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Database: PDB
Entry: 5FTS
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HEADER    TRANSFERASE                             14-JAN-16   5FTS              
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 5FTS    1       REMARK                                   
REVDAT   1   22-FEB-17 5FTS    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.    2.20 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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 134.37                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 62257                          
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3144                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4252                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.50                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 215                          
REMARK   3   BIN FREE R VALUE                    : 0.3310                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9220                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 164                                     
REMARK   3   SOLVENT ATOMS            : 337                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.25                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.48000                                              
REMARK   3    B22 (A**2) : 0.56700                                              
REMARK   3    B33 (A**2) : -1.01400                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.36000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.319         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.241         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.200         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.206         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.897                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9680 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  9166 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13160 ; 1.686 ; 2.003       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 21064 ; 1.018 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1174 ; 6.910 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   438 ;34.502 ;24.247       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1572 ;15.160 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    56 ;16.965 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1414 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10984 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2232 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4204 ; 0.207 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):   160 ; 0.196 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  9176 ; 0.176 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   488 ; 0.144 ; 0.200       
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):  4702 ; 2.241 ; 2.950       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4701 ; 2.241 ; 2.950       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5868 ; 3.562 ; 4.415       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4978 ; 2.570 ; 3.306       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  7290 ; 4.206 ; 4.825       
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   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
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 5FTS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1290066042.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
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   : 62373                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 23.660                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.8                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.16000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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   (%): 49.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
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       32.00500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       76.97000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       32.00500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       76.97000            
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: 17760 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 44040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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       64.01000            
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: 17460 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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       58.44891            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      134.36497            
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    -9                                                      
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 A   3   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 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       33.93    -81.92                                   
REMARK 500    TYR A  31      -97.82     60.89                                   
REMARK 500    TYR B  31      -85.93     61.19                                   
REMARK 500    PRO B 193      -23.03    -39.96                                   
REMARK 500    TYR C  31      -97.94     60.79                                   
REMARK 500    ARG C 128      102.62    -58.37                                   
REMARK 500    TYR D  31      -96.41     62.39                                   
REMARK 500    ARG D 128       98.61    -65.91                                   
REMARK 500    ASP D 179     -162.31   -101.07                                   
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 P3I 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 P3I 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 P3I 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 P3I 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 D 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 A 1296                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1296                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 N-TERMINAL HIS-TAG PRESENT                                           
DBREF  5FTS A    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  5FTS B    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  5FTS C    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  5FTS D    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
SEQADV 5FTS HIS A   -9  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS A   -8  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS A   -7  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS A   -6  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS A   -5  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS A   -4  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS GLY A   -3  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS SER A   -2  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS MET A   -1  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS ALA A    0  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS B   -9  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS B   -8  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS B   -7  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS B   -6  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS B   -5  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS B   -4  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS GLY B   -3  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS SER B   -2  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS MET B   -1  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS ALA B    0  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS C   -9  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS C   -8  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS C   -7  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS C   -6  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS C   -5  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS C   -4  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS GLY C   -3  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS SER C   -2  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS MET C   -1  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS ALA C    0  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS D   -9  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS D   -8  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS D   -7  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS D   -6  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS D   -5  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS HIS D   -4  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS GLY D   -3  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS SER D   -2  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS MET D   -1  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FTS 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    P3I  A1294      44                                                       
HET    MES  A1295      12                                                       
HET     CL  A1296       1                                                       
HET    P3I  B1294      44                                                       
HET    MES  B1295      12                                                       
HET     CL  B1296       1                                                       
HET    P3I  C1294      44                                                       
HET    MES  C1295      12                                                       
HET     CL  C1296       1                                                       
HET    P3I  D1294      44                                                       
HET    MES  D1295      12                                                       
HET     CL  D1296       1                                                       
HETNAM     P3I N-(6-AMINO-1-(2-BROMOBENZYL)-2,4-DIOXO-1,2,3,4-                  
HETNAM   2 P3I  TETRAHYDROPYRIMIDIN-5-YL)-N-METHYLBENZENESULFONAMIDE            
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM      CL CHLORIDE ION                                                     
FORMUL   5  P3I    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   *337(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 GLN A   90  GLY A   95  1                                   6    
HELIX    6   6 GLY A   95  GLY A  100  1                                   6    
HELIX    7   7 ASP A  117  GLN A  127  1                                  11    
HELIX    8   8 ASP A  141  ARG A  144  5                                   4    
HELIX    9   9 GLN A  181  LEU A  189  1                                   9    
HELIX   10  10 GLU A  198  ARG A  209  1                                  12    
HELIX   11  11 THR A  228  GLY A  247  1                                  20    
HELIX   12  12 CYS A  252  GLN A  260  1                                   9    
HELIX   13  13 ASP A  264  ALA A  273  1                                  10    
HELIX   14  14 PRO A  274  ALA A  276  5                                   3    
HELIX   15  15 ASN A  278  LEU A  288  1                                  11    
HELIX   16  16 PRO B   18  ILE B   23  1                                   6    
HELIX   17  17 SER B   24  LEU B   27  5                                   4    
HELIX   18  18 ILE B   36  ALA B   46  1                                  11    
HELIX   19  19 ASP B   59  GLY B   68  1                                  10    
HELIX   20  20 GLY B   70  GLY B   74  5                                   5    
HELIX   21  21 ALA B   89  GLY B   95  1                                   7    
HELIX   22  22 GLY B   95  GLY B  100  1                                   6    
HELIX   23  23 ASP B  117  GLN B  127  1                                  11    
HELIX   24  24 ASP B  141  ARG B  144  5                                   4    
HELIX   25  25 GLN B  181  ASP B  188  1                                   8    
HELIX   26  26 GLU B  198  ARG B  209  1                                  12    
HELIX   27  27 THR B  228  GLY B  247  1                                  20    
HELIX   28  28 CYS B  252  GLN B  260  1                                   9    
HELIX   29  29 ASP B  264  ALA B  273  1                                  10    
HELIX   30  30 PRO B  274  ALA B  276  5                                   3    
HELIX   31  31 ASN B  278  GLU B  290  1                                  13    
HELIX   32  32 SER C   24  LEU C   27  5                                   4    
HELIX   33  33 ILE C   36  ALA C   46  1                                  11    
HELIX   34  34 ASP C   59  GLY C   68  1                                  10    
HELIX   35  35 GLY C   70  GLY C   74  5                                   5    
HELIX   36  36 ALA C   89  GLY C   95  1                                   7    
HELIX   37  37 GLY C   95  GLY C  100  1                                   6    
HELIX   38  38 ASP C  117  ARG C  128  1                                  12    
HELIX   39  39 ASP C  141  ARG C  144  5                                   4    
HELIX   40  40 GLN C  181  LEU C  189  1                                   9    
HELIX   41  41 GLU C  198  ARG C  209  1                                  12    
HELIX   42  42 THR C  228  GLY C  247  1                                  20    
HELIX   43  43 CYS C  252  GLN C  260  1                                   9    
HELIX   44  44 ASP C  264  ALA C  273  1                                  10    
HELIX   45  45 ASN C  278  GLU C  290  1                                  13    
HELIX   46  46 PRO D   18  ILE D   23  1                                   6    
HELIX   47  47 SER D   24  LEU D   27  5                                   4    
HELIX   48  48 ILE D   36  ALA D   46  1                                  11    
HELIX   49  49 ASP D   59  GLY D   68  1                                  10    
HELIX   50  50 GLY D   70  GLY D   74  5                                   5    
HELIX   51  51 ALA D   89  GLY D   95  1                                   7    
HELIX   52  52 GLY D   95  GLY D  100  1                                   6    
HELIX   53  53 ASP D  117  ARG D  128  1                                  12    
HELIX   54  54 ASP D  141  ARG D  144  5                                   4    
HELIX   55  55 GLN D  181  ASP D  188  1                                   8    
HELIX   56  56 GLU D  198  ARG D  209  1                                  12    
HELIX   57  57 THR D  228  GLY D  247  1                                  20    
HELIX   58  58 CYS D  252  GLN D  260  1                                   9    
HELIX   59  59 ASP D  264  ALA D  273  1                                  10    
HELIX   60  60 PRO D  274  ALA D  276  5                                   3    
HELIX   61  61 ASN D  278  GLU D  290  1                                  13    
SHEET    1   A 5 ASP A  76  VAL A  81  0                                        
SHEET    2   A 5 GLU A  50  SER A  55  1  N  ILE A  53   O  GLN A  78           
SHEET    3   A 5 ARG A   3  ALA A   9  1  N  GLY A   5   O  GLU A  50           
SHEET    4   A 5 LEU A 103  LEU A 108  1  O  ALA A 105   N  ILE A   6           
SHEET    5   A 5 LEU A 175  TYR A 178 -1  O  TYR A 176   N  LEU A 106           
SHEET    1   B 2 PRO A  29  VAL A  30  0                                        
SHEET    2   B 2 LYS A  33  PRO A  34 -1  O  LYS A  33   N  VAL A  30           
SHEET    1   C 2 LEU A 112  TYR A 114  0                                        
SHEET    2   C 2 ALA A 222  LEU A 224 -1  O  ALA A 222   N  TYR A 114           
SHEET    1   D 3 TYR A 170  VAL A 172  0                                        
SHEET    2   D 3 ALA A 132  HIS A 138 -1  N  TYR A 137   O  ALA A 171           
SHEET    3   D 3 LEU A 212  ILE A 216  1  O  GLU A 215   N  ALA A 136           
SHEET    1   E 2 GLY A 146  PHE A 150  0                                        
SHEET    2   E 2 ALA A 156  GLU A 161 -1  O  ILE A 157   N  GLU A 149           
SHEET    1   F 7 ASP B  76  VAL B  81  0                                        
SHEET    2   F 7 GLU B  50  SER B  55  1  N  ILE B  53   O  GLN B  78           
SHEET    3   F 7 ARG B   3  LEU B   8  1  N  GLY B   5   O  LEU B  52           
SHEET    4   F 7 LEU B 103  LEU B 108  1  O  ALA B 105   N  ILE B   6           
SHEET    5   F 7 TYR B 170  TYR B 178 -1  O  TYR B 176   N  LEU B 106           
SHEET    6   F 7 ALA B 132  HIS B 138 -1  N  PHE B 135   O  THR B 173           
SHEET    7   F 7 LEU B 212  ILE B 216  1  O  SER B 213   N  ALA B 132           
SHEET    1   G 2 PRO B  29  VAL B  30  0                                        
SHEET    2   G 2 LYS B  33  PRO B  34 -1  O  LYS B  33   N  VAL B  30           
SHEET    1   H 2 ASN B 111  TYR B 114  0                                        
SHEET    2   H 2 ALA B 222  ASP B 225 -1  O  ALA B 222   N  TYR B 114           
SHEET    1   I 2 GLY B 146  PHE B 150  0                                        
SHEET    2   I 2 ALA B 156  GLU B 161 -1  O  ILE B 157   N  GLU B 149           
SHEET    1   J 5 ASP C  76  VAL C  81  0                                        
SHEET    2   J 5 GLU C  50  SER C  55  1  N  ILE C  53   O  GLN C  78           
SHEET    3   J 5 ARG C   3  ALA C   9  1  N  ALA C   9   O  ILE C  54           
SHEET    4   J 5 LEU C 103  LEU C 108  1  O  LEU C 103   N  LYS C   4           
SHEET    5   J 5 LEU C 175  TYR C 178 -1  O  TYR C 176   N  LEU C 106           
SHEET    1   K 2 PRO C  29  VAL C  30  0                                        
SHEET    2   K 2 LYS C  33  PRO C  34 -1  O  LYS C  33   N  VAL C  30           
SHEET    1   L 2 LEU C 112  TYR C 114  0                                        
SHEET    2   L 2 ALA C 222  LEU C 224 -1  O  ALA C 222   N  TYR C 114           
SHEET    1   M 3 TYR C 170  VAL C 172  0                                        
SHEET    2   M 3 ALA C 132  HIS C 138 -1  N  TYR C 137   O  ALA C 171           
SHEET    3   M 3 LEU C 212  ILE C 216  1  O  SER C 213   N  ALA C 132           
SHEET    1   N 2 GLY C 146  PHE C 150  0                                        
SHEET    2   N 2 ALA C 156  GLU C 161 -1  O  ILE C 157   N  GLU C 149           
SHEET    1   O 7 ASP D  76  VAL D  81  0                                        
SHEET    2   O 7 GLU D  50  SER D  55  1  N  ILE D  53   O  GLN D  78           
SHEET    3   O 7 ARG D   3  LEU D   8  1  N  GLY D   5   O  GLU D  50           
SHEET    4   O 7 LEU D 103  LEU D 108  1  O  ALA D 105   N  ILE D   6           
SHEET    5   O 7 TYR D 170  TYR D 178 -1  O  TYR D 176   N  LEU D 106           
SHEET    6   O 7 ALA D 132  HIS D 138 -1  N  SER D 133   O  PHE D 177           
SHEET    7   O 7 LEU D 212  ILE D 216  1  O  SER D 213   N  ALA D 132           
SHEET    1   P 2 PRO D  29  VAL D  30  0                                        
SHEET    2   P 2 LYS D  33  PRO D  34 -1  O  LYS D  33   N  VAL D  30           
SHEET    1   Q 2 ASN D 111  TYR D 114  0                                        
SHEET    2   Q 2 ALA D 222  ASP D 225 -1  O  LEU D 224   N  LEU D 112           
SHEET    1   R 2 GLY D 146  PHE D 150  0                                        
SHEET    2   R 2 ALA D 156  GLU D 161 -1  O  ILE D 157   N  GLU D 149           
CISPEP   1 HIS A   17    PRO A   18          0         8.59                     
CISPEP   2 HIS B   17    PRO B   18          0         5.32                     
CISPEP   3 HIS C   17    PRO C   18          0        10.59                     
CISPEP   4 HIS D   17    PRO D   18          0         2.85                     
SITE     1 AC1 13 SER A  41  LEU A  45  TYR A 113  GLY A 115                    
SITE     2 AC1 13 PHE A 118  HIS A 119  ARG A 219  LYS A 249                    
SITE     3 AC1 13 VAL A 250  ALA A 251  GLU A 255  HOH A2044                    
SITE     4 AC1 13 HOH A2091                                                     
SITE     1 AC2  5 PHE A 150  GLY A 154  ALA A 156  SER A 213                    
SITE     2 AC2  5 VAL A 214                                                     
SITE     1 AC3 12 SER B  41  LEU B  45  TYR B 113  GLY B 115                    
SITE     2 AC3 12 PHE B 118  HIS B 119  ARG B 219  LYS B 249                    
SITE     3 AC3 12 VAL B 250  ALA B 251  HOH B2033  HOH B2072                    
SITE     1 AC4  5 PHE B 150  GLY B 154  ALA B 156  SER B 213                    
SITE     2 AC4  5 VAL B 214                                                     
SITE     1 AC5 11 SER C  41  LEU C  45  TYR C 113  GLY C 115                    
SITE     2 AC5 11 HIS C 119  LYS C 249  VAL C 250  ALA C 251                    
SITE     3 AC5 11 ARG C 259  HOH C2035  HOH C2067                               
SITE     1 AC6  7 PHE C 150  GLY C 154  LYS C 155  ALA C 156                    
SITE     2 AC6  7 LEU C 212  VAL C 214  TYR C 293                               
SITE     1 AC7 11 SER D  41  LEU D  45  TYR D 113  GLY D 115                    
SITE     2 AC7 11 HIS D 119  ARG D 219  LYS D 249  VAL D 250                    
SITE     3 AC7 11 ALA D 251  HOH D2037  HOH D2063                               
SITE     1 AC8  6 PHE D 150  GLY D 154  LYS D 155  ALA D 156                    
SITE     2 AC8  6 VAL D 214  TYR D 293                                          
SITE     1 AC9  2 HIS D 116  GLY D 220                                          
SITE     1 BC1  3 HIS B 116  GLY B 220  HOH B2032                               
SITE     1 BC2  3 HIS A 116  GLY A 218  GLY A 220                               
SITE     1 BC3  2 HIS C 116  GLY C 220                                          
CRYST1   64.010  153.940  134.480  90.00  92.37  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      0.015623  0.000000  0.000647        0.00000                         
SCALE2      0.000000  0.006496  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007442        0.00000                         
MTRIX1   1  0.999100 -0.007168 -0.042000        5.53500    1                    
MTRIX2   1 -0.006587 -0.999900  0.013950      -17.18000    1                    
MTRIX3   1 -0.042100 -0.013620 -0.999000       68.09000    1                    
MTRIX1   2 -0.938000  0.008696 -0.346400       62.29000    1                    
MTRIX2   2 -0.004596 -0.999900 -0.012650      -35.80000    1                    
MTRIX3   2 -0.346500 -0.010280  0.938000       10.73000    1                    
MTRIX1   3 -0.957600  0.010190  0.288100       40.46000    1                    
MTRIX2   3  0.013570  0.999900  0.009741      -20.60000    1                    
MTRIX3   3 -0.287900  0.013240 -0.957600       72.42000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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