GenomeNet

Database: PDB
Entry: 4ECI
LinkDB: 4ECI
Original site: 4ECI 
HEADER    TRANSFERASE                             26-MAR-12   4ECI              
TITLE     CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE PRK13972 (TARGET EFI-  
TITLE    2 501853) FROM PSEUDOMONAS AERUGINOSA PACS2 COMPLEXED WITH ACETATE     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 388272;                                              
SOURCE   4 STRAIN: PACS2;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    TRANSFERASE-LIKE PROTEIN, TRANSCRIPTION REGULATION, TRANSFERASE       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.PATSKOVSKY,R.TORO,R.BHOSLE,W.D.ZENCHECK,B.HILLERICH,R.D.SEIDEL,     
AUTHOR   2 E.WASHINGTON,A.SCOTT GLENN,S.CHOWDHURY,B.EVANS,J.HAMMONDS,H.J.IMKER, 
AUTHOR   3 R.N.ARMSTRONG,J.A.GERLT,S.C.ALMO,ENZYME FUNCTION INITIATIVE (EFI)    
REVDAT   1   18-APR-12 4ECI    0                                                
JRNL        AUTH   Y.PATSKOVSKY,R.TORO,R.BHOSLE,W.D.ZENCHECK,B.HILLERICH,       
JRNL        AUTH 2 R.D.SEIDEL,E.WASHINGTON,A.SCOTT GLENN,S.CHOWDHURY,B.EVANS,   
JRNL        AUTH 3 J.HAMMONDS,H.J.IMKER,R.N.ARMSTRONG,J.A.GERLT,S.C.ALMO        
JRNL        TITL   CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE PRK13972 FROM 
JRNL        TITL 2 PSEUDOMONAS AERUGINOSA                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 39773                          
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                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1279                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2621                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.77                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3440                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 78                           
REMARK   3   BIN FREE R VALUE                    : 0.3560                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3251                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 211                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.74                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.21000                                              
REMARK   3    B22 (A**2) : 3.12000                                              
REMARK   3    B33 (A**2) : -4.33000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.118         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.114         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.097         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.292         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.962                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3387 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4595 ; 1.312 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   418 ; 5.436 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   172 ;30.258 ;22.791       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   566 ;13.168 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    37 ;17.230 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   484 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2653 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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 WITH 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   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4ECI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-APR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071444.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44316                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.760                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -5.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : 7.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 69.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.83000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3GX0                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17M AMMONIUM ACETATE, 0.085M SODIUM    
REMARK 280  CITRATE, 25.5% PEG4000, 15% GLYCEROL, PH 5.6, VAPOR DIFFUSION,      
REMARK 280  SITTING DROP, TEMPERATURE 294K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       42.44800            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.97650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.44800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.97650            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    -1                                                      
REMARK 465     GLU A   204                                                      
REMARK 465     LYS A   205                                                      
REMARK 465     GLU A   206                                                      
REMARK 465     GLY A   207                                                      
REMARK 465     ASP A   208                                                      
REMARK 465     ASP A   209                                                      
REMARK 465     ALA A   210                                                      
REMARK 465     ILE A   211                                                      
REMARK 465     ARG A   212                                                      
REMARK 465     THR A   213                                                      
REMARK 465     ALA A   214                                                      
REMARK 465     GLN A   215                                                      
REMARK 465     SER A   216                                                      
REMARK 465     MET A   217                                                      
REMARK 465     LEU A   218                                                      
REMARK 465     THR A   219                                                      
REMARK 465     ARG A   220                                                      
REMARK 465     ALA A   221                                                      
REMARK 465     GLU A   222                                                      
REMARK 465     ASN A   223                                                      
REMARK 465     LEU A   224                                                      
REMARK 465     TYR A   225                                                      
REMARK 465     PHE A   226                                                      
REMARK 465     GLN A   227                                                      
REMARK 465     SER A   228                                                      
REMARK 465     HIS A   229                                                      
REMARK 465     HIS A   230                                                      
REMARK 465     HIS A   231                                                      
REMARK 465     HIS A   232                                                      
REMARK 465     HIS A   233                                                      
REMARK 465     HIS A   234                                                      
REMARK 465     TRP A   235                                                      
REMARK 465     SER A   236                                                      
REMARK 465     HIS A   237                                                      
REMARK 465     PRO A   238                                                      
REMARK 465     GLN A   239                                                      
REMARK 465     PHE A   240                                                      
REMARK 465     GLU A   241                                                      
REMARK 465     LYS A   242                                                      
REMARK 465     ARG B   203                                                      
REMARK 465     GLU B   204                                                      
REMARK 465     LYS B   205                                                      
REMARK 465     GLU B   206                                                      
REMARK 465     GLY B   207                                                      
REMARK 465     ASP B   208                                                      
REMARK 465     ASP B   209                                                      
REMARK 465     ALA B   210                                                      
REMARK 465     ILE B   211                                                      
REMARK 465     ARG B   212                                                      
REMARK 465     THR B   213                                                      
REMARK 465     ALA B   214                                                      
REMARK 465     GLN B   215                                                      
REMARK 465     SER B   216                                                      
REMARK 465     MET B   217                                                      
REMARK 465     LEU B   218                                                      
REMARK 465     THR B   219                                                      
REMARK 465     ARG B   220                                                      
REMARK 465     ALA B   221                                                      
REMARK 465     GLU B   222                                                      
REMARK 465     ASN B   223                                                      
REMARK 465     LEU B   224                                                      
REMARK 465     TYR B   225                                                      
REMARK 465     PHE B   226                                                      
REMARK 465     GLN B   227                                                      
REMARK 465     SER B   228                                                      
REMARK 465     HIS B   229                                                      
REMARK 465     HIS B   230                                                      
REMARK 465     HIS B   231                                                      
REMARK 465     HIS B   232                                                      
REMARK 465     HIS B   233                                                      
REMARK 465     HIS B   234                                                      
REMARK 465     TRP B   235                                                      
REMARK 465     SER B   236                                                      
REMARK 465     HIS B   237                                                      
REMARK 465     PRO B   238                                                      
REMARK 465     GLN B   239                                                      
REMARK 465     PHE B   240                                                      
REMARK 465     GLU B   241                                                      
REMARK 465     LYS B   242                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG B 202    CG   CD   NE   CZ   NH1  NH2                        
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    GLU A  67      113.11     73.92                                   
REMARK 500    LEU A 178       79.06   -101.11                                   
REMARK 500    GLU B  67      108.39     79.61                                   
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 ACT A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EFI-501853   RELATED DB: TARGETTRACK                     
DBREF  4ECI A    1   220  UNP    Q02KA8   Q02KA8_PSEAB     1    220             
DBREF  4ECI B    1   220  UNP    Q02KA8   Q02KA8_PSEAB     1    220             
SEQADV 4ECI MET A   -1  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI VAL A    0  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI ALA A  221  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI GLU A  222  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI ASN A  223  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI LEU A  224  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI TYR A  225  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI PHE A  226  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI GLN A  227  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI SER A  228  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI HIS A  229  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI HIS A  230  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI HIS A  231  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI HIS A  232  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI HIS A  233  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI HIS A  234  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI TRP A  235  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI SER A  236  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI HIS A  237  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI PRO A  238  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI GLN A  239  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI PHE A  240  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI GLU A  241  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI LYS A  242  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI MET B   -1  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI VAL B    0  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI ALA B  221  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI GLU B  222  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI ASN B  223  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI LEU B  224  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI TYR B  225  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI PHE B  226  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI GLN B  227  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI SER B  228  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI HIS B  229  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI HIS B  230  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI HIS B  231  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI HIS B  232  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI HIS B  233  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI HIS B  234  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI TRP B  235  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI SER B  236  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI HIS B  237  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI PRO B  238  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI GLN B  239  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI PHE B  240  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI GLU B  241  UNP  Q02KA8              EXPRESSION TAG                 
SEQADV 4ECI LYS B  242  UNP  Q02KA8              EXPRESSION TAG                 
SEQRES   1 A  244  MET VAL MET ILE ASP LEU TYR THR ALA ALA THR PRO ASN          
SEQRES   2 A  244  GLY HIS LYS VAL SER ILE ALA LEU GLU GLU MET GLY LEU          
SEQRES   3 A  244  PRO TYR ARG VAL HIS ALA LEU SER PHE ASP LYS LYS GLU          
SEQRES   4 A  244  GLN LYS ALA PRO GLU PHE LEU ARG ILE ASN PRO ASN GLY          
SEQRES   5 A  244  ARG ILE PRO ALA ILE VAL ASP ARG ASP ASN ASP ASP PHE          
SEQRES   6 A  244  ALA VAL PHE GLU SER GLY ALA ILE LEU ILE TYR LEU ALA          
SEQRES   7 A  244  GLU LYS THR GLY GLN LEU MET PRO ALA ASP VAL LYS GLY          
SEQRES   8 A  244  ARG SER ARG VAL ILE GLN TRP LEU MET PHE GLN MET GLY          
SEQRES   9 A  244  GLY VAL GLY PRO MET GLN GLY GLN ALA ASN VAL PHE PHE          
SEQRES  10 A  244  ARG TYR PHE PRO GLU LYS LEU GLN GLY ALA ILE ASP ARG          
SEQRES  11 A  244  TYR GLN HIS GLU THR ARG ARG LEU TYR GLU VAL LEU ASP          
SEQRES  12 A  244  GLY ARG LEU GLY GLU ALA GLU TYR LEU ALA GLY ASP TYR          
SEQRES  13 A  244  SER ILE ALA ASP ILE ALA THR TYR PRO TRP VAL ARG ILE          
SEQRES  14 A  244  HIS ASP TRP SER GLY VAL ALA VAL ASP GLY LEU ASP ASN          
SEQRES  15 A  244  LEU GLN ARG TRP ILE ALA ALA ILE GLU ALA ARG PRO ALA          
SEQRES  16 A  244  VAL GLN ARG GLY LEU LEU VAL PRO ARG ARG GLU LYS GLU          
SEQRES  17 A  244  GLY ASP ASP ALA ILE ARG THR ALA GLN SER MET LEU THR          
SEQRES  18 A  244  ARG ALA GLU ASN LEU TYR PHE GLN SER HIS HIS HIS HIS          
SEQRES  19 A  244  HIS HIS TRP SER HIS PRO GLN PHE GLU LYS                      
SEQRES   1 B  244  MET VAL MET ILE ASP LEU TYR THR ALA ALA THR PRO ASN          
SEQRES   2 B  244  GLY HIS LYS VAL SER ILE ALA LEU GLU GLU MET GLY LEU          
SEQRES   3 B  244  PRO TYR ARG VAL HIS ALA LEU SER PHE ASP LYS LYS GLU          
SEQRES   4 B  244  GLN LYS ALA PRO GLU PHE LEU ARG ILE ASN PRO ASN GLY          
SEQRES   5 B  244  ARG ILE PRO ALA ILE VAL ASP ARG ASP ASN ASP ASP PHE          
SEQRES   6 B  244  ALA VAL PHE GLU SER GLY ALA ILE LEU ILE TYR LEU ALA          
SEQRES   7 B  244  GLU LYS THR GLY GLN LEU MET PRO ALA ASP VAL LYS GLY          
SEQRES   8 B  244  ARG SER ARG VAL ILE GLN TRP LEU MET PHE GLN MET GLY          
SEQRES   9 B  244  GLY VAL GLY PRO MET GLN GLY GLN ALA ASN VAL PHE PHE          
SEQRES  10 B  244  ARG TYR PHE PRO GLU LYS LEU GLN GLY ALA ILE ASP ARG          
SEQRES  11 B  244  TYR GLN HIS GLU THR ARG ARG LEU TYR GLU VAL LEU ASP          
SEQRES  12 B  244  GLY ARG LEU GLY GLU ALA GLU TYR LEU ALA GLY ASP TYR          
SEQRES  13 B  244  SER ILE ALA ASP ILE ALA THR TYR PRO TRP VAL ARG ILE          
SEQRES  14 B  244  HIS ASP TRP SER GLY VAL ALA VAL ASP GLY LEU ASP ASN          
SEQRES  15 B  244  LEU GLN ARG TRP ILE ALA ALA ILE GLU ALA ARG PRO ALA          
SEQRES  16 B  244  VAL GLN ARG GLY LEU LEU VAL PRO ARG ARG GLU LYS GLU          
SEQRES  17 B  244  GLY ASP ASP ALA ILE ARG THR ALA GLN SER MET LEU THR          
SEQRES  18 B  244  ARG ALA GLU ASN LEU TYR PHE GLN SER HIS HIS HIS HIS          
SEQRES  19 B  244  HIS HIS TRP SER HIS PRO GLN PHE GLU LYS                      
HET    ACT  A 301       4                                                       
HET    ACT  B 301       4                                                       
HETNAM     ACT ACETATE ION                                                      
FORMUL   3  ACT    2(C2 H3 O2 1-)                                               
FORMUL   5  HOH   *211(H2 O)                                                    
HELIX    1   1 THR A    9  GLY A   23  1                                  15    
HELIX    2   2 SER A   32  LYS A   39  5                                   8    
HELIX    3   3 ALA A   40  ARG A   45  1                                   6    
HELIX    4   4 ASP A   59  ASP A   61  5                                   3    
HELIX    5   5 GLU A   67  GLY A   80  1                                  14    
HELIX    6   6 ASP A   86  GLY A  103  1                                  18    
HELIX    7   7 GLY A  103  TYR A  117  1                                  15    
HELIX    8   8 LEU A  122  ALA A  147  1                                  26    
HELIX    9   9 SER A  155  ILE A  167  1                                  13    
HELIX   10  10 ILE A  167  GLY A  172  1                                   6    
HELIX   11  11 LEU A  178  ALA A  190  1                                  13    
HELIX   12  12 ARG A  191  LEU A  198  1                                   8    
HELIX   13  13 THR B    9  GLY B   23  1                                  15    
HELIX   14  14 LYS B   36  LYS B   39  5                                   4    
HELIX   15  15 ALA B   40  ARG B   45  1                                   6    
HELIX   16  16 ASP B   59  ASP B   61  5                                   3    
HELIX   17  17 GLU B   67  GLY B   80  1                                  14    
HELIX   18  18 ASP B   86  GLY B  103  1                                  18    
HELIX   19  19 GLY B  103  TYR B  117  1                                  15    
HELIX   20  20 LEU B  122  LEU B  144  1                                  23    
HELIX   21  21 SER B  155  ILE B  167  1                                  13    
HELIX   22  22 ILE B  167  GLY B  172  1                                   6    
HELIX   23  23 LEU B  178  ALA B  190  1                                  13    
HELIX   24  24 ARG B  191  LEU B  198  1                                   8    
SHEET    1   A 4 TYR A  26  ALA A  30  0                                        
SHEET    2   A 4 ILE A   2  THR A   6  1  N  LEU A   4   O  HIS A  29           
SHEET    3   A 4 ALA A  54  ASP A  57 -1  O  ALA A  54   N  TYR A   5           
SHEET    4   A 4 PHE A  63  PHE A  66 -1  O  PHE A  63   N  ASP A  57           
SHEET    1   B 4 TYR B  26  ALA B  30  0                                        
SHEET    2   B 4 ILE B   2  THR B   6  1  N  LEU B   4   O  ARG B  27           
SHEET    3   B 4 ALA B  54  ASP B  57 -1  O  VAL B  56   N  ASP B   3           
SHEET    4   B 4 PHE B  63  PHE B  66 -1  O  VAL B  65   N  ILE B  55           
CISPEP   1 ILE A   52    PRO A   53          0         1.39                     
CISPEP   2 VAL A  200    PRO A  201          0         1.41                     
CISPEP   3 ILE B   52    PRO B   53          0         0.96                     
CISPEP   4 VAL B  200    PRO B  201          0         2.27                     
SITE     1 AC1  7 ASN A  11  ARG A  51  PRO A  53  GLU A  67                    
SITE     2 AC1  7 SER A  68  HOH A 410  HOH A 492                               
SITE     1 AC2  5 PRO B  53  GLU B  67  SER B  68  HOH B 407                    
SITE     2 AC2  5 HOH B 478                                                     
CRYST1   84.896   99.953   51.494  90.00  90.00  90.00 P 21 21 2     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      0.011779  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010005  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019420        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2 -0.940064 -0.259576 -0.221134        9.34361    1                    
MTRIX2   2 -0.259644  0.124486  0.957647       -7.10804    1                    
MTRIX3   2 -0.221055  0.957666 -0.184422       10.73361    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system