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Database: PDB
Entry: 4ASY
LinkDB: 4ASY
Original site: 4ASY 
HEADER    TRANSFERASE                             03-MAY-12   4ASY              
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_PLASMID: PET23A                                    
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.S.ALPHEY,L.PIRRIE,L.S.TORRIE,M.GARDINER,A.SARKAR,R.BRENK,           
AUTHOR   2 N.J.WESTWOOD,D.GRAY,J.H.NAISMITH                                     
REVDAT   5   07-FEB-18 4ASY    1       JRNL                                     
REVDAT   4   05-JUL-17 4ASY    1       REMARK                                   
REVDAT   3   06-MAR-13 4ASY    1       JRNL                                     
REVDAT   2   21-NOV-12 4ASY    1       AUTHOR JRNL                              
REVDAT   1   31-OCT-12 4ASY    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.    2.30 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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 62887                          
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) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3145                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4019                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.99                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 207                          
REMARK   3   BIN FREE R VALUE                    : 0.3780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9164                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 156                                     
REMARK   3   SOLVENT ATOMS            : 396                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06100                                             
REMARK   3    B22 (A**2) : -0.36500                                             
REMARK   3    B33 (A**2) : 0.40000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.05500                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.337         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.247         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.158         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.335         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.901                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.867                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9524 ; 0.009 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  6450 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12930 ; 1.339 ; 2.000       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 15725 ; 0.889 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1167 ; 6.280 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   428 ;33.100 ;24.299       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1569 ;15.607 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    56 ;15.844 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1403 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10617 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1919 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2257 ; 0.221 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.210 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4675 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   259 ; 0.135 ; 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):  9524 ; 2.692 ; 4.639       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  6450 ; 0.714 ; 4.761       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12930 ; 4.096 ; 6.904       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3220 ; 6.824 ;14.198       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  7803 ; 5.710 ;22.684       
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 4ASY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-MAY-12.                  
REMARK 100 THE DEPOSITION ID IS D_1290052379.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-AUG-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   : 62887                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
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   (%): 56.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
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% BETA-MERCAPTOETHANOL                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       68.49000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13950 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -100.3 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 B     1                                                      
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    ALA A   9       72.47   -107.42                                   
REMARK 500    TYR A  31      -95.47     57.35                                   
REMARK 500    ASP A 117       30.41     70.09                                   
REMARK 500    ALA B   9       72.93   -104.03                                   
REMARK 500    TYR B  31      -91.17     65.34                                   
REMARK 500    ALA C   9       69.11   -109.42                                   
REMARK 500    TYR C  31      -97.20     61.91                                   
REMARK 500    ASP C 141       62.24   -118.32                                   
REMARK 500    GLU C 165       77.26   -119.39                                   
REMARK 500    ALA D   9       67.72   -107.48                                   
REMARK 500    TYR D  31     -100.04     53.49                                   
REMARK 500    ASP D 179     -163.01    -77.25                                   
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 N5Y 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 MES A 1296                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N5Y 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 MES B 1296                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N5Y C 1294                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES C 1296                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N5Y D 1294                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 1295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES D 1296                
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     
REMARK 900 RELATED ID: 4ASJ   RELATED DB: PDB                                   
REMARK 900 PSEUDOMONAS AERUGINOSA RMLA IN COMPLEX WITH ALLOSTERIC INHIBITOR     
REMARK 900 RELATED ID: 4ASP   RELATED DB: PDB                                   
REMARK 900 PSEUDOMONAS AERUGINOSA RMLA IN COMPLEX WITH ALLOSTERIC INHIBITOR     
DBREF  4ASY A    1   293  UNP    G3XCK4   G3XCK4_PSEAI     1    293             
DBREF  4ASY B    1   293  UNP    G3XCK4   G3XCK4_PSEAI     1    293             
DBREF  4ASY C    1   293  UNP    G3XCK4   G3XCK4_PSEAI     1    293             
DBREF  4ASY 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    N5Y  A1294      26                                                       
HET     CL  A1295       1                                                       
HET    MES  A1296      12                                                       
HET    N5Y  B1294      26                                                       
HET     CL  B1295       1                                                       
HET    MES  B1296      12                                                       
HET    N5Y  C1294      26                                                       
HET     CL  C1295       1                                                       
HET    MES  C1296      12                                                       
HET    N5Y  D1294      26                                                       
HET     CL  D1295       1                                                       
HET    MES  D1296      12                                                       
HETNAM     N5Y N-(6-AMINO-1-BENZYL-2,4-DIOXO-1,2,3,4-                           
HETNAM   2 N5Y  TETRAHYDROPYRIMIDIN-5-YL)-N-METHYLBENZAMIDE                     
HETNAM      CL CHLORIDE ION                                                     
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
FORMUL   5  N5Y    4(C19 H18 N4 O3)                                             
FORMUL   6   CL    4(CL 1-)                                                     
FORMUL   7  MES    4(C6 H13 N O4 S)                                             
FORMUL  17  HOH   *396(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  GLN A  127  1                                  11    
HELIX    8   8 ASP A  141  ARG A  144  5                                   4    
HELIX    9   9 GLN A  181  LEU A  189  1                                   9    
HELIX   10  10 GLU A  198  GLU A  208  1                                  11    
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 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  GLU B  290  1                                  13    
HELIX   30  30 SER C   24  LEU C   27  5                                   4    
HELIX   31  31 ILE C   36  ALA C   46  1                                  11    
HELIX   32  32 ASP C   59  GLY C   68  1                                  10    
HELIX   33  33 GLY C   70  GLY C   74  5                                   5    
HELIX   34  34 GLY C   87  ALA C   89  5                                   3    
HELIX   35  35 GLN C   90  GLY C   95  1                                   6    
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  LEU C  189  1                                   9    
HELIX   40  40 GLU C  198  GLU C  208  1                                  11    
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 ASN C  278  GLU C  290  1                                  13    
HELIX   45  45 SER D   24  LEU D   27  5                                   4    
HELIX   46  46 ILE D   36  ALA D   46  1                                  11    
HELIX   47  47 ASP D   59  GLY D   68  1                                  10    
HELIX   48  48 GLY D   70  GLY D   74  5                                   5    
HELIX   49  49 GLY D   87  ALA D   89  5                                   3    
HELIX   50  50 GLN D   90  GLY D   95  1                                   6    
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  GLU D  290  1                                  13    
SHEET    1  AA 7 ASP A  76  VAL A  81  0                                        
SHEET    2  AA 7 GLU A  50  SER A  55  1  O  ILE A  51   N  GLN A  78           
SHEET    3  AA 7 ARG A   3  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 ASN A 111  TYR A 114  0                                        
SHEET    2  AC 2 ALA A 222  ASP A 225 -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 ASN B 111  TYR B 114  0                                        
SHEET    2  BC 2 ALA B 222  ASP B 225 -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  ALA C   9  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 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 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         6.23                     
CISPEP   2 HIS B   17    PRO B   18          0         8.56                     
CISPEP   3 HIS C   17    PRO C   18          0         1.55                     
CISPEP   4 HIS D   17    PRO D   18          0         4.87                     
SITE     1 AC1 11 SER A  41  THR A  42  LEU A  45  TYR A 113                    
SITE     2 AC1 11 GLY A 115  VAL A 250  ALA A 251  GLU A 255                    
SITE     3 AC1 11 HOH A2010  HOH A2076  ARG B 219                               
SITE     1 AC2  2 GLY A 220  HIS B 116                                          
SITE     1 AC3  7 GLY A 154  LYS A 155  ALA A 156  LEU A 212                    
SITE     2 AC3  7 SER A 213  VAL A 214  ILE A 216                               
SITE     1 AC4 11 ARG A 219  SER B  41  THR B  42  LEU B  45                    
SITE     2 AC4 11 TYR B 113  TYR B 114  GLY B 115  VAL B 250                    
SITE     3 AC4 11 ALA B 251  GLU B 255  HOH B2091                               
SITE     1 AC5  3 HIS A 116  ARG B 219  GLY B 220                               
SITE     1 AC6  5 GLY B 154  LYS B 155  ALA B 156  VAL B 214                    
SITE     2 AC6  5 ILE B 216                                                     
SITE     1 AC7 12 SER C  41  THR C  42  LEU C  45  TYR C 113                    
SITE     2 AC7 12 TYR C 114  GLY C 115  VAL C 250  ALA C 251                    
SITE     3 AC7 12 GLU C 255  HOH C2041  HOH C2091  ARG D 219                    
SITE     1 AC8  4 ARG C 219  GLY C 220  HIS D 116  HOH D2034                    
SITE     1 AC9  6 PHE C 150  GLY C 154  ALA C 156  SER C 213                    
SITE     2 AC9  6 VAL C 214  ILE C 216                                          
SITE     1 BC1 11 ARG C 219  HOH C2081  LEU D  45  TYR D 113                    
SITE     2 BC1 11 TYR D 114  GLY D 115  VAL D 250  ALA D 251                    
SITE     3 BC1 11 GLU D 255  GLN D 260  HOH D2013                               
SITE     1 BC2  3 HIS C 116  ARG D 219  GLY D 220                               
SITE     1 BC3  6 GLY D 154  LYS D 155  ALA D 156  SER D 213                    
SITE     2 BC3  6 VAL D 214  ILE D 216                                          
CRYST1   73.990  136.980   75.190  90.00 103.28  90.00 P 1 21 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      0.013515  0.000000  0.003190        0.00000                         
SCALE2      0.000000  0.007300  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013665        0.00000                         
MTRIX1   1 -0.975200  0.199700 -0.095390        5.14700    1                    
MTRIX2   1  0.196500  0.582800 -0.788500        7.58600    1                    
MTRIX3   1 -0.101900 -0.787700 -0.607600       16.55000    1                    
MTRIX1   2  0.886800 -0.030920  0.461000       -9.57200    1                    
MTRIX2   2 -0.025420 -0.999500 -0.018140      -37.31000    1                    
MTRIX3   2  0.461400  0.004365 -0.887200       37.05000    1                    
MTRIX1   3 -0.916600 -0.163500 -0.364700        3.64000    1                    
MTRIX2   3 -0.200900 -0.600400  0.774100      -45.43000    1                    
MTRIX3   3 -0.345500  0.782800  0.517500       24.01000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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