GenomeNet

Database: PDB
Entry: 5FUH
LinkDB: 5FUH
Original site: 5FUH 
HEADER    TRANSFERASE                             27-JAN-16   5FUH              
TITLE     PSEUDOMONAS AERUGINOSA RMLA IN COMPLEX WITH ALLOSTERIC                
TITLE    2 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   1   22-FEB-17 5FUH    0                                                
JRNL        AUTH   F.TRAN,M.S.ALPHEY,N.J.WESTWOOD,J.H.NAISMITH                  
JRNL        TITL   ALLOSTERIC COMPETITIVE INHIBITORS OF THE GLUCOSE-1-          
JRNL        TITL 2 PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA) FROM PSEUDOMONAS      
JRNL        TITL 3 AERUGINOSA.                                                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.600                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 67.349                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.180                         
REMARK   3   NUMBER OF REFLECTIONS             : 172334                         
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.2020                          
REMARK   3   FREE R VALUE                     : 0.2269                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.03                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 8570                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.6                          
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.642                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 11749                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.279                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 597                          
REMARK   3   BIN FREE R VALUE                    : 0.288                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9343                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 188                                     
REMARK   3   SOLVENT ATOMS            : 572                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.5                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.619                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.557                                                
REMARK   3    B22 (A**2) : 0.307                                                
REMARK   3    B33 (A**2) : -0.820                                               
REMARK   3    B12 (A**2) : 0.000                                                
REMARK   3    B13 (A**2) : -0.468                                               
REMARK   3    B23 (A**2) : 0.000                                                
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.094         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.092         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.070         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.997         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9752 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  9311 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13258 ; 1.310 ; 1.998       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 21421 ; 0.913 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1204 ; 5.951 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   443 ;32.695 ;24.289       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1609 ;11.463 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    56 ;12.997 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1444 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11056 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2234 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4432 ; 0.191 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):   152 ; 0.181 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  9206 ; 0.168 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   454 ; 0.102 ; 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):  4750 ; 1.413 ; 2.780       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4749 ; 1.412 ; 2.780       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5934 ; 2.283 ; 4.164       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5001 ; 1.816 ; 3.050       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  7310 ; 2.941 ; 4.472       
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   : 1.200                                         
REMARK   3   ION PROBE RADIUS   : 0.400                                         
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   3   SOME RESIDUES AT THE N-TERMINUS ARE DISORDERED. SOME               
REMARK   3    RESIDUES HAVE BEEN MODELLED IN MULTIPLE CONFORMATIONS.            
REMARK   3    THE BOUND INHIBITOR HAS PARTIAL OCCUPANCY.                        
REMARK   3 SOME EXTRA ELECTRON DENSITY IS OBSERVED IN THE PARTIALLY             
REMARK   3 OCCUPIED INHIBITOR BINDING SITE, MOST LIKELY DUE TO WATERS           
REMARK   3 BOUND WHEN INHIBITOR IS ABSENT.                                      
REMARK   3 SOME EXTRA ELECTRON DENSITY IS OBSERVED NEAR THE MULTIPLE            
REMARK   3 CONFORMATIONS OF GLN237, MOST LIKELY DUE TO WATERS BOUND             
REMARK   3 WHEN SIDE CHAIN IS IN ALTERNATIVE CONFORMATION.                      
REMARK   4                                                                      
REMARK   4 5FUH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JAN-16.                  
REMARK 100 THE PDBE ID CODE IS EBI-66122.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 175397                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.59                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 67.35                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 6                                  
REMARK 200  R MERGE                    (I) : 0.10                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.50                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.5                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.68                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.10                               
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   (%): 52.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 4% PEG 6000, 0.1 M MES PH 6,             
REMARK 280  0.05 M 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       32.23000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       77.63000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       32.23000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       77.63000            
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: 19360 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -89.6 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       64.46000            
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: 20270 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -108.3 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       58.50827            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      134.69857            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2082   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH B2054   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH B2113   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH C2063   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH C2121   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH D2041   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH D2077   LIES ON A SPECIAL POSITION.                         
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    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     MET A    -1                                                      
REMARK 465     ALA A     0                                                      
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     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     SER C    -2                                                      
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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1B GLN C   237     OE1B GLN D   237              1.35            
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    HIS A  -6      -63.06    -99.25                                   
REMARK 500    SER A  12       33.84   -153.67                                   
REMARK 500    TYR A  31      -96.07     60.55                                   
REMARK 500    ALA B   9       58.56   -118.80                                   
REMARK 500    SER B  12       32.46    -93.23                                   
REMARK 500    TYR B  31      -83.84     61.23                                   
REMARK 500    ALA C   9       61.02   -119.43                                   
REMARK 500    SER C  12       25.96   -147.44                                   
REMARK 500    TYR C  31      -85.65     61.35                                   
REMARK 500    ALA D   9       66.78   -103.77                                   
REMARK 500    TYR D  31      -88.94     60.73                                   
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 HKX A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A1294                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HKX B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B1294                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HKX C 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES C1294                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HKX D 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES D1294                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL D1295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL C1295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1296                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D1296                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1296                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D1297                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5FU8   RELATED DB: PDB                                   
REMARK 900  PSEUDOMONAS AERUGINOSA RMLA IN COMPLEX WITH ALLOSTERIC              
REMARK 900  INHIBITOR                                                           
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 N-TERMINAL HIS-TAG PRESENT                                           
DBREF  5FUH A    1   293  UNP    Q9HU22   G3XCK4_PSEAI     1    293             
DBREF  5FUH B    1   293  UNP    Q9HU22   G3XCK4_PSEAI     1    293             
DBREF  5FUH C    1   293  UNP    Q9HU22   G3XCK4_PSEAI     1    293             
DBREF  5FUH D    1   293  UNP    Q9HU22   G3XCK4_PSEAI     1    293             
SEQADV 5FUH HIS A   -9  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS A   -8  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS A   -7  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS A   -6  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS A   -5  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS A   -4  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH GLY A   -3  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH SER A   -2  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH MET A   -1  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH ALA A    0  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS B   -9  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS B   -8  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS B   -7  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS B   -6  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS B   -5  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS B   -4  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH GLY B   -3  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH SER B   -2  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH MET B   -1  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH ALA B    0  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS C   -9  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS C   -8  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS C   -7  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS C   -6  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS C   -5  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS C   -4  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH GLY C   -3  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH SER C   -2  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH MET C   -1  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH ALA C    0  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS D   -9  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS D   -8  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS D   -7  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS D   -6  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS D   -5  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH HIS D   -4  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH GLY D   -3  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH SER D   -2  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH MET D   -1  UNP  Q9HU22              EXPRESSION TAG                 
SEQADV 5FUH 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    HKX  A 400      28                                                       
HET    MES  A1294      12                                                       
HET    HKX  B 400      28                                                       
HET    MES  B1294      12                                                       
HET    HKX  C 400      28                                                       
HET    MES  C1294      12                                                       
HET    HKX  D 400      28                                                       
HET    MES  D1294      12                                                       
HET     CL  A1295       1                                                       
HET     CL  B1295       1                                                       
HET     CL  D1295       1                                                       
HET     CL  C1295       1                                                       
HET    GOL  A1296       6                                                       
HET    GOL  D1296       6                                                       
HET    GOL  C1296       6                                                       
HET    GOL  D1297       6                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM     HKX N-[6-AMINO-1-(3-BROMOBENZYL)-2,4-DIOXO-1,2,3,                    
HETNAM   2 HKX  4-TETRAHYDROPYRIMIDIN-5-YL]-N-                                  
HETNAM   3 HKX  METHYLBENZENESULFONAMIDE                                        
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5   CL    4(CL 1-)                                                     
FORMUL   6  GOL    4(C3 H8 O3)                                                  
FORMUL   7  HKX    4(C18 H17 BR N4 O4 S)                                        
FORMUL   8  MES    4(C6 H13 N O4 S)                                             
FORMUL   9  HOH   *572(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 ALA A   89  GLY A   95  1                                   7    
HELIX    6   6 GLY A   95  GLY A  100  1                                   6    
HELIX    7   7 ASP A  117  ARG A  128  1                                  12    
HELIX    8   8 ASP A  141  ARG A  144  5                                   4    
HELIX    9   9 GLN A  181  ASP A  188  1                                   8    
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 SER B   24  LEU B   27  5                                   4    
HELIX   17  17 ILE B   36  ALA B   46  1                                  11    
HELIX   18  18 ASP B   59  GLY B   68  1                                  10    
HELIX   19  19 GLY B   70  GLY B   74  5                                   5    
HELIX   20  20 ALA B   89  GLY B   95  1                                   7    
HELIX   21  21 GLY B   95  GLY B  100  1                                   6    
HELIX   22  22 ASP B  117  ARG B  128  1                                  12    
HELIX   23  23 ASP B  141  ARG B  144  5                                   4    
HELIX   24  24 GLN B  181  ASP B  188  1                                   8    
HELIX   25  25 GLU B  198  ARG B  209  1                                  12    
HELIX   26  26 THR B  228  GLY B  247  1                                  20    
HELIX   27  27 CYS B  252  GLN B  260  1                                   9    
HELIX   28  28 ASP B  264  ALA B  273  1                                  10    
HELIX   29  29 ASN B  278  LEU B  288  1                                  11    
HELIX   30  30 PRO C   18  ILE C   23  1                                   6    
HELIX   31  31 SER C   24  LEU C   27  5                                   4    
HELIX   32  32 ILE C   36  ALA C   46  1                                  11    
HELIX   33  33 ASP C   59  GLY C   68  1                                  10    
HELIX   34  34 GLY C   70  GLY C   74  5                                   5    
HELIX   35  35 ALA C   89  GLY C   95  1                                   7    
HELIX   36  36 GLY C   95  GLY C  100  1                                   6    
HELIX   37  37 ASP C  117  ARG C  128  1                                  12    
HELIX   38  38 ASP C  141  ARG C  144  5                                   4    
HELIX   39  39 GLN C  181  ASP C  188  1                                   8    
HELIX   40  40 GLU C  198  ARG C  209  1                                  12    
HELIX   41  41 THR C  228  GLY C  247  1                                  20    
HELIX   42  42 CYS C  252  GLN C  260  1                                   9    
HELIX   43  43 ASP C  264  ALA C  273  1                                  10    
HELIX   44  44 PRO C  274  ALA C  276  5                                   3    
HELIX   45  45 ASN C  278  LEU C  288  1                                  11    
HELIX   46  46 SER D   24  LEU D   27  5                                   4    
HELIX   47  47 ILE D   36  ALA D   46  1                                  11    
HELIX   48  48 ASP D   59  GLY D   68  1                                  10    
HELIX   49  49 GLY D   70  GLY D   74  5                                   5    
HELIX   50  50 ALA D   89  GLY D   95  1                                   7    
HELIX   51  51 GLY D   95  GLY D  100  1                                   6    
HELIX   52  52 ASP D  117  ARG D  128  1                                  12    
HELIX   53  53 ASP D  141  ARG D  144  5                                   4    
HELIX   54  54 GLN D  181  ASP D  188  1                                   8    
HELIX   55  55 GLU D  198  ARG D  209  1                                  12    
HELIX   56  56 THR D  228  GLY D  247  1                                  20    
HELIX   57  57 CYS D  252  GLN D  260  1                                   9    
HELIX   58  58 ASP D  264  ALA D  273  1                                  10    
HELIX   59  59 PRO D  274  ALA D  276  5                                   3    
HELIX   60  60 ASN D  278  LEU D  288  1                                  11    
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  ALA A   9  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 7 ASP B  76  VAL B  81  0                                        
SHEET    2  BA 7 GLU B  50  SER B  55  1  O  ILE B  51   N  GLN B  78           
SHEET    3  BA 7 ARG B   3  ALA B   9  1  O  GLY B   5   N  LEU B  52           
SHEET    4  BA 7 LEU B 103  LEU B 108  1  O  LEU B 103   N  LYS B   4           
SHEET    5  BA 7 TYR B 170  TYR B 178 -1  O  GLY B 174   N  LEU B 108           
SHEET    6  BA 7 ALA B 132  HIS B 138 -1  O  SER B 133   N  PHE B 177           
SHEET    7  BA 7 LEU B 212  ILE B 216  1  O  SER B 213   N  VAL B 134           
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 2 GLY B 146  PHE B 150  0                                        
SHEET    2  BD 2 ALA B 156  GLU B 161 -1  N  ILE B 157   O  GLU B 149           
SHEET    1  CA 5 ASP C  76  VAL C  81  0                                        
SHEET    2  CA 5 GLU C  50  SER C  55  1  O  ILE C  51   N  GLN C  78           
SHEET    3  CA 5 ARG C   3  LEU C   8  1  O  GLY C   5   N  LEU C  52           
SHEET    4  CA 5 LEU C 103  LEU C 108  1  O  LEU C 103   N  LYS C   4           
SHEET    5  CA 5 LEU C 175  TYR C 178 -1  O  TYR C 176   N  LEU C 106           
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 LEU C 112  TYR C 114  0                                        
SHEET    2  CC 2 ALA C 222  LEU C 224 -1  O  ALA C 222   N  TYR C 114           
SHEET    1  CD 3 TYR C 170  VAL C 172  0                                        
SHEET    2  CD 3 ALA C 132  HIS C 138 -1  O  TYR C 137   N  ALA C 171           
SHEET    3  CD 3 LEU C 212  ILE C 216  1  O  SER C 213   N  VAL C 134           
SHEET    1  CE 2 GLY C 146  PHE C 150  0                                        
SHEET    2  CE 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  ALA D   9  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 ALA D 132  HIS D 138 -1  O  SER D 133   N  PHE D 177           
SHEET    7  DA 7 LEU D 212  ILE D 216  1  O  SER D 213   N  VAL D 134           
SHEET    1  DB 2 PRO D  29  VAL D  30  0                                        
SHEET    2  DB 2 LYS D  33  PRO D  34 -1  O  LYS D  33   N  VAL D  30           
SHEET    1  DC 2 ASN D 111  TYR D 114  0                                        
SHEET    2  DC 2 ALA D 222  ASP D 225 -1  O  ALA D 222   N  TYR D 114           
SHEET    1  DD 2 GLY D 146  PHE D 150  0                                        
SHEET    2  DD 2 ALA D 156  GLU D 161 -1  N  ILE D 157   O  GLU D 149           
CISPEP   1 HIS A   17    PRO A   18          0        11.98                     
CISPEP   2 HIS B   17    PRO B   18          0         8.52                     
CISPEP   3 HIS C   17    PRO C   18          0         6.92                     
CISPEP   4 HIS D   17    PRO D   18          0         7.05                     
SITE     1 AC1 14 THR A  42  LEU A  45  TYR A 113  GLY A 115                    
SITE     2 AC1 14 PHE A 118  HIS A 119  ARG A 219  VAL A 250                    
SITE     3 AC1 14 ALA A 251  GLU A 255  ARG A 259  GLN A 260                    
SITE     4 AC1 14 HOH A2084  HOH A2157                                          
SITE     1 AC2  7 PHE A 150  GLY A 154  LYS A 155  ALA A 156                    
SITE     2 AC2  7 SER A 213  VAL A 214  ILE A 216                               
SITE     1 AC3 13 SER B  41  THR B  42  LEU B  45  TYR B 113                    
SITE     2 AC3 13 GLY B 115  PHE B 118  HIS B 119  ARG B 219                    
SITE     3 AC3 13 VAL B 250  ALA B 251  GLN B 260  HOH B2055                    
SITE     4 AC3 13 HOH B2117                                                     
SITE     1 AC4  8 PHE B 150  GLY B 154  LYS B 155  ALA B 156                    
SITE     2 AC4  8 LEU B 212  SER B 213  VAL B 214  ILE B 216                    
SITE     1 AC5 15 SER C  41  THR C  42  LEU C  45  TYR C 113                    
SITE     2 AC5 15 GLY C 115  PHE C 118  HIS C 119  ARG C 219                    
SITE     3 AC5 15 VAL C 250  ALA C 251  GLU C 255  GLN C 260                    
SITE     4 AC5 15 HOH C2062  HOH C2065  HOH C2124                               
SITE     1 AC6  6 PHE C 150  GLY C 154  ALA C 156  SER C 213                    
SITE     2 AC6  6 VAL C 214  ILE C 216                                          
SITE     1 AC7 12 THR D  42  LEU D  45  TYR D 113  GLY D 115                    
SITE     2 AC7 12 PHE D 118  HIS D 119  ARG D 219  VAL D 250                    
SITE     3 AC7 12 ALA D 251  GLN D 260  HOH D2042  HOH D2079                    
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  4 HIS A 116  GLY A 218  ARG A 219  GLY A 220                    
SITE     1 BC1  4 HIS B 116  GLY B 218  ARG B 219  GLY B 220                    
SITE     1 BC2  4 HIS D 116  GLY D 218  ARG D 219  GLY D 220                    
SITE     1 BC3  4 HIS C 116  GLY C 218  ARG C 219  GLY C 220                    
SITE     1 BC4  7 LEU A 140  GLU A 243  GLY A 247  LYS A 249                    
SITE     2 BC4  7 TYR A 283  HOH A2027  HOH A2172                               
SITE     1 BC5  6 LEU D  66  LEU D  67  GLY D  70  ASN D  72                    
SITE     2 BC5  6 TRP D  73  HOH D2027                                          
SITE     1 BC6  6 GLU C 243  GLY C 247  LYS C 249  TYR C 283                    
SITE     2 BC6  6 ARG C 286  HOH C2143                                          
SITE     1 BC7  4 GLU D 243  LYS D 249  ARG D 286  HOH D2091                    
CRYST1   64.460  155.260  134.830  90.00  92.53  90.00 C 1 2 1       8          
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      0.015513  0.000000  0.000685        0.00000                         
SCALE2      0.000000  0.006441  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007424        0.00000                         
MTRIX1   1 -0.935900  0.011020 -0.352200       62.74000    1                    
MTRIX2   1 -0.004872 -0.999800 -0.018340      -35.89000    1                    
MTRIX3   1 -0.352400 -0.015450  0.935700       10.84000    1                    
MTRIX1   2  0.999500 -0.001456 -0.032480        5.14100    1                    
MTRIX2   2 -0.000964 -0.999900  0.015150      -17.38000    1                    
MTRIX3   2 -0.032500 -0.015110 -0.999400       68.02000    1                    
MTRIX1   3 -0.956400  0.010340  0.291800       40.39000    1                    
MTRIX2   3  0.013550  0.999900  0.008977      -20.73000    1                    
MTRIX3   3 -0.291700  0.012540 -0.956400       72.60000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system