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Database: PDB
Entry: 4ASJ
LinkDB: 4ASJ
Original site: 4ASJ 
HEADER    TRANSFERASE                             01-MAY-12   4ASJ              
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: 2.7.7.74;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 208964;                                              
SOURCE   4 STRAIN: PAO1;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET23A                                     
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.S.ALPHEY,L.PIRRIE,L.S.TORRIE,M.GARDINER,N.J.WESTWOOD,D.GRAY,        
AUTHOR   2 J.H.NAISMITH                                                         
REVDAT   5   07-FEB-18 4ASJ    1       JRNL                                     
REVDAT   4   05-JUL-17 4ASJ    1       REMARK                                   
REVDAT   3   06-MAR-13 4ASJ    1       JRNL                                     
REVDAT   2   21-NOV-12 4ASJ    1       AUTHOR JRNL                              
REVDAT   1   31-OCT-12 4ASJ    0                                                
JRNL        AUTH   M.S.ALPHEY,L.PIRRIE,L.S.TORRIE,W.A.BOULKEROUA,M.GARDINER,    
JRNL        AUTH 2 A.SARKAR,M.MARINGER,W.OEHLMANN,R.BRENK,M.S.SCHERMAN,         
JRNL        AUTH 3 M.MCNEIL,M.REJZEK,R.A.FIELD,M.SINGH,D.GRAY,N.J.WESTWOOD,     
JRNL        AUTH 4 J.H.NAISMITH                                                 
JRNL        TITL   ALLOSTERIC COMPETITIVE INHIBITORS OF THE GLUCOSE-1-PHOSPHATE 
JRNL        TITL 2 THYMIDYLYLTRANSFERASE (RMLA) FROM PSEUDOMONAS AERUGINOSA.    
JRNL        REF    ACS CHEM. BIOL.               V.   8   387 2013              
JRNL        REFN                   ESSN 1554-8937                               
JRNL        PMID   23138692                                                     
JRNL        DOI    10.1021/CB300426U                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 55248                          
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) : 0.242                           
REMARK   3   R VALUE            (WORKING SET) : 0.238                           
REMARK   3   FREE R VALUE                     : 0.318                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.160                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2799                            
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) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.31                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3281                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 76.23                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4880                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 164                          
REMARK   3   BIN FREE R VALUE                    : 0.5860                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9122                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 122                                     
REMARK   3   SOLVENT ATOMS            : 373                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.14800                                              
REMARK   3    B22 (A**2) : -0.81800                                             
REMARK   3    B33 (A**2) : -0.35600                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.34100                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.469         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.324         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.236         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.351         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.889                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.797                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9446 ; 0.012 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  6360 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12838 ; 1.580 ; 1.996       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 15498 ; 0.949 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1162 ; 6.776 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   428 ;34.169 ;24.299       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1552 ;16.303 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    56 ;16.911 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1394 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10574 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1914 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2321 ; 0.223 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    99 ; 0.178 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4584 ; 0.186 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   280 ; 0.160 ; 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):  9444 ; 2.350 ; 3.789       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  6359 ; 0.627 ; 3.888       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12838 ; 3.485 ; 5.650       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3198 ; 5.131 ;11.615       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  7754 ; 5.336 ;18.431       
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 4ASJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-MAY-12.                  
REMARK 100 THE DEPOSITION ID IS D_1290052317.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUL-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56889                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.220                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.140                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.7                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.700                              
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 4ARW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 4% PEG 6000, 0.1 M MES PH6, 0.05 M       
REMARK 280  MGCL2, 0.1 M NABR, 1% B-ME                                          
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       32.08500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       77.28000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       32.08500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       77.28000            
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, 3, 4                                              
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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       58.99993            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      134.58073            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.2 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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       64.17000            
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.6 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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       64.17000            
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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       58.99993            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      134.58073            
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 B2042  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C2029  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH D2027  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH D2059  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     MET A     1                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     MET C     1                                                      
REMARK 465     MET D     1                                                      
REMARK 465     LYS D     2                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS B 138   CG    HIS B 138   CD2     0.055                       
REMARK 500    HIS C 119   CG    HIS C 119   CD2     0.055                       
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    TYR A  31      -87.74     61.76                                   
REMARK 500    ARG A 128       99.70    -62.27                                   
REMARK 500    ASP A 141       67.59   -118.16                                   
REMARK 500    LYS A 261       39.30     77.99                                   
REMARK 500    ALA B   9       64.72   -118.91                                   
REMARK 500    ILE B  23      149.06    177.43                                   
REMARK 500    TYR B  31      -90.45     59.96                                   
REMARK 500    ARG B 128       95.24    -61.68                                   
REMARK 500    ALA C   9       58.46   -118.63                                   
REMARK 500    TYR C  31      -91.82     62.66                                   
REMARK 500    ALA D   9       70.01   -106.51                                   
REMARK 500    SER D  24      135.59    -39.70                                   
REMARK 500    TYR D  31      -91.54     52.88                                   
REMARK 500    ASP D 141       67.67   -119.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D2080        DISTANCE =  5.81 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N6A A 1294                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1296                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N6A B 1294                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N6A C 1294                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 1296                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N6A D 1294                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 1295                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ARW   RELATED DB: PDB                                   
REMARK 900 PSEUDOMONAS AERUGINOSA RMLA IN COMPLEX WITH ALLOSTERIC INHIBITOR     
REMARK 900 RELATED ID: 4AS6   RELATED DB: PDB                                   
REMARK 900 PSEUDOMONAS AERUGINOSA RMLA IN COMPLEX WITH ALLOSTERIC INHIBITOR     
DBREF  4ASJ A    1   293  UNP    G3XCK4   G3XCK4_PSEAI     1    293             
DBREF  4ASJ B    1   293  UNP    G3XCK4   G3XCK4_PSEAI     1    293             
DBREF  4ASJ C    1   293  UNP    G3XCK4   G3XCK4_PSEAI     1    293             
DBREF  4ASJ D    1   293  UNP    G3XCK4   G3XCK4_PSEAI     1    293             
SEQRES   1 A  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 A  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 A  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 A  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 A  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 A  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 A  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 A  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 A  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 A  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 A  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 A  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 A  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 A  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 A  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 A  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 A  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 A  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 A  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 A  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 A  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 A  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 A  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 B  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 B  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 B  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 B  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 B  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 B  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 B  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 B  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 B  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 B  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 B  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 B  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 B  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 B  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 B  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 B  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 B  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 B  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 B  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 B  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 B  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 B  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 B  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 C  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 C  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 C  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 C  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 C  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 C  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 C  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 C  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 C  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 C  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 C  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 C  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 C  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 C  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 C  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 C  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 C  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 C  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 C  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 C  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 C  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 C  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 C  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 D  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 D  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 D  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 D  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 D  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 D  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 D  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 D  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 D  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 D  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 D  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 D  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 D  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 D  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 D  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 D  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 D  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 D  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 D  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 D  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 D  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 D  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 D  293  LEU LEU THR GLU THR VAL TYR                                  
HET    N6A  A1294      27                                                       
HET     CL  A1295       1                                                       
HET    PO4  A1296       5                                                       
HET    N6A  B1294      27                                                       
HET     CL  B1295       1                                                       
HET    N6A  C1294      27                                                       
HET     CL  C1295       1                                                       
HET    PO4  C1296       5                                                       
HET    N6A  D1294      27                                                       
HET     CL  D1295       1                                                       
HETNAM     N6A N-(6-AMINO-1-BENZYL-2,4-DIOXO-1,2,3,4-                           
HETNAM   2 N6A  TETRAHYDROPYRIMIDIN-5-YL)-N-METHYLBENZENESULFONAMIDE            
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   5  N6A    4(C18 H18 N4 O4 S)                                           
FORMUL   6   CL    4(CL 1-)                                                     
FORMUL   7  PO4    2(O4 P 3-)                                                   
FORMUL  15  HOH   *373(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  GLY A  210  1                                  13    
HELIX   11  11 THR A  228  GLY A  247  1                                  20    
HELIX   12  12 CYS A  252  LYS A  261  1                                  10    
HELIX   13  13 ASP A  264  ALA A  273  1                                  10    
HELIX   14  14 ASN A  278  LEU A  287  1                                  10    
HELIX   15  15 SER B   24  LEU B   27  5                                   4    
HELIX   16  16 ILE B   36  ALA B   46  1                                  11    
HELIX   17  17 ASP B   59  GLY B   68  1                                  10    
HELIX   18  18 GLY B   70  GLY B   74  5                                   5    
HELIX   19  19 ALA B   89  GLY B   95  1                                   7    
HELIX   20  20 GLY B   95  GLY B  100  1                                   6    
HELIX   21  21 ASP B  117  ARG B  128  1                                  12    
HELIX   22  22 ASP B  141  ARG B  144  5                                   4    
HELIX   23  23 GLN B  181  ASP B  188  1                                   8    
HELIX   24  24 GLU B  198  ARG B  209  1                                  12    
HELIX   25  25 THR B  228  GLY B  247  1                                  20    
HELIX   26  26 CYS B  252  GLN B  260  1                                   9    
HELIX   27  27 ASP B  264  ALA B  273  1                                  10    
HELIX   28  28 PRO B  274  ALA B  276  5                                   3    
HELIX   29  29 ASN B  278  LEU B  287  1                                  10    
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 GLY C   87  ALA C   89  5                                   3    
HELIX   36  36 GLN C   90  GLY C   95  1                                   6    
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  ASP C  188  1                                   8    
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 PRO C  274  ALA C  276  5                                   3    
HELIX   46  46 ASN C  278  LEU C  287  1                                  10    
HELIX   47  47 PRO D   18  ILE D   23  1                                   6    
HELIX   48  48 SER D   24  LEU D   27  5                                   4    
HELIX   49  49 ILE D   36  ALA D   46  1                                  11    
HELIX   50  50 ASP D   59  GLY D   68  1                                  10    
HELIX   51  51 GLY D   70  GLY D   74  5                                   5    
HELIX   52  52 GLY D   87  ALA D   89  5                                   3    
HELIX   53  53 GLN D   90  GLY D   95  1                                   6    
HELIX   54  54 GLY D   95  GLY D  100  1                                   6    
HELIX   55  55 ASP D  117  ARG D  128  1                                  12    
HELIX   56  56 ASP D  141  ARG D  144  5                                   4    
HELIX   57  57 GLN D  181  ASP D  188  1                                   8    
HELIX   58  58 GLU D  198  ARG D  209  1                                  12    
HELIX   59  59 THR D  228  GLY D  247  1                                  20    
HELIX   60  60 CYS D  252  GLN D  260  1                                   9    
HELIX   61  61 ASP D  264  ALA D  273  1                                  10    
HELIX   62  62 PRO D  274  ALA D  276  5                                   3    
HELIX   63  63 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 5 ASP B  76  VAL B  81  0                                        
SHEET    2  BA 5 GLU B  50  SER B  55  1  O  ILE B  51   N  GLN B  78           
SHEET    3  BA 5 LYS B   4  ALA B   9  1  O  GLY B   5   N  LEU B  52           
SHEET    4  BA 5 SER B 104  LEU B 108  1  O  ALA B 105   N  ILE B   6           
SHEET    5  BA 5 LEU B 175  TYR B 178 -1  O  TYR B 176   N  LEU B 106           
SHEET    1  BB 2 PRO B  29  VAL B  30  0                                        
SHEET    2  BB 2 LYS B  33  PRO B  34 -1  O  LYS B  33   N  VAL B  30           
SHEET    1  BC 2 LEU B 112  TYR B 114  0                                        
SHEET    2  BC 2 ALA B 222  LEU B 224 -1  O  ALA B 222   N  TYR B 114           
SHEET    1  BD 3 TYR B 170  VAL B 172  0                                        
SHEET    2  BD 3 ALA B 132  HIS B 138 -1  O  TYR B 137   N  ALA B 171           
SHEET    3  BD 3 LEU B 212  ILE B 216  1  O  SER B 213   N  VAL B 134           
SHEET    1  BE 2 GLY B 146  PHE B 150  0                                        
SHEET    2  BE 2 ALA B 156  GLU B 161 -1  N  ILE B 157   O  GLU B 149           
SHEET    1  CA 7 ASP C  76  VAL C  81  0                                        
SHEET    2  CA 7 GLU C  50  SER C  55  1  O  ILE C  51   N  GLN C  78           
SHEET    3  CA 7 ARG C   3  LEU C   8  1  O  GLY C   5   N  LEU C  52           
SHEET    4  CA 7 LEU C 103  LEU C 108  1  O  LEU C 103   N  LYS C   4           
SHEET    5  CA 7 TYR C 170  TYR C 178 -1  O  GLY C 174   N  LEU C 108           
SHEET    6  CA 7 ALA C 132  HIS C 138 -1  O  SER C 133   N  PHE C 177           
SHEET    7  CA 7 LEU C 212  ILE C 216  1  O  SER C 213   N  VAL C 134           
SHEET    1  CB 2 PRO C  29  VAL C  30  0                                        
SHEET    2  CB 2 LYS C  33  PRO C  34 -1  O  LYS C  33   N  VAL C  30           
SHEET    1  CC 2 ASN C 111  TYR C 114  0                                        
SHEET    2  CC 2 ALA C 222  ASP C 225 -1  O  ALA C 222   N  TYR C 114           
SHEET    1  CD 2 GLY C 146  PHE C 150  0                                        
SHEET    2  CD 2 ALA C 156  GLU C 161 -1  N  ILE C 157   O  GLU C 149           
SHEET    1  DA 7 ASP D  76  VAL D  81  0                                        
SHEET    2  DA 7 GLU D  50  SER D  55  1  O  ILE D  51   N  GLN D  78           
SHEET    3  DA 7 LYS D   4  LEU D   8  1  O  GLY D   5   N  LEU D  52           
SHEET    4  DA 7 SER D 104  LEU D 108  1  O  ALA D 105   N  ILE D   6           
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         7.66                     
CISPEP   2 HIS B   17    PRO B   18          0         3.98                     
CISPEP   3 HIS C   17    PRO C   18          0         4.96                     
CISPEP   4 HIS D   17    PRO D   18          0        -1.26                     
SITE     1 AC1 14 SER A  41  LEU A  45  TYR A 113  GLY A 115                    
SITE     2 AC1 14 PHE A 118  ARG A 219  VAL A 250  ALA A 251                    
SITE     3 AC1 14 GLU A 255  ILE A 256  HOH A2035  HOH A2037                    
SITE     4 AC1 14 HOH A2083  HOH A2097                                          
SITE     1 AC2  3 HIS A 116  ARG A 219  GLY A 220                               
SITE     1 AC3  5 GLY A 154  LYS A 155  ALA A 156  LEU A 212                    
SITE     2 AC3  5 VAL A 214                                                     
SITE     1 AC4 15 SER B  41  THR B  42  LEU B  45  TYR B 113                    
SITE     2 AC4 15 GLY B 115  PHE B 118  ARG B 219  LYS B 249                    
SITE     3 AC4 15 VAL B 250  ALA B 251  GLU B 255  ILE B 256                    
SITE     4 AC4 15 ARG B 259  HOH B2041  HOH B2045                               
SITE     1 AC5  4 HIS B 116  GLY B 218  ARG B 219  GLY B 220                    
SITE     1 AC6 16 SER C  41  LEU C  45  TYR C 113  GLY C 115                    
SITE     2 AC6 16 PHE C 118  HIS C 119  ARG C 219  LYS C 249                    
SITE     3 AC6 16 VAL C 250  ALA C 251  GLU C 255  ILE C 256                    
SITE     4 AC6 16 ARG C 259  HOH C2028  HOH C2030  HOH C2076                    
SITE     1 AC7  3 HIS C 116  GLY C 218  GLY C 220                               
SITE     1 AC8  3 ALA C 156  LEU C 212  VAL C 214                               
SITE     1 AC9 14 SER D  41  LEU D  45  TYR D 113  GLY D 115                    
SITE     2 AC9 14 PHE D 118  ARG D 219  LYS D 249  VAL D 250                    
SITE     3 AC9 14 ALA D 251  GLU D 255  ILE D 256  HOH D2025                    
SITE     4 AC9 14 HOH D2026  HOH D2060                                          
SITE     1 BC1  2 HIS D 116  GLY D 220                                          
CRYST1   64.170  154.560  134.680  90.00  92.20  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      0.015584  0.000000  0.000599        0.00000                         
SCALE2      0.000000  0.006470  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007430        0.00000                         
MTRIX1   1 -0.935700  0.008397 -0.352600       62.39000    1                    
MTRIX2   1 -0.004174 -0.999900 -0.012730      -36.19000    1                    
MTRIX3   1 -0.352700 -0.010440  0.935700       10.98000    1                    
MTRIX1   2  0.999100 -0.005878 -0.042880        5.41200    1                    
MTRIX2   2 -0.005281 -0.999900  0.014020      -17.45000    1                    
MTRIX3   2 -0.042960 -0.013780 -0.999000       68.20000    1                    
MTRIX1   3 -0.953700  0.008025  0.300800       39.85000    1                    
MTRIX2   3  0.011560  0.999900  0.009984      -20.63000    1                    
MTRIX3   3 -0.300600  0.013000 -0.953600       72.72000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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