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Database: PDB
Entry: 4ARW
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Original site: 4ARW 
HEADER    TRANSFERASE                             26-APR-12   4ARW              
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   7   04-MAR-20 4ARW    1       REMARK                                   
REVDAT   6   07-FEB-18 4ARW    1       JRNL                                     
REVDAT   5   05-JUL-17 4ARW    1       REMARK                                   
REVDAT   4   06-MAR-13 4ARW    1       JRNL                                     
REVDAT   3   19-DEC-12 4ARW    1       COMPND SOURCE REMARK SEQADV              
REVDAT   3 2                   1       SEQRES DBREF  ATOM   TER                 
REVDAT   3 3                   1       HETATM CONECT MASTER                     
REVDAT   2   21-NOV-12 4ARW    1       AUTHOR JRNL                              
REVDAT   1   31-OCT-12 4ARW    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.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.82                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 62911                          
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) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.140                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3192                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3530                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 198                          
REMARK   3   BIN FREE R VALUE                    : 0.2740                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9116                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 161                                     
REMARK   3   SOLVENT ATOMS            : 547                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.80000                                              
REMARK   3    B22 (A**2) : -0.38400                                             
REMARK   3    B33 (A**2) : -0.44700                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.38400                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.277         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.192         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.130         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.124         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9500 ; 0.008 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  6417 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12904 ; 1.228 ; 1.997       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 15532 ; 0.864 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1166 ; 6.005 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   433 ;34.233 ;24.388       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1557 ;14.338 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    54 ;15.373 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1403 ; 0.066 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10568 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1874 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2300 ; 0.215 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):   106 ; 0.165 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4610 ; 0.178 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   229 ; 0.142 ; 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):  9499 ; 2.020 ; 4.057       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  6416 ; 0.509 ; 4.171       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12900 ; 3.173 ; 6.039       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3210 ; 5.396 ;12.430       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  7698 ; 5.071 ;19.772       
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 4ARW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-APR-12.                  
REMARK 100 THE DEPOSITION ID IS D_1290052177.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-APR-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   : 62911                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
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 1FZW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 4% PEG6000, 0.1M MES PH6, 0.05M MGCL2,   
REMARK 280  0.1M 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       31.99500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       76.88000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       31.99500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       76.88000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       63.99000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       58.53929            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      134.53963            
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 A2059  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B2058  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C2044  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH D2062  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B   193                                                      
REMARK 465     ARG B   194                                                      
REMARK 465     HIS C    -8                                                      
REMARK 465     HIS C    -7                                                      
REMARK 465     HIS C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     ALA C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     LYS C     2                                                      
REMARK 465     PRO C   193                                                      
REMARK 465     ARG C   194                                                      
REMARK 465     HIS D    -8                                                      
REMARK 465     HIS D    -7                                                      
REMARK 465     HIS D    -6                                                      
REMARK 465     HIS D    -5                                                      
REMARK 465     HIS D    -4                                                      
REMARK 465     HIS D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     ALA D     0                                                      
REMARK 465     MET D     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    TYR A  31      -91.81     61.50                                   
REMARK 500    ARG A 128       98.89    -68.08                                   
REMARK 500    TYR B  31      -82.47     61.48                                   
REMARK 500    PRO B  85       76.85    -65.18                                   
REMARK 500    TYR C  31      -85.40     56.94                                   
REMARK 500    ALA C 273      -71.10    -37.02                                   
REMARK 500    ALA D   9       59.16   -117.63                                   
REMARK 500    TYR D  31      -90.12     58.24                                   
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 HNR A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 450                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HNR B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 450                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HNR C 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES C 450                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HNR D 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES D 450                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 1294                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1294                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1294                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1294                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 1295                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1295                
DBREF  4ARW A    1   293  UNP    G3XCK4   G3XCK4_PSEAI     1    293             
DBREF  4ARW B    1   293  UNP    G3XCK4   G3XCK4_PSEAI     1    293             
DBREF  4ARW C    1   293  UNP    G3XCK4   G3XCK4_PSEAI     1    293             
DBREF  4ARW D    1   293  UNP    G3XCK4   G3XCK4_PSEAI     1    293             
SEQADV 4ARW HIS A   -8  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS A   -7  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS A   -6  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS A   -5  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS A   -4  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS A   -3  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW GLY A   -2  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW SER A   -1  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW ALA A    0  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS B   -8  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS B   -7  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS B   -6  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS B   -5  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS B   -4  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS B   -3  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW GLY B   -2  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW SER B   -1  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW ALA B    0  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS C   -8  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS C   -7  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS C   -6  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS C   -5  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS C   -4  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS C   -3  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW GLY C   -2  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW SER C   -1  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW ALA C    0  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS D   -8  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS D   -7  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS D   -6  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS D   -5  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS D   -4  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW HIS D   -3  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW GLY D   -2  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW SER D   -1  UNP  G3XCK4              EXPRESSION TAG                 
SEQADV 4ARW ALA D    0  UNP  G3XCK4              EXPRESSION TAG                 
SEQRES   1 A  302  HIS HIS HIS HIS HIS HIS GLY SER ALA MET LYS ARG LYS          
SEQRES   2 A  302  GLY ILE ILE LEU ALA GLY GLY SER GLY THR ARG LEU HIS          
SEQRES   3 A  302  PRO ALA THR LEU ALA ILE SER LYS GLN LEU LEU PRO VAL          
SEQRES   4 A  302  TYR ASP LYS PRO MET ILE TYR TYR PRO LEU SER THR LEU          
SEQRES   5 A  302  MET LEU ALA GLY ILE ARG GLU ILE LEU ILE ILE SER THR          
SEQRES   6 A  302  PRO GLN ASP THR PRO ARG PHE GLN GLN LEU LEU GLY ASP          
SEQRES   7 A  302  GLY SER ASN TRP GLY LEU ASP LEU GLN TYR ALA VAL GLN          
SEQRES   8 A  302  PRO SER PRO ASP GLY LEU ALA GLN ALA PHE LEU ILE GLY          
SEQRES   9 A  302  GLU SER PHE ILE GLY ASN ASP LEU SER ALA LEU VAL LEU          
SEQRES  10 A  302  GLY ASP ASN LEU TYR TYR GLY HIS ASP PHE HIS GLU LEU          
SEQRES  11 A  302  LEU GLY SER ALA SER GLN ARG GLN THR GLY ALA SER VAL          
SEQRES  12 A  302  PHE ALA TYR HIS VAL LEU ASP PRO GLU ARG TYR GLY VAL          
SEQRES  13 A  302  VAL GLU PHE ASP GLN GLY GLY LYS ALA ILE SER LEU GLU          
SEQRES  14 A  302  GLU LYS PRO LEU GLU PRO LYS SER ASN TYR ALA VAL THR          
SEQRES  15 A  302  GLY LEU TYR PHE TYR ASP GLN GLN VAL VAL ASP ILE ALA          
SEQRES  16 A  302  ARG ASP LEU LYS PRO SER PRO ARG GLY GLU LEU GLU ILE          
SEQRES  17 A  302  THR ASP VAL ASN ARG ALA TYR LEU GLU ARG GLY GLN LEU          
SEQRES  18 A  302  SER VAL GLU ILE MET GLY ARG GLY TYR ALA TRP LEU ASP          
SEQRES  19 A  302  THR GLY THR HIS ASP SER LEU LEU GLU ALA GLY GLN PHE          
SEQRES  20 A  302  ILE ALA THR LEU GLU ASN ARG GLN GLY LEU LYS VAL ALA          
SEQRES  21 A  302  CYS PRO GLU GLU ILE ALA TYR ARG GLN LYS TRP ILE ASP          
SEQRES  22 A  302  ALA ALA GLN LEU GLU LYS LEU ALA ALA PRO LEU ALA LYS          
SEQRES  23 A  302  ASN GLY TYR GLY GLN TYR LEU LYS ARG LEU LEU THR GLU          
SEQRES  24 A  302  THR VAL TYR                                                  
SEQRES   1 B  302  HIS HIS HIS HIS HIS HIS GLY SER ALA MET LYS ARG LYS          
SEQRES   2 B  302  GLY ILE ILE LEU ALA GLY GLY SER GLY THR ARG LEU HIS          
SEQRES   3 B  302  PRO ALA THR LEU ALA ILE SER LYS GLN LEU LEU PRO VAL          
SEQRES   4 B  302  TYR ASP LYS PRO MET ILE TYR TYR PRO LEU SER THR LEU          
SEQRES   5 B  302  MET LEU ALA GLY ILE ARG GLU ILE LEU ILE ILE SER THR          
SEQRES   6 B  302  PRO GLN ASP THR PRO ARG PHE GLN GLN LEU LEU GLY ASP          
SEQRES   7 B  302  GLY SER ASN TRP GLY LEU ASP LEU GLN TYR ALA VAL GLN          
SEQRES   8 B  302  PRO SER PRO ASP GLY LEU ALA GLN ALA PHE LEU ILE GLY          
SEQRES   9 B  302  GLU SER PHE ILE GLY ASN ASP LEU SER ALA LEU VAL LEU          
SEQRES  10 B  302  GLY ASP ASN LEU TYR TYR GLY HIS ASP PHE HIS GLU LEU          
SEQRES  11 B  302  LEU GLY SER ALA SER GLN ARG GLN THR GLY ALA SER VAL          
SEQRES  12 B  302  PHE ALA TYR HIS VAL LEU ASP PRO GLU ARG TYR GLY VAL          
SEQRES  13 B  302  VAL GLU PHE ASP GLN GLY GLY LYS ALA ILE SER LEU GLU          
SEQRES  14 B  302  GLU LYS PRO LEU GLU PRO LYS SER ASN TYR ALA VAL THR          
SEQRES  15 B  302  GLY LEU TYR PHE TYR ASP GLN GLN VAL VAL ASP ILE ALA          
SEQRES  16 B  302  ARG ASP LEU LYS PRO SER PRO ARG GLY GLU LEU GLU ILE          
SEQRES  17 B  302  THR ASP VAL ASN ARG ALA TYR LEU GLU ARG GLY GLN LEU          
SEQRES  18 B  302  SER VAL GLU ILE MET GLY ARG GLY TYR ALA TRP LEU ASP          
SEQRES  19 B  302  THR GLY THR HIS ASP SER LEU LEU GLU ALA GLY GLN PHE          
SEQRES  20 B  302  ILE ALA THR LEU GLU ASN ARG GLN GLY LEU LYS VAL ALA          
SEQRES  21 B  302  CYS PRO GLU GLU ILE ALA TYR ARG GLN LYS TRP ILE ASP          
SEQRES  22 B  302  ALA ALA GLN LEU GLU LYS LEU ALA ALA PRO LEU ALA LYS          
SEQRES  23 B  302  ASN GLY TYR GLY GLN TYR LEU LYS ARG LEU LEU THR GLU          
SEQRES  24 B  302  THR VAL TYR                                                  
SEQRES   1 C  302  HIS HIS HIS HIS HIS HIS GLY SER ALA MET LYS ARG LYS          
SEQRES   2 C  302  GLY ILE ILE LEU ALA GLY GLY SER GLY THR ARG LEU HIS          
SEQRES   3 C  302  PRO ALA THR LEU ALA ILE SER LYS GLN LEU LEU PRO VAL          
SEQRES   4 C  302  TYR ASP LYS PRO MET ILE TYR TYR PRO LEU SER THR LEU          
SEQRES   5 C  302  MET LEU ALA GLY ILE ARG GLU ILE LEU ILE ILE SER THR          
SEQRES   6 C  302  PRO GLN ASP THR PRO ARG PHE GLN GLN LEU LEU GLY ASP          
SEQRES   7 C  302  GLY SER ASN TRP GLY LEU ASP LEU GLN TYR ALA VAL GLN          
SEQRES   8 C  302  PRO SER PRO ASP GLY LEU ALA GLN ALA PHE LEU ILE GLY          
SEQRES   9 C  302  GLU SER PHE ILE GLY ASN ASP LEU SER ALA LEU VAL LEU          
SEQRES  10 C  302  GLY ASP ASN LEU TYR TYR GLY HIS ASP PHE HIS GLU LEU          
SEQRES  11 C  302  LEU GLY SER ALA SER GLN ARG GLN THR GLY ALA SER VAL          
SEQRES  12 C  302  PHE ALA TYR HIS VAL LEU ASP PRO GLU ARG TYR GLY VAL          
SEQRES  13 C  302  VAL GLU PHE ASP GLN GLY GLY LYS ALA ILE SER LEU GLU          
SEQRES  14 C  302  GLU LYS PRO LEU GLU PRO LYS SER ASN TYR ALA VAL THR          
SEQRES  15 C  302  GLY LEU TYR PHE TYR ASP GLN GLN VAL VAL ASP ILE ALA          
SEQRES  16 C  302  ARG ASP LEU LYS PRO SER PRO ARG GLY GLU LEU GLU ILE          
SEQRES  17 C  302  THR ASP VAL ASN ARG ALA TYR LEU GLU ARG GLY GLN LEU          
SEQRES  18 C  302  SER VAL GLU ILE MET GLY ARG GLY TYR ALA TRP LEU ASP          
SEQRES  19 C  302  THR GLY THR HIS ASP SER LEU LEU GLU ALA GLY GLN PHE          
SEQRES  20 C  302  ILE ALA THR LEU GLU ASN ARG GLN GLY LEU LYS VAL ALA          
SEQRES  21 C  302  CYS PRO GLU GLU ILE ALA TYR ARG GLN LYS TRP ILE ASP          
SEQRES  22 C  302  ALA ALA GLN LEU GLU LYS LEU ALA ALA PRO LEU ALA LYS          
SEQRES  23 C  302  ASN GLY TYR GLY GLN TYR LEU LYS ARG LEU LEU THR GLU          
SEQRES  24 C  302  THR VAL TYR                                                  
SEQRES   1 D  302  HIS HIS HIS HIS HIS HIS GLY SER ALA MET LYS ARG LYS          
SEQRES   2 D  302  GLY ILE ILE LEU ALA GLY GLY SER GLY THR ARG LEU HIS          
SEQRES   3 D  302  PRO ALA THR LEU ALA ILE SER LYS GLN LEU LEU PRO VAL          
SEQRES   4 D  302  TYR ASP LYS PRO MET ILE TYR TYR PRO LEU SER THR LEU          
SEQRES   5 D  302  MET LEU ALA GLY ILE ARG GLU ILE LEU ILE ILE SER THR          
SEQRES   6 D  302  PRO GLN ASP THR PRO ARG PHE GLN GLN LEU LEU GLY ASP          
SEQRES   7 D  302  GLY SER ASN TRP GLY LEU ASP LEU GLN TYR ALA VAL GLN          
SEQRES   8 D  302  PRO SER PRO ASP GLY LEU ALA GLN ALA PHE LEU ILE GLY          
SEQRES   9 D  302  GLU SER PHE ILE GLY ASN ASP LEU SER ALA LEU VAL LEU          
SEQRES  10 D  302  GLY ASP ASN LEU TYR TYR GLY HIS ASP PHE HIS GLU LEU          
SEQRES  11 D  302  LEU GLY SER ALA SER GLN ARG GLN THR GLY ALA SER VAL          
SEQRES  12 D  302  PHE ALA TYR HIS VAL LEU ASP PRO GLU ARG TYR GLY VAL          
SEQRES  13 D  302  VAL GLU PHE ASP GLN GLY GLY LYS ALA ILE SER LEU GLU          
SEQRES  14 D  302  GLU LYS PRO LEU GLU PRO LYS SER ASN TYR ALA VAL THR          
SEQRES  15 D  302  GLY LEU TYR PHE TYR ASP GLN GLN VAL VAL ASP ILE ALA          
SEQRES  16 D  302  ARG ASP LEU LYS PRO SER PRO ARG GLY GLU LEU GLU ILE          
SEQRES  17 D  302  THR ASP VAL ASN ARG ALA TYR LEU GLU ARG GLY GLN LEU          
SEQRES  18 D  302  SER VAL GLU ILE MET GLY ARG GLY TYR ALA TRP LEU ASP          
SEQRES  19 D  302  THR GLY THR HIS ASP SER LEU LEU GLU ALA GLY GLN PHE          
SEQRES  20 D  302  ILE ALA THR LEU GLU ASN ARG GLN GLY LEU LYS VAL ALA          
SEQRES  21 D  302  CYS PRO GLU GLU ILE ALA TYR ARG GLN LYS TRP ILE ASP          
SEQRES  22 D  302  ALA ALA GLN LEU GLU LYS LEU ALA ALA PRO LEU ALA LYS          
SEQRES  23 D  302  ASN GLY TYR GLY GLN TYR LEU LYS ARG LEU LEU THR GLU          
SEQRES  24 D  302  THR VAL TYR                                                  
HET    HNR  A 400      24                                                       
HET    MES  A 450      12                                                       
HET     CL  A1294       1                                                       
HET    HNR  B 400      24                                                       
HET    MES  B 450      12                                                       
HET     CL  B1294       1                                                       
HET    GOL  B1295       6                                                       
HET    HNR  C 400      24                                                       
HET    MES  C 450      12                                                       
HET     CL  C1294       1                                                       
HET     CL  C1295       1                                                       
HET    HNR  D 400      24                                                       
HET    MES  D 450      12                                                       
HET     CL  D1294       1                                                       
HET    GOL  D1295       6                                                       
HETNAM     HNR N-(6-AMINO-1-BUTYL-2,4-DIOXO-1,2,3,4-                            
HETNAM   2 HNR  TETRAHYDROPYRIMIDIN-5-YL)-N-METHYL-BENZENESULFONAMIDE           
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  HNR    4(C15 H20 N4 O4 S)                                           
FORMUL   6  MES    4(C6 H13 N O4 S)                                             
FORMUL   7   CL    5(CL 1-)                                                     
FORMUL  11  GOL    2(C3 H8 O3)                                                  
FORMUL  20  HOH   *547(H2 O)                                                    
HELIX    1   1 SER A   24  LEU A   27  5                                   4    
HELIX    2   2 ILE A   36  ALA A   46  1                                  11    
HELIX    3   3 ASP A   59  GLY A   68  1                                  10    
HELIX    4   4 GLY A   70  GLY A   74  5                                   5    
HELIX    5   5 GLY A   87  ALA A   89  5                                   3    
HELIX    6   6 GLN A   90  GLY A   95  1                                   6    
HELIX    7   7 GLY A   95  GLY A  100  1                                   6    
HELIX    8   8 ASP A  117  ARG A  128  1                                  12    
HELIX    9   9 ASP A  141  ARG A  144  5                                   4    
HELIX   10  10 GLN A  181  ASP A  188  1                                   8    
HELIX   11  11 GLU A  198  ARG A  209  1                                  12    
HELIX   12  12 THR A  228  GLY A  247  1                                  20    
HELIX   13  13 CYS A  252  GLN A  260  1                                   9    
HELIX   14  14 ASP A  264  ALA A  273  1                                  10    
HELIX   15  15 PRO A  274  ALA A  276  5                                   3    
HELIX   16  16 ASN A  278  LEU A  287  1                                  10    
HELIX   17  17 PRO B   18  ILE B   23  1                                   6    
HELIX   18  18 SER B   24  LEU B   27  5                                   4    
HELIX   19  19 ILE B   36  ALA B   46  1                                  11    
HELIX   20  20 ASP B   59  GLY B   68  1                                  10    
HELIX   21  21 GLY B   70  GLY B   74  5                                   5    
HELIX   22  22 ALA B   89  GLY B   95  1                                   7    
HELIX   23  23 GLY B   95  GLY B  100  1                                   6    
HELIX   24  24 ASP B  117  ARG B  128  1                                  12    
HELIX   25  25 ASP B  141  ARG B  144  5                                   4    
HELIX   26  26 GLN B  181  ASP B  188  1                                   8    
HELIX   27  27 GLU B  198  ARG B  209  1                                  12    
HELIX   28  28 THR B  228  GLY B  247  1                                  20    
HELIX   29  29 CYS B  252  GLN B  260  1                                   9    
HELIX   30  30 ASP B  264  ALA B  273  1                                  10    
HELIX   31  31 PRO B  274  ALA B  276  5                                   3    
HELIX   32  32 ASN B  278  GLU B  290  1                                  13    
HELIX   33  33 PRO C   18  ALA C   22  5                                   5    
HELIX   34  34 SER C   24  LEU C   27  5                                   4    
HELIX   35  35 ILE C   36  ALA C   46  1                                  11    
HELIX   36  36 ASP C   59  GLY C   68  1                                  10    
HELIX   37  37 GLY C   70  GLY C   74  5                                   5    
HELIX   38  38 GLY C   87  ALA C   89  5                                   3    
HELIX   39  39 GLN C   90  GLY C   95  1                                   6    
HELIX   40  40 GLY C   95  GLY C  100  1                                   6    
HELIX   41  41 ASP C  117  ARG C  128  1                                  12    
HELIX   42  42 ASP C  141  ARG C  144  5                                   4    
HELIX   43  43 GLN C  181  ASP C  188  1                                   8    
HELIX   44  44 GLU C  198  ARG C  209  1                                  12    
HELIX   45  45 THR C  228  GLY C  247  1                                  20    
HELIX   46  46 CYS C  252  GLN C  260  1                                   9    
HELIX   47  47 ASP C  264  ALA C  273  1                                  10    
HELIX   48  48 PRO C  274  ALA C  276  5                                   3    
HELIX   49  49 ASN C  278  LEU C  288  1                                  11    
HELIX   50  50 SER D   24  LEU D   27  5                                   4    
HELIX   51  51 ILE D   36  ALA D   46  1                                  11    
HELIX   52  52 ASP D   59  GLY D   68  1                                  10    
HELIX   53  53 GLY D   70  GLY D   74  5                                   5    
HELIX   54  54 ALA D   89  GLY D   95  1                                   7    
HELIX   55  55 GLY D   95  GLY D  100  1                                   6    
HELIX   56  56 ASP D  117  ARG D  128  1                                  12    
HELIX   57  57 ASP D  141  ARG D  144  5                                   4    
HELIX   58  58 GLN D  181  ASP D  188  1                                   8    
HELIX   59  59 GLU D  198  ARG D  209  1                                  12    
HELIX   60  60 THR D  228  GLY D  247  1                                  20    
HELIX   61  61 CYS D  252  LYS D  261  1                                  10    
HELIX   62  62 ASP D  264  ALA D  273  1                                  10    
HELIX   63  63 PRO D  274  ALA D  276  5                                   3    
HELIX   64  64 ASN D  278  GLU D  290  1                                  13    
SHEET    1  AA 7 ASP A  76  VAL A  81  0                                        
SHEET    2  AA 7 GLU A  50  SER A  55  1  O  ILE A  51   N  GLN A  78           
SHEET    3  AA 7 LYS A   4  LEU A   8  1  O  GLY A   5   N  LEU A  52           
SHEET    4  AA 7 SER A 104  LEU A 108  1  O  ALA A 105   N  ILE A   6           
SHEET    5  AA 7 TYR A 170  TYR A 178 -1  O  GLY A 174   N  LEU A 108           
SHEET    6  AA 7 ALA A 132  HIS A 138 -1  O  SER A 133   N  PHE A 177           
SHEET    7  AA 7 LEU A 212  ILE A 216  1  O  SER A 213   N  VAL A 134           
SHEET    1  AB 2 PRO A  29  VAL A  30  0                                        
SHEET    2  AB 2 LYS A  33  PRO A  34 -1  O  LYS A  33   N  VAL A  30           
SHEET    1  AC 2 LEU A 112  TYR A 114  0                                        
SHEET    2  AC 2 ALA A 222  LEU A 224 -1  O  ALA A 222   N  TYR A 114           
SHEET    1  AD 2 GLY A 146  PHE A 150  0                                        
SHEET    2  AD 2 ALA A 156  GLU A 161 -1  N  ILE A 157   O  GLU A 149           
SHEET    1  BA 5 ASP B  76  VAL B  81  0                                        
SHEET    2  BA 5 GLU B  50  SER B  55  1  O  ILE B  51   N  GLN B  78           
SHEET    3  BA 5 ARG B   3  ALA B   9  1  O  GLY B   5   N  LEU B  52           
SHEET    4  BA 5 LEU B 103  LEU B 108  1  O  LEU B 103   N  LYS B   4           
SHEET    5  BA 5 LEU B 175  TYR B 178 -1  O  TYR B 176   N  LEU B 106           
SHEET    1  BB 2 PRO B  29  VAL B  30  0                                        
SHEET    2  BB 2 LYS B  33  PRO B  34 -1  O  LYS B  33   N  VAL B  30           
SHEET    1  BC 2 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 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 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 LYS C   4  LEU C   8  1  O  GLY C   5   N  LEU C  52           
SHEET    4  CA 5 SER C 104  LEU C 108  1  O  ALA C 105   N  ILE C   6           
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 LEU D 112  TYR D 114  0                                        
SHEET    2  DC 2 ALA D 222  LEU D 224 -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         7.30                     
CISPEP   2 HIS B   17    PRO B   18          0        -7.11                     
CISPEP   3 HIS C   17    PRO C   18          0         3.00                     
CISPEP   4 HIS D   17    PRO D   18          0         4.38                     
SITE     1 AC1 15 SER A  41  LEU A  45  TYR A 113  GLY A 115                    
SITE     2 AC1 15 PHE A 118  ARG A 219  VAL A 250  ALA A 251                    
SITE     3 AC1 15 GLU A 255  ILE A 256  ARG A 259  HOH A2058                    
SITE     4 AC1 15 HOH A2060  HOH A2122  HOH A2147                               
SITE     1 AC2  8 PHE A 150  GLY A 154  LYS A 155  ALA A 156                    
SITE     2 AC2  8 LEU A 212  SER A 213  VAL A 214  HOH A2106                    
SITE     1 AC3 13 SER B  41  LEU B  45  TYR B 113  GLY B 115                    
SITE     2 AC3 13 ARG B 219  VAL B 250  ALA B 251  GLU B 255                    
SITE     3 AC3 13 ILE B 256  HOH B2057  HOH B2060  HOH B2111                    
SITE     4 AC3 13 HOH B2127                                                     
SITE     1 AC4  6 GLY B 154  ALA B 156  SER B 213  VAL B 214                    
SITE     2 AC4  6 TYR B 293  HOH B2075                                          
SITE     1 AC5 13 LEU C  45  TYR C 113  GLY C 115  PHE C 118                    
SITE     2 AC5 13 ARG C 219  VAL C 250  ALA C 251  GLU C 255                    
SITE     3 AC5 13 ILE C 256  HOH C2043  HOH C2046  HOH C2102                    
SITE     4 AC5 13 HOH C2130                                                     
SITE     1 AC6 11 PHE C 150  GLY C 154  LYS C 155  ALA C 156                    
SITE     2 AC6 11 SER C 213  VAL C 214  ILE C 216  HOH C2066                    
SITE     3 AC6 11 HOH C2067  HOH C2131  HOH C2132                               
SITE     1 AC7 11 LEU D  45  TYR D 113  GLY D 115  ARG D 219                    
SITE     2 AC7 11 VAL D 250  ALA D 251  GLU D 255  HOH D2061                    
SITE     3 AC7 11 HOH D2064  HOH D2120  HOH D2135                               
SITE     1 AC8  8 GLY D 154  LYS D 155  ALA D 156  LEU D 212                    
SITE     2 AC8  8 SER D 213  VAL D 214  ILE D 216  TYR D 293                    
SITE     1 AC9  4 HIS D 116  GLY D 218  ARG D 219  GLY D 220                    
SITE     1 BC1  3 HIS A 116  GLY A 218  GLY A 220                               
SITE     1 BC2  2 HIS C 116  GLY C 220                                          
SITE     1 BC3  2 HIS B 116  GLY B 220                                          
SITE     1 BC4  1 VAL C  81                                                     
SITE     1 BC5  5 LEU D 140  GLU D 243  GLY D 247  LYS D 249                    
SITE     2 BC5  5 HOH D2021                                                     
SITE     1 BC6  4 LEU B 140  GLU B 243  LYS B 249  HOH B2016                    
CRYST1   63.990  153.760  134.650  90.00  92.32  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      0.015627  0.000000  0.000633        0.00000                         
SCALE2      0.000000  0.006504  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007433        0.00000                         
MTRIX1   1 -0.955300  0.010080  0.295500       39.90000    1                    
MTRIX2   1  0.013700  0.999900  0.010200      -20.59000    1                    
MTRIX3   1 -0.295300  0.013790 -0.955300       72.57000    1                    
MTRIX1   2  0.999000 -0.006691 -0.044550        5.64300    1                    
MTRIX2   2 -0.006102 -0.999900  0.013330      -16.89000    1                    
MTRIX3   2 -0.044640 -0.013050 -0.998900       68.22000    1                    
MTRIX1   3 -0.936200  0.008018 -0.351300       62.19000    1                    
MTRIX2   3 -0.004666 -0.999900 -0.010390      -35.53000    1                    
MTRIX3   3 -0.351300 -0.008088  0.936200       10.96000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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