMLA) FROM PSEUDOMONAS AERUGINOSA.    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.21 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.21                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 134.69                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 64529                          
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) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3245                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.21                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.27                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4165                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 216                          
REMARK   3   BIN FREE R VALUE                    : 0.5670                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9230                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 164                                     
REMARK   3   SOLVENT ATOMS            : 473                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.43                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.56100                                              
REMARK   3    B22 (A**2) : -0.21200                                             
REMARK   3    B33 (A**2) : -0.30800                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.48100                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.346         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.249         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.195         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.120         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.893                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.859                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9619 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  9138 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13067 ; 1.572 ; 1.994       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 21010 ; 0.993 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1175 ; 6.748 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   439 ;35.025 ;24.237       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1573 ;15.421 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    56 ;18.006 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1415 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10913 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2209 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4504 ; 0.205 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):   161 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  9274 ; 0.172 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   486 ; 0.139 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.006 ; 0.200       
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):  4706 ; 1.691 ; 2.499       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4705 ; 1.691 ; 2.499       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5873 ; 2.806 ; 3.742       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4913 ; 1.880 ; 2.680       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  7192 ; 3.132 ; 3.924       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL PLUS MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.40                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 5FTV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1290066054.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-MAR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
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          : RIGAKU MICROMAX-007 HF             
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                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MSC SATURN 944                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64889                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
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: PDB ENTRY 4ASJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 4% PEG 6000, 0.1 M MES PH 6, 0.05 M      
REMARK 280  MGCL2, 0.1 M NA BR, 1% BETA-MERCAPTOETHANOL                         
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       32.13000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       77.17500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       32.13000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       77.17500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15700 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       64.26000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15190 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       58.61474            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      134.69175            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     MET A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     MET B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     MET C    -1                                                      
REMARK 465     ALA C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     HIS D    -9                                                      
REMARK 465     HIS D    -8                                                      
REMARK 465     HIS D    -7                                                      
REMARK 465     HIS D    -6                                                      
REMARK 465     HIS D    -5                                                      
REMARK 465     HIS D    -4                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     MET D    -1                                                      
REMARK 465     ALA D     0                                                      
REMARK 465     MET D     1                                                      
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    ARG B 128   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  12       34.01    -87.93                                   
REMARK 500    TYR A  31     -102.30     61.57                                   
REMARK 500    TYR B  31     -104.53     51.31                                   
REMARK 500    ALA C   9       63.50   -111.28                                   
REMARK 500    SER C  12       30.86    -90.00                                   
REMARK 500    TYR C  31      -95.12     56.48                                   
REMARK 500    ASP C  86       35.66    -97.27                                   
REMARK 500    ARG C 128       96.37    -65.83                                   
REMARK 500    ASP C 141       65.64   -118.49                                   
REMARK 500    ALA D   9       65.47   -102.55                                   
REMARK 500    TYR D  31      -98.74     58.05                                   
REMARK 500    PRO D  85       77.63    -67.83                                   
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 KDT A 1294                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 1295                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KDT B 1294                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 1295                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KDT C 1294                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES C 1295                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KDT D 1294                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES D 1295                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1296                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1296                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1296                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 1296                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 N-TERMINAL HIS-TAG PRESENT                                           
DBREF  5FTV A    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  5FTV B    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  5FTV C    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  5FTV D    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
SEQADV 5FTV HIS A   -9  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS A   -8  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS A   -7  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS A   -6  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS A   -5  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS A   -4  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV GLY A   -3  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV SER A   -2  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV MET A   -1  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV ALA A    0  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS B   -9  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS B   -8  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS B   -7  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS B   -6  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS B   -5  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS B   -4  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV GLY B   -3  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV SER B   -2  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV MET B   -1  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV ALA B    0  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS C   -9  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS C   -8  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS C   -7  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS C   -6  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS C   -5  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS C   -4  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV GLY C   -3  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV SER C   -2  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV MET C   -1  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV ALA C    0  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS D   -9  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS D   -8  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS D   -7  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS D   -6  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS D   -5  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV HIS D   -4  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV GLY D   -3  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV SER D   -2  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV MET D   -1  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTV ALA D    0  UNP  Q9HU22              EXPRESSION TAG                 
SEQRES   1 A  303  HIS HIS HIS HIS HIS HIS GLY SER MET ALA MET LYS ARG          
SEQRES   2 A  303  LYS GLY ILE ILE LEU ALA GLY GLY SER GLY THR ARG LEU          
SEQRES   3 A  303  HIS PRO ALA THR LEU ALA ILE SER LYS GLN LEU LEU PRO          
SEQRES   4 A  303  VAL TYR ASP LYS PRO MET ILE TYR TYR PRO LEU SER THR          
SEQRES   5 A  303  LEU MET LEU ALA GLY ILE ARG GLU ILE LEU ILE ILE SER          
SEQRES   6 A  303  THR PRO GLN ASP THR PRO ARG PHE GLN GLN LEU LEU GLY          
SEQRES   7 A  303  ASP GLY SER ASN TRP GLY LEU ASP LEU GLN TYR ALA VAL          
SEQRES   8 A  303  GLN PRO SER PRO ASP GLY LEU ALA GLN ALA PHE LEU ILE          
SEQRES   9 A  303  GLY GLU SER PHE ILE GLY ASN ASP LEU SER ALA LEU VAL          
SEQRES  10 A  303  LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP PHE HIS GLU          
SEQRES  11 A  303  LEU LEU GLY SER ALA SER GLN ARG GLN THR GLY ALA SER          
SEQRES  12 A  303  VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU ARG TYR GLY          
SEQRES  13 A  303  VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA ILE SER LEU          
SEQRES  14 A  303  GLU GLU LYS PRO LEU GLU PRO LYS SER ASN TYR ALA VAL          
SEQRES  15 A  303  THR GLY LEU TYR PHE TYR ASP GLN GLN VAL VAL ASP ILE          
SEQRES  16 A  303  ALA ARG ASP LEU LYS PRO SER PRO ARG GLY GLU LEU GLU          
SEQRES  17 A  303  ILE THR ASP VAL ASN ARG ALA TYR LEU GLU ARG GLY GLN          
SEQRES  18 A  303  LEU SER VAL GLU ILE MET GLY ARG GLY TYR ALA TRP LEU          
SEQRES  19 A  303  ASP THR GLY THR HIS ASP SER LEU LEU GLU ALA GLY GLN          
SEQRES  20 A  303  PHE ILE ALA THR LEU GLU ASN ARG GLN GLY LEU LYS VAL          
SEQRES  21 A  303  ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN LYS TRP ILE          
SEQRES  22 A  303  ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA PRO LEU ALA          
SEQRES  23 A  303  LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG LEU LEU THR          
SEQRES  24 A  303  GLU THR VAL TYR                                              
SEQRES   1 B  303  HIS HIS HIS HIS HIS HIS GLY SER MET ALA MET LYS ARG          
SEQRES   2 B  303  LYS GLY ILE ILE LEU ALA GLY GLY SER GLY THR ARG LEU          
SEQRES   3 B  303  HIS PRO ALA THR LEU ALA ILE SER LYS GLN LEU LEU PRO          
SEQRES   4 B  303  VAL TYR ASP LYS PRO MET ILE TYR TYR PRO LEU SER THR          
SEQRES   5 B  303  LEU MET LEU ALA GLY ILE ARG GLU ILE LEU ILE ILE SER          
SEQRES   6 B  303  THR PRO GLN ASP THR PRO ARG PHE GLN GLN LEU LEU GLY          
SEQRES   7 B  303  ASP GLY SER ASN TRP GLY LEU ASP LEU GLN TYR ALA VAL          
SEQRES   8 B  303  GLN PRO SER PRO ASP GLY LEU ALA GLN ALA PHE LEU ILE          
SEQRES   9 B  303  GLY GLU SER PHE ILE GLY ASN ASP LEU SER ALA LEU VAL          
SEQRES  10 B  303  LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP PHE HIS GLU          
SEQRES  11 B  303  LEU LEU GLY SER ALA SER GLN ARG GLN THR GLY ALA SER          
SEQRES  12 B  303  VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU ARG TYR GLY          
SEQRES  13 B  303  VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA ILE SER LEU          
SEQRES  14 B  303  GLU GLU LYS PRO LEU GLU PRO LYS SER ASN TYR ALA VAL          
SEQRES  15 B  303  THR GLY LEU TYR PHE TYR ASP GLN GLN VAL VAL ASP ILE          
SEQRES  16 B  303  ALA ARG ASP LEU LYS PRO SER PRO ARG GLY GLU LEU GLU          
SEQRES  17 B  303  ILE THR ASP VAL ASN ARG ALA TYR LEU GLU ARG GLY GLN          
SEQRES  18 B  303  LEU SER VAL GLU ILE MET GLY ARG GLY TYR ALA TRP LEU          
SEQRES  19 B  303  ASP THR GLY THR HIS ASP SER LEU LEU GLU ALA GLY GLN          
SEQRES  20 B  303  PHE ILE ALA THR LEU GLU ASN ARG GLN GLY LEU LYS VAL          
SEQRES  21 B  303  ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN LYS TRP ILE          
SEQRES  22 B  303  ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA PRO LEU ALA          
SEQRES  23 B  303  LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG LEU LEU THR          
SEQRES  24 B  303  GLU THR VAL TYR                                              
SEQRES   1 C  303  HIS HIS HIS HIS HIS HIS GLY SER MET ALA MET LYS ARG          
SEQRES   2 C  303  LYS GLY ILE ILE LEU ALA GLY GLY SER GLY THR ARG LEU          
SEQRES   3 C  303  HIS PRO ALA THR LEU ALA ILE SER LYS GLN LEU LEU PRO          
SEQRES   4 C  303  VAL TYR ASP LYS PRO MET ILE TYR TYR PRO LEU SER THR          
SEQRES   5 C  303  LEU MET LEU ALA GLY ILE ARG GLU ILE LEU ILE ILE SER          
SEQRES   6 C  303  THR PRO GLN ASP THR PRO ARG PHE GLN GLN LEU LEU GLY          
SEQRES   7 C  303  ASP GLY SER ASN TRP GLY LEU ASP LEU GLN TYR ALA VAL          
SEQRES   8 C  303  GLN PRO SER PRO ASP GLY LEU ALA GLN ALA PHE LEU ILE          
SEQRES   9 C  303  GLY GLU SER PHE ILE GLY ASN ASP LEU SER ALA LEU VAL          
SEQRES  10 C  303  LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP PHE HIS GLU          
SEQRES  11 C  303  LEU LEU GLY SER ALA SER GLN ARG GLN THR GLY ALA SER          
SEQRES  12 C  303  VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU ARG TYR GLY          
SEQRES  13 C  303  VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA ILE SER LEU          
SEQRES  14 C  303  GLU GLU LYS PRO LEU GLU PRO LYS SER ASN TYR ALA VAL          
SEQRES  15 C  303  THR GLY LEU TYR PHE TYR ASP GLN GLN VAL VAL ASP ILE          
SEQRES  16 C  303  ALA ARG ASP LEU LYS PRO SER PRO ARG GLY GLU LEU GLU          
SEQRES  17 C  303  ILE THR ASP VAL ASN ARG ALA TYR LEU GLU ARG GLY GLN          
SEQRES  18 C  303  LEU SER VAL GLU ILE MET GLY ARG GLY TYR ALA TRP LEU          
SEQRES  19 C  303  ASP THR GLY THR HIS ASP SER LEU LEU GLU ALA GLY GLN          
SEQRES  20 C  303  PHE ILE ALA THR LEU GLU ASN ARG GLN GLY LEU LYS VAL          
SEQRES  21 C  303  ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN LYS TRP ILE          
SEQRES  22 C  303  ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA PRO LEU ALA          
SEQRES  23 C  303  LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG LEU LEU THR          
SEQRES  24 C  303  GLU THR VAL TYR                                              
SEQRES   1 D  303  HIS HIS HIS HIS HIS HIS GLY SER MET ALA MET LYS ARG          
SEQRES   2 D  303  LYS GLY ILE ILE LEU ALA GLY GLY SER GLY THR ARG LEU          
SEQRES   3 D  303  HIS PRO ALA THR LEU ALA ILE SER LYS GLN LEU LEU PRO          
SEQRES   4 D  303  VAL TYR ASP LYS PRO MET ILE TYR TYR PRO LEU SER THR          
SEQRES   5 D  303  LEU MET LEU ALA GLY ILE ARG GLU ILE LEU ILE ILE SER          
SEQRES   6 D  303  THR PRO GLN ASP THR PRO ARG PHE GLN GLN LEU LEU GLY          
SEQRES   7 D  303  ASP GLY SER ASN TRP GLY LEU ASP LEU GLN TYR ALA VAL          
SEQRES   8 D  303  GLN PRO SER PRO ASP GLY LEU ALA GLN ALA PHE LEU ILE          
SEQRES   9 D  303  GLY GLU SER PHE ILE GLY ASN ASP LEU SER ALA LEU VAL          
SEQRES  10 D  303  LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP PHE HIS GLU          
SEQRES  11 D  303  LEU LEU GLY SER ALA SER GLN ARG GLN THR GLY ALA SER          
SEQRES  12 D  303  VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU ARG TYR GLY          
SEQRES  13 D  303  VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA ILE SER LEU          
SEQRES  14 D  303  GLU GLU LYS PRO LEU GLU PRO LYS SER ASN TYR ALA VAL          
SEQRES  15 D  303  THR GLY LEU TYR PHE TYR ASP GLN GLN VAL VAL ASP ILE          
SEQRES  16 D  303  ALA ARG ASP LEU LYS PRO SER PRO ARG GLY GLU LEU GLU          
SEQRES  17 D  303  ILE THR ASP VAL ASN ARG ALA TYR LEU GLU ARG GLY GLN          
SEQRES  18 D  303  LEU SER VAL GLU ILE MET GLY ARG GLY TYR ALA TRP LEU          
SEQRES  19 D  303  ASP THR GLY THR HIS ASP SER LEU LEU GLU ALA GLY GLN          
SEQRES  20 D  303  PHE ILE ALA THR LEU GLU ASN ARG GLN GLY LEU LYS VAL          
SEQRES  21 D  303  ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN LYS TRP ILE          
SEQRES  22 D  303  ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA PRO LEU ALA          
SEQRES  23 D  303  LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG LEU LEU THR          
SEQRES  24 D  303  GLU THR VAL TYR                                              
HET    KDT  A1294      28                                                       
HET    MES  A1295      12                                                       
HET     CL  A1296       1                                                       
HET    KDT  B1294      28                                                       
HET    MES  B1295      12                                                       
HET     CL  B1296       1                                                       
HET    KDT  C1294      28                                                       
HET    MES  C1295      12                                                       
HET     CL  C1296       1                                                       
HET    KDT  D1294      28                                                       
HET    MES  D1295      12                                                       
HET     CL  D1296       1                                                       
HETNAM     KDT N-(6-AMINO-1-(4-BROMOBENZYL)-2,4-DIOXO-1,2,3,4-                  
HETNAM   2 KDT  TETRAHYDROPYRIMIDIN-5-YL)-N-METHYLBENZENESULFONAMIDE            
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM      CL CHLORIDE ION                                                     
FORMUL   5  KDT    4(C18 H17 BR N4 O4 S)                                        
FORMUL   6  MES    4(C6 H13 N O4 S)                                             
FORMUL   7   CL    4(CL 1-)                                                     
FORMUL  17  HOH   *473(H2 O)                                                    
HELIX    1   1 SER A   24  LEU A   27  5                                   4    
HELIX    2   2 ILE A   36  ALA A   46  1                                  11    
HELIX    3   3 ASP A   59  GLY A   68  1                                  10    
HELIX    4   4 GLY A   70  GLY A   74  5                                   5    
HELIX    5   5 GLY A   87  ALA A   89  5                                   3    
HELIX    6   6 GLN A   90  GLY A   95  1                                   6    
HELIX    7   7 GLY A   95  GLY A  100  1                                   6    
HELIX    8   8 ASP A  117  ARG A  128  1                                  12    
HELIX    9   9 ASP A  141  ARG A  144  5                                   4    
HELIX   10  10 GLN A  181  LEU A  189  1                                   9    
HELIX   11  11 GLU A  198  ARG A  209  1                                  12    
HELIX   12  12 THR A  228  GLY A  247  1                                  20    
HELIX   13  13 CYS A  252  GLN A  260  1                                   9    
HELIX   14  14 ASP A  264  ALA A  273  1                                  10    
HELIX   15  15 PRO A  274  ALA A  276  5                                   3    
HELIX   16  16 ASN A  278  LEU A  287  1                                  10    
HELIX   17  17 LEU A  288  GLU A  290  5                                   3    
HELIX   18  18 SER B   24  LEU B   27  5                                   4    
HELIX   19  19 ILE B   36  ALA B   46  1                                  11    
HELIX   20  20 ASP B   59  GLY B   68  1                                  10    
HELIX   21  21 GLY B   70  GLY B   74  5                                   5    
HELIX   22  22 ALA B   89  GLY B   95  1                                   7    
HELIX   23  23 GLY B   95  GLY B  100  1                                   6    
HELIX   24  24 ASP B  117  ARG B  128  1                                  12    
HELIX   25  25 ASP B  141  ARG B  144  5                                   4    
HELIX   26  26 GLN B  181  ASP B  188  1                                   8    
HELIX   27  27 GLU B  198  ARG B  209  1                                  12    
HELIX   28  28 THR B  228  GLY B  247  1                                  20    
HELIX   29  29 CYS B  252  GLN B  260  1                                   9    
HELIX   30  30 ASP B  264  ALA B  272  1                                   9    
HELIX   31  31 ASN B  278  LEU B  288  1                                  11    
HELIX   32  32 PRO C   18  ALA C   22  5                                   5    
HELIX   33  33 SER C   24  LEU C   27  5                                   4    
HELIX   34  34 ILE C   36  ALA C   46  1                                  11    
HELIX   35  35 ASP C   59  GLY C   68  1                                  10    
HELIX   36  36 GLY C   70  GLY C   74  5                                   5    
HELIX   37  37 GLY C   87  ALA C   89  5                                   3    
HELIX   38  38 GLN C   90  GLY C   95  1                                   6    
HELIX   39  39 GLY C   95  GLY C  100  1                                   6    
HELIX   40  40 ASP C  117  ARG C  128  1                                  12    
HELIX   41  41 ASP C  141  ARG C  144  5                                   4    
HELIX   42  42 GLN C  181  ASP C  188  1                                   8    
HELIX   43  43 GLU C  198  ARG C  209  1                                  12    
HELIX   44  44 THR C  228  GLY C  247  1                                  20    
HELIX   45  45 CYS C  252  GLN C  260  1                                   9    
HELIX   46  46 ASP C  264  ALA C  273  1                                  10    
HELIX   47  47 PRO C  274  ALA C  276  5                                   3    
HELIX   48  48 ASN C  278  GLU C  290  1                                  13    
HELIX   49  49 PRO D   18  ILE D   23  1                                   6    
HELIX   50  50 SER D   24  LEU D   27  5                                   4    
HELIX   51  51 ILE D   36  ALA D   46  1                                  11    
HELIX   52  52 GLN D   58  GLY D   68  1                                  11    
HELIX   53  53 GLY D   70  GLY D   74  5                                   5    
HELIX   54  54 ALA D   89  GLY D   95  1                                   7    
HELIX   55  55 GLY D   95  GLY D  100  1                                   6    
HELIX   56  56 ASP D  117  ARG D  128  1                                  12    
HELIX   57  57 ASP D  141  ARG D  144  5                                   4    
HELIX   58  58 GLN D  181  ASP D  188  1                                   8    
HELIX   59  59 GLU D  198  ARG D  209  1                                  12    
HELIX   60  60 THR D  228  GLY D  247  1                                  20    
HELIX   61  61 CYS D  252  GLN D  260  1                                   9    
HELIX   62  62 ASP D  264  ALA D  273  1                                  10    
HELIX   63  63 PRO D  274  ALA D  276  5                                   3    
HELIX   64  64 ASN D  278  GLU D  290  1                                  13    
SHEET    1  AA 7 ASP A  76  VAL A  81  0                                        
SHEET    2  AA 7 GLU A  50  SER A  55  1  O  ILE A  51   N  GLN A  78           
SHEET    3  AA 7 ARG A   3  LEU A   8  1  O  GLY A   5   N  LEU A  52           
SHEET    4  AA 7 LEU A 103  LEU A 108  1  O  LEU A 103   N  LYS A   4           
SHEET    5  AA 7 TYR A 170  TYR A 178 -1  O  GLY A 174   N  LEU A 108           
SHEET    6  AA 7 ALA A 132  HIS A 138 -1  O  SER A 133   N  PHE A 177           
SHEET    7  AA 7 LEU A 212  ILE A 216  1  O  SER A 213   N  VAL A 134           
SHEET    1  AB 2 PRO A  29  VAL A  30  0                                        
SHEET    2  AB 2 LYS A  33  PRO A  34 -1  O  LYS A  33   N  VAL A  30           
SHEET    1  AC 2 LEU A 112  TYR A 114  0                                        
SHEET    2  AC 2 ALA A 222  LEU A 224 -1  O  ALA A 222   N  TYR A 114           
SHEET    1  AD 2 GLY A 146  PHE A 150  0                                        
SHEET    2  AD 2 ALA A 156  GLU A 161 -1  N  ILE A 157   O  GLU A 149           
SHEET    1  BA 5 ASP B  76  VAL B  81  0                                        
SHEET    2  BA 5 GLU B  50  SER B  55  1  O  ILE B  51   N  GLN B  78           
SHEET    3  BA 5 ARG B   3  LEU B   8  1  O  GLY B   5   N  LEU B  52           
SHEET    4  BA 5 LEU B 103  LEU B 108  1  O  LEU B 103   N  LYS B   4           
SHEET    5  BA 5 LEU B 175  TYR B 178 -1  O  TYR B 176   N  LEU B 106           
SHEET    1  BB 2 PRO B  29  VAL B  30  0                                        
SHEET    2  BB 2 LYS B  33  PRO B  34 -1  O  LYS B  33   N  VAL B  30           
SHEET    1  BC 2 LEU B 112  TYR B 114  0                                        
SHEET    2  BC 2 ALA B 222  LEU B 224 -1  O  ALA B 222   N  TYR B 114           
SHEET    1  BD 3 TYR B 170  VAL B 172  0                                        
SHEET    2  BD 3 ALA B 132  HIS B 138 -1  O  TYR B 137   N  ALA B 171           
SHEET    3  BD 3 LEU B 212  ILE B 216  1  O  SER B 213   N  VAL B 134           
SHEET    1  BE 2 GLY B 146  PHE B 150  0                                        
SHEET    2  BE 2 ALA B 156  GLU B 161 -1  N  ILE B 157   O  GLU B 149           
SHEET    1  CA 7 ASP C  76  VAL C  81  0                                        
SHEET    2  CA 7 GLU C  50  SER C  55  1  O  ILE C  51   N  GLN C  78           
SHEET    3  CA 7 ARG C   3  LEU C   8  1  O  GLY C   5   N  LEU C  52           
SHEET    4  CA 7 LEU C 103  LEU C 108  1  O  LEU C 103   N  LYS C   4           
SHEET    5  CA 7 TYR C 170  TYR C 178 -1  O  GLY C 174   N  LEU C 108           
SHEET    6  CA 7 ALA C 132  HIS C 138 -1  O  SER C 133   N  PHE C 177           
SHEET    7  CA 7 LEU C 212  ILE C 216  1  O  SER C 213   N  VAL C 134           
SHEET    1  CB 2 PRO C  29  VAL C  30  0                                        
SHEET    2  CB 2 LYS C  33  PRO C  34 -1  O  LYS C  33   N  VAL C  30           
SHEET    1  CC 2 ASN C 111  TYR C 114  0                                        
SHEET    2  CC 2 ALA C 222  ASP C 225 -1  O  ALA C 222   N  TYR C 114           
SHEET    1  CD 2 GLY C 146  PHE C 150  0                                        
SHEET    2  CD 2 ALA C 156  GLU C 161 -1  N  ILE C 157   O  GLU C 149           
SHEET    1  DA 7 ASP D  76  VAL D  81  0                                        
SHEET    2  DA 7 GLU D  50  SER D  55  1  O  ILE D  51   N  GLN D  78           
SHEET    3  DA 7 ARG D   3  LEU D   8  1  O  GLY D   5   N  LEU D  52           
SHEET    4  DA 7 LEU D 103  LEU D 108  1  O  LEU D 103   N  LYS D   4           
SHEET    5  DA 7 TYR D 170  TYR D 178 -1  O  GLY D 174   N  LEU D 108           
SHEET    6  DA 7 GLY D 146  PHE D 150  1  O  GLY D 146   N  VAL D 172           
SHEET    7  DA 7 ALA D 156  GLU D 161  1  N  ILE D 157   O  GLU D 149           
SHEET    1  DB 7 ASP D  76  VAL D  81  0                                        
SHEET    2  DB 7 GLU D  50  SER D  55  1  O  ILE D  51   N  GLN D  78           
SHEET    3  DB 7 ARG D   3  LEU D   8  1  O  GLY D   5   N  LEU D  52           
SHEET    4  DB 7 LEU D 103  LEU D 108  1  O  LEU D 103   N  LYS D   4           
SHEET    5  DB 7 TYR D 170  TYR D 178 -1  O  GLY D 174   N  LEU D 108           
SHEET    6  DB 7 ALA D 132  HIS D 138 -1  O  SER D 133   N  PHE D 177           
SHEET    7  DB 7 LEU D 212  ILE D 216  1  O  SER D 213   N  VAL D 134           
SHEET    1  DC 2 PRO D  29  VAL D  30  0                                        
SHEET    2  DC 2 LYS D  33  PRO D  34 -1  O  LYS D  33   N  VAL D  30           
SHEET    1  DD 2 ASN D 111  TYR D 114  0                                        
SHEET    2  DD 2 ALA D 222  ASP D 225 -1  O  ALA D 222   N  TYR D 114           
CISPEP   1 HIS A   17    PRO A   18          0         7.86                     
CISPEP   2 HIS B   17    PRO B   18          0         6.37                     
CISPEP   3 HIS C   17    PRO C   18          0         5.25                     
CISPEP   4 HIS D   17    PRO D   18          0         6.11                     
SITE     1 AC1 17 LEU A  45  TYR A 113  TYR A 114  GLY A 115                    
SITE     2 AC1 17 PHE A 118  ARG A 219  LYS A 249  VAL A 250                    
SITE     3 AC1 17 ALA A 251  GLU A 255  ILE A 256  ARG A 259                    
SITE     4 AC1 17 GLN A 260  HOH A2049  HOH A2051  HOH A2110                    
SITE     5 AC1 17 HOH A2128                                                     
SITE     1 AC2  8 GLY A 154  LYS A 155  ALA A 156  SER A 213                    
SITE     2 AC2  8 VAL A 214  ILE A 216  TYR A 293  HOH A2071                    
SITE     1 AC3 14 LEU B  45  TYR B 113  GLY B 115  PHE B 118                    
SITE     2 AC3 14 ARG B 219  LYS B 249  VAL B 250  ALA B 251                    
SITE     3 AC3 14 GLU B 255  ILE B 256  GLN B 260  HOH B2041                    
SITE     4 AC3 14 HOH B2043  HOH B2097                                          
SITE     1 AC4  8 PHE B 150  GLY B 154  ALA B 156  LEU B 212                    
SITE     2 AC4  8 SER B 213  VAL B 214  ILE B 216  TYR B 293                    
SITE     1 AC5 16 SER C  41  LEU C  45  TYR C 113  TYR C 114                    
SITE     2 AC5 16 GLY C 115  PHE C 118  ARG C 219  VAL C 250                    
SITE     3 AC5 16 ALA C 251  GLU C 255  ILE C 256  ARG C 259                    
SITE     4 AC5 16 GLN C 260  HOH C2046  HOH C2047  HOH C2106                    
SITE     1 AC6  7 PHE C 150  GLY C 154  ALA C 156  SER C 213                    
SITE     2 AC6  7 VAL C 214  ILE C 216  TYR C 293                               
SITE     1 AC7 15 SER D  41  LEU D  45  TYR D 113  TYR D 114                    
SITE     2 AC7 15 GLY D 115  ARG D 219  VAL D 250  ALA D 251                    
SITE     3 AC7 15 GLU D 255  ILE D 256  GLN D 260  HOH D2042                    
SITE     4 AC7 15 HOH D2044  HOH D2084  HOH D2110                               
SITE     1 AC8  5 GLY D 154  ALA D 156  SER D 213  VAL D 214                    
SITE     2 AC8  5 ILE D 216                                                     
SITE     1 AC9  3 HIS A 116  ARG A 219  GLY A 220                               
SITE     1 BC1  3 HIS B 116  GLY B 218  GLY B 220                               
SITE     1 BC2  3 HIS C 116  GLY C 218  GLY C 220                               
SITE     1 BC3  3 HIS D 116  GLY D 218  GLY D 220                               
CRYST1   64.260  154.350  134.810  90.00  92.40  90.00 C 1 2 1      16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015562  0.000000  0.000652        0.00000                         
SCALE2      0.000000  0.006479  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007424        0.00000                         
MTRIX1   1 -0.936100  0.009204 -0.351600       62.49000    1                    
MTRIX2   1 -0.004838 -0.999900 -0.013300      -35.85000    1                    
MTRIX3   1 -0.351600 -0.010750  0.936100       10.93000    1                    
MTRIX1   2  0.999000 -0.005062 -0.043660        5.69800    1                    
MTRIX2   2 -0.004378 -0.999900  0.015750      -17.30000    1                    
MTRIX3   2 -0.043730 -0.015550 -0.998900       68.22000    1                    
MTRIX1   3 -0.956800  0.009164  0.290600       40.38000    1                    
MTRIX2   3  0.012210  0.999900  0.008668      -20.57000    1                    
MTRIX3   3 -0.290500  0.011840 -0.956800       72.62000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system