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Database: PDB
Entry: 4K91
LinkDB: 4K91
Original site: 4K91 
HEADER    HYDROLASE                               19-APR-13   4K91              
TITLE     CRYSTAL STRUCTURE OF PENICILLIN-BINDING PROTEIN 5 (PBP5) FROM         
TITLE    2 PSEUDOMONAS AERUGINOSA IN APO STATE                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALA-D-ALA-CARBOXYPEPTIDASE;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: A SOLUBLE FRAGMENT EXCLUDING THE 24-RESIDUE N-TERMINAL     
COMPND   5 SIGNAL PEPTIDE AND THE 17-RESIDUE C-TERMINAL  MEMBRANE ANCHOR (UNP   
COMPND   6 RESIDUES 25-369);                                                    
COMPND   7 EC: 3.4.16.4;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA UCBPP-PA14;              
SOURCE   3 ORGANISM_TAXID: 208963;                                              
SOURCE   4 STRAIN: PAO1;                                                        
SOURCE   5 GENE: DACC, PA14_12100;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET24D(+)                                 
KEYWDS    DD-CARBOXYPEPTIDASE, MEMBRANE ASSOCIATED, HYDROLASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.SMITH,M.TOTH,S.VAKULENKO,S.MOBASHERY,Y.CHEN                         
REVDAT   1   25-SEP-13 4K91    0                                                
JRNL        AUTH   J.D.SMITH,M.KUMARASIRI,W.ZHANG,D.HESEK,M.LEE,M.TOTH,         
JRNL        AUTH 2 S.VAKULENKO,J.F.FISHER,S.MOBASHERY,Y.CHEN                    
JRNL        TITL   STRUCTURAL ANALYSIS OF THE ROLE OF PSEUDOMONAS AERUGINOSA    
JRNL        TITL 2 PENICILLIN-BINDING PROTEIN 5 IN BETA-LACTAM RESISTANCE.      
JRNL        REF    ANTIMICROB.AGENTS CHEMOTHER.  V.  57  3137 2013              
JRNL        REFN                   ISSN 0066-4804                               
JRNL        PMID   23629710                                                     
JRNL        DOI    10.1128/AAC.00505-13                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 46302                          
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) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2344                            
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) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3176                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.41                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 175                          
REMARK   3   BIN FREE R VALUE                    : 0.3520                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5239                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 155                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.35000                                              
REMARK   3    B22 (A**2) : 0.72000                                              
REMARK   3    B33 (A**2) : -1.42000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.49000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.219         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.193         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.153         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.646         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
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):  5369 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7260 ; 1.287 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   686 ; 3.721 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   237 ;31.876 ;24.937       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   939 ;13.003 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;13.879 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   815 ; 0.110 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4048 ; 0.003 ; 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):  3397 ; 1.410 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5437 ; 2.334 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1972 ; 3.475 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1823 ; 5.458 ; 4.500       
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 : 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 ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 4K91 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB079043.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-JUN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.11587                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46480                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2 M SUCCINIC ACID, PH    
REMARK 280  7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 288K                
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      116.07150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       19.95450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      116.07150            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       19.95450            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ALA A     2                                                      
REMARK 465     GLY A   345                                                      
REMARK 465     PHE A   346                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     PHE B   346                                                      
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    SER A   4       55.40    -99.11                                   
REMARK 500    ALA A  14      143.60   -170.63                                   
REMARK 500    ALA A  40     -136.58     55.25                                   
REMARK 500    PHE A  81       42.26     76.87                                   
REMARK 500    LEU A 202      -54.79   -130.31                                   
REMARK 500    PHE A 258      -65.75    -95.01                                   
REMARK 500    THR A 263      138.72    -31.61                                   
REMARK 500    LYS A 272        4.23     92.33                                   
REMARK 500    ASP A 285      137.49    -21.20                                   
REMARK 500    GLN A 307       51.34    -97.16                                   
REMARK 500    ILE A 318      -71.04   -103.38                                   
REMARK 500    ASP A 326       70.40     51.36                                   
REMARK 500    ILE A 330      -94.84   -125.76                                   
REMARK 500    GLU A 342     -157.79    -73.78                                   
REMARK 500    GLU A 343       28.96   -149.33                                   
REMARK 500    ALA B  40     -132.94     49.44                                   
REMARK 500    PHE B  81       53.63     80.03                                   
REMARK 500    LEU B 202      -50.32   -130.04                                   
REMARK 500    PHE B 258      -76.12    -95.63                                   
REMARK 500    THR B 266     -159.73   -147.95                                   
REMARK 500    GLN B 296       44.75    -87.26                                   
REMARK 500    LYS B 297       11.62   -145.90                                   
REMARK 500    GLN B 307       41.15    -69.66                                   
REMARK 500    ILE B 330      -33.10   -132.20                                   
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 SIN A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN B 402                 
DBREF  4K91 A    2   346  UNP    Q02SG6   Q02SG6_PSEAB    25    369             
DBREF  4K91 B    2   346  UNP    Q02SG6   Q02SG6_PSEAB    25    369             
SEQADV 4K91 MET A    1  UNP  Q02SG6              INITIATING METHIONINE          
SEQADV 4K91 MET B    1  UNP  Q02SG6              INITIATING METHIONINE          
SEQRES   1 A  346  MET ALA GLU SER MET VAL PRO ALA PRO PRO GLN LEU ALA          
SEQRES   2 A  346  ALA LYS SER TYR VAL LEU MET ASP GLY GLU SER GLY GLN          
SEQRES   3 A  346  VAL LEU VAL GLU ASN ASN GLY ASP GLN ARG LEU PRO PRO          
SEQRES   4 A  346  ALA SER LEU THR LYS LEU MET THR ALA TYR ILE ALA THR          
SEQRES   5 A  346  LYS GLU ILE GLU ALA GLY ARG ILE GLY GLU ASN ASP LEU          
SEQRES   6 A  346  VAL THR VAL SER GLU HIS ALA TRP ARG THR GLY GLY SER          
SEQRES   7 A  346  ARG MET PHE ILE LYS VAL GLY SER GLN VAL SER VAL SER          
SEQRES   8 A  346  ASP LEU LEU HIS GLY ILE ILE ILE GLN SER GLY ASN ASP          
SEQRES   9 A  346  ALA SER VAL ALA LEU ALA GLU HIS ILE ALA GLY SER GLU          
SEQRES  10 A  346  ASP ALA PHE ALA ASP MET MET ASN THR THR ALA GLN LYS          
SEQRES  11 A  346  LEU GLY LEU THR ASN SER HIS PHE MET ASP ALA THR GLY          
SEQRES  12 A  346  LEU PRO ASN PRO ASP HIS TYR SER SER ALA ARG ASP MET          
SEQRES  13 A  346  ALA VAL LEU ALA ARG ALA ILE ILE TYR GLY GLU PRO SER          
SEQRES  14 A  346  HIS TYR ALA ILE TYR ALA GLN LYS GLU PHE LEU TRP ASN          
SEQRES  15 A  346  ASN ILE LYS GLN PRO ASN ARG ASN LEU LEU LEU TRP ARG          
SEQRES  16 A  346  ASP LYS THR VAL ASP GLY LEU LYS THR GLY HIS THR ASP          
SEQRES  17 A  346  GLU ALA GLY TYR CYS LEU VAL ALA SER ALA VAL ARG ASP          
SEQRES  18 A  346  GLY GLN ARG MET ILE ALA VAL VAL PHE GLY THR ASN SER          
SEQRES  19 A  346  GLU GLN ALA ARG ALA ALA GLU THR GLN LYS LEU LEU THR          
SEQRES  20 A  346  TYR GLY PHE ARG PHE PHE GLU SER ARG ASN PHE TYR LYS          
SEQRES  21 A  346  LYS GLY THR GLU LEU THR LYS GLY LEU VAL TRP LYS GLY          
SEQRES  22 A  346  SER GLU HIS GLU VAL LYS ALA GLY LEU ALA GLU ASP LEU          
SEQRES  23 A  346  THR MET THR LEU PRO ARG GLY GLN MET GLN LYS LEU GLN          
SEQRES  24 A  346  ALA SER MET VAL LEU GLU PRO GLN LEU MET ALA PRO ILE          
SEQRES  25 A  346  GLN GLN GLY GLN VAL ILE GLY LYS VAL GLU VAL LYS LEU          
SEQRES  26 A  346  ASP ASP LYS VAL ILE ARG SER ALA ASP LEU VAL ALA LEU          
SEQRES  27 A  346  ASN ALA VAL GLU GLU GLY GLY PHE                              
SEQRES   1 B  346  MET ALA GLU SER MET VAL PRO ALA PRO PRO GLN LEU ALA          
SEQRES   2 B  346  ALA LYS SER TYR VAL LEU MET ASP GLY GLU SER GLY GLN          
SEQRES   3 B  346  VAL LEU VAL GLU ASN ASN GLY ASP GLN ARG LEU PRO PRO          
SEQRES   4 B  346  ALA SER LEU THR LYS LEU MET THR ALA TYR ILE ALA THR          
SEQRES   5 B  346  LYS GLU ILE GLU ALA GLY ARG ILE GLY GLU ASN ASP LEU          
SEQRES   6 B  346  VAL THR VAL SER GLU HIS ALA TRP ARG THR GLY GLY SER          
SEQRES   7 B  346  ARG MET PHE ILE LYS VAL GLY SER GLN VAL SER VAL SER          
SEQRES   8 B  346  ASP LEU LEU HIS GLY ILE ILE ILE GLN SER GLY ASN ASP          
SEQRES   9 B  346  ALA SER VAL ALA LEU ALA GLU HIS ILE ALA GLY SER GLU          
SEQRES  10 B  346  ASP ALA PHE ALA ASP MET MET ASN THR THR ALA GLN LYS          
SEQRES  11 B  346  LEU GLY LEU THR ASN SER HIS PHE MET ASP ALA THR GLY          
SEQRES  12 B  346  LEU PRO ASN PRO ASP HIS TYR SER SER ALA ARG ASP MET          
SEQRES  13 B  346  ALA VAL LEU ALA ARG ALA ILE ILE TYR GLY GLU PRO SER          
SEQRES  14 B  346  HIS TYR ALA ILE TYR ALA GLN LYS GLU PHE LEU TRP ASN          
SEQRES  15 B  346  ASN ILE LYS GLN PRO ASN ARG ASN LEU LEU LEU TRP ARG          
SEQRES  16 B  346  ASP LYS THR VAL ASP GLY LEU LYS THR GLY HIS THR ASP          
SEQRES  17 B  346  GLU ALA GLY TYR CYS LEU VAL ALA SER ALA VAL ARG ASP          
SEQRES  18 B  346  GLY GLN ARG MET ILE ALA VAL VAL PHE GLY THR ASN SER          
SEQRES  19 B  346  GLU GLN ALA ARG ALA ALA GLU THR GLN LYS LEU LEU THR          
SEQRES  20 B  346  TYR GLY PHE ARG PHE PHE GLU SER ARG ASN PHE TYR LYS          
SEQRES  21 B  346  LYS GLY THR GLU LEU THR LYS GLY LEU VAL TRP LYS GLY          
SEQRES  22 B  346  SER GLU HIS GLU VAL LYS ALA GLY LEU ALA GLU ASP LEU          
SEQRES  23 B  346  THR MET THR LEU PRO ARG GLY GLN MET GLN LYS LEU GLN          
SEQRES  24 B  346  ALA SER MET VAL LEU GLU PRO GLN LEU MET ALA PRO ILE          
SEQRES  25 B  346  GLN GLN GLY GLN VAL ILE GLY LYS VAL GLU VAL LYS LEU          
SEQRES  26 B  346  ASP ASP LYS VAL ILE ARG SER ALA ASP LEU VAL ALA LEU          
SEQRES  27 B  346  ASN ALA VAL GLU GLU GLY GLY PHE                              
HET    SIN  A 601       8                                                       
HET    SIN  B 401       8                                                       
HET    SIN  B 402       8                                                       
HETNAM     SIN SUCCINIC ACID                                                    
FORMUL   3  SIN    3(C4 H6 O4)                                                  
FORMUL   6  HOH   *155(H2 O)                                                    
HELIX    1   1 PRO A   39  SER A   41  5                                   3    
HELIX    2   2 LEU A   42  ALA A   57  1                                  16    
HELIX    3   3 SER A   69  ARG A   74  1                                   6    
HELIX    4   4 VAL A   90  SER A  101  1                                  12    
HELIX    5   5 GLY A  102  GLY A  115  1                                  14    
HELIX    6   6 SER A  116  GLY A  132  1                                  17    
HELIX    7   7 SER A  152  TYR A  165  1                                  14    
HELIX    8   8 GLU A  167  ALA A  172  1                                   6    
HELIX    9   9 ILE A  173  GLN A  176  5                                   4    
HELIX   10  10 LEU A  191  ASP A  196  1                                   6    
HELIX   11  11 SER A  234  PHE A  252  1                                  19    
HELIX   12  12 GLN A  294  GLN A  296  5                                   3    
HELIX   13  13 PRO B   39  LEU B   42  5                                   4    
HELIX   14  14 THR B   43  ALA B   57  1                                  15    
HELIX   15  15 SER B   69  ARG B   74  1                                   6    
HELIX   16  16 VAL B   90  SER B  101  1                                  12    
HELIX   17  17 GLY B  102  GLY B  115  1                                  14    
HELIX   18  18 SER B  116  GLY B  132  1                                  17    
HELIX   19  19 SER B  152  TYR B  165  1                                  14    
HELIX   20  20 GLU B  167  ALA B  172  1                                   6    
HELIX   21  21 ILE B  173  GLN B  176  5                                   4    
HELIX   22  22 ASN B  190  ASP B  196  1                                   7    
HELIX   23  23 SER B  234  PHE B  252  1                                  19    
HELIX   24  24 GLN B  294  GLN B  296  5                                   3    
SHEET    1   A 5 VAL A  27  ASN A  31  0                                        
SHEET    2   A 5 SER A  16  ASP A  21 -1  N  TYR A  17   O  ASN A  31           
SHEET    3   A 5 GLN A 223  THR A 232 -1  O  PHE A 230   N  SER A  16           
SHEET    4   A 5 GLY A 211  ARG A 220 -1  N  ALA A 216   O  ALA A 227           
SHEET    5   A 5 VAL A 199  THR A 207 -1  N  GLY A 205   O  CYS A 213           
SHEET    1   B 2 LEU A  65  THR A  67  0                                        
SHEET    2   B 2 GLN A  87  SER A  89 -1  O  VAL A  88   N  VAL A  66           
SHEET    1   C 2 GLU A 178  TRP A 181  0                                        
SHEET    2   C 2 ILE A 184  PRO A 187 -1  O  ILE A 184   N  TRP A 181           
SHEET    1   D 2 PHE A 253  TYR A 259  0                                        
SHEET    2   D 2 LEU A 286  PRO A 291 -1  O  LEU A 286   N  TYR A 259           
SHEET    1   E 5 THR A 266  LEU A 269  0                                        
SHEET    2   E 5 GLU A 277  LEU A 282 -1  O  ALA A 280   N  THR A 266           
SHEET    3   E 5 LEU A 335  ALA A 337 -1  O  VAL A 336   N  GLY A 281           
SHEET    4   E 5 VAL A 317  LEU A 325 -1  N  ILE A 318   O  LEU A 335           
SHEET    5   E 5 LEU A 298  VAL A 303 -1  N  SER A 301   O  GLU A 322           
SHEET    1   F 5 THR A 266  LEU A 269  0                                        
SHEET    2   F 5 GLU A 277  LEU A 282 -1  O  ALA A 280   N  THR A 266           
SHEET    3   F 5 LEU A 335  ALA A 337 -1  O  VAL A 336   N  GLY A 281           
SHEET    4   F 5 VAL A 317  LEU A 325 -1  N  ILE A 318   O  LEU A 335           
SHEET    5   F 5 VAL A 329  SER A 332 -1  O  ILE A 330   N  VAL A 323           
SHEET    1   G 5 VAL B  27  ASN B  31  0                                        
SHEET    2   G 5 SER B  16  ASP B  21 -1  N  LEU B  19   O  LEU B  28           
SHEET    3   G 5 GLN B 223  THR B 232 -1  O  ILE B 226   N  MET B  20           
SHEET    4   G 5 GLY B 211  ARG B 220 -1  N  ALA B 216   O  ALA B 227           
SHEET    5   G 5 VAL B 199  THR B 207 -1  N  GLY B 205   O  CYS B 213           
SHEET    1   H 2 LEU B  65  THR B  67  0                                        
SHEET    2   H 2 GLN B  87  SER B  89 -1  O  VAL B  88   N  VAL B  66           
SHEET    1   I 2 GLU B 178  TRP B 181  0                                        
SHEET    2   I 2 ILE B 184  PRO B 187 -1  O  GLN B 186   N  PHE B 179           
SHEET    1   J 2 PHE B 253  TYR B 259  0                                        
SHEET    2   J 2 LEU B 286  PRO B 291 -1  O  MET B 288   N  ARG B 256           
SHEET    1   K 5 GLU B 264  LEU B 269  0                                        
SHEET    2   K 5 GLU B 277  LEU B 282 -1  O  VAL B 278   N  GLY B 268           
SHEET    3   K 5 LYS B 328  ALA B 337 -1  O  VAL B 336   N  GLY B 281           
SHEET    4   K 5 VAL B 317  LEU B 325 -1  N  LEU B 325   O  LYS B 328           
SHEET    5   K 5 LEU B 298  LEU B 304 -1  N  GLN B 299   O  LYS B 324           
CISPEP   1 GLY A  201    LEU A  202          0         0.23                     
CISPEP   2 ALA A  310    PRO A  311          0         1.58                     
CISPEP   3 GLY B  201    LEU B  202          0        -2.29                     
CISPEP   4 ALA B  310    PRO B  311          0         2.23                     
SITE     1 AC1  9 ALA A  40  SER A  41  ARG A 189  THR A 204                    
SITE     2 AC1  9 GLY A 205  HIS A 206  HOH A 707  HOH A 721                    
SITE     3 AC1  9 HOH A 722                                                     
SITE     1 AC2  9 ARG A 189  HOH A 737  TRP B  73  ARG B  79                    
SITE     2 AC2  9 PHE B  81  LYS B  83  HOH B 515  HOH B 516                    
SITE     3 AC2  9 HOH B 558                                                     
SITE     1 AC3 10 ALA B  40  SER B  41  SER B 101  ARG B 189                    
SITE     2 AC3 10 THR B 204  GLY B 205  HIS B 206  HOH B 507                    
SITE     3 AC3 10 HOH B 517  HOH B 549                                          
CRYST1  232.143   39.909   85.461  90.00 111.03  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.004308  0.000000  0.001656        0.00000                         
SCALE2      0.000000  0.025057  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012536        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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