GenomeNet

Database: PDB
Entry: 5AKO
LinkDB: 5AKO
Original site: 5AKO 
HEADER    UNKNOWN FUNCTION                        04-MAR-15   5AKO              
TITLE     THE COMPLEX OF TSE2 AND TSI2 FROM PSEUDOMONAS AERUGINOSA              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TSI2;                                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: TSE2;                                                      
COMPND   7 CHAIN: C, D;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE  11 ORGANISM_TAXID: 287;                                                 
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  14 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    UNKNOWN FUNCTION, T6SS, IMMUNITY PROTEIN, TOXIN                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.S.ROBB,F.E.NANO,A.B.BORASTON                                        
REVDAT   4   23-AUG-17 5AKO    1       REMARK                                   
REVDAT   3   02-MAR-16 5AKO    1       JRNL                                     
REVDAT   2   20-JAN-16 5AKO    1       JRNL                                     
REVDAT   1   23-DEC-15 5AKO    0                                                
JRNL        AUTH   C.S.ROBB,M.ROBB,F.E.NANO,A.B.BORASTON                        
JRNL        TITL   THE STRUCTURE OF THE TOXIN AND TYPE SIX SECRETION SYSTEM     
JRNL        TITL 2 SUBSTRATE TSE2 IN COMPLEX WITH ITS IMMUNITY PROTEIN.         
JRNL        REF    STRUCTURE                     V.  24   277 2016              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   26749446                                                     
JRNL        DOI    10.1016/J.STR.2015.11.012                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.83                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 16778                          
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 896                             
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1239                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2370                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 63                           
REMARK   3   BIN FREE R VALUE                    : 0.3350                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3437                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 74                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.87                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.81000                                             
REMARK   3    B22 (A**2) : -2.66000                                             
REMARK   3    B33 (A**2) : 9.46000                                              
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): 0.117         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.061         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.149         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.182         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3510 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3257 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4790 ; 1.543 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7455 ; 1.020 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   449 ; 6.875 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   160 ;36.793 ;24.125       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   515 ;14.210 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;22.422 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   534 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4071 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   773 ; 0.004 ; 0.020       
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   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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   : 1.20                                          
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.                                                          
REMARK   4                                                                      
REMARK   4 5AKO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-MAR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1290063198.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 113                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : LIQUID NITROGEN-COOLED DOUBLE      
REMARK 200                                   CRYSTAL                            
REMARK 200  OPTICS                         : K-B FOCUSING MIRRORS               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17725                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.840                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.73000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3VPV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM TRIS PH 8.5, 0.2 M NACL, 22% PEG   
REMARK 280  4K                                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       18.86250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       57.32100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.56900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       57.32100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       18.86250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       51.56900            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.9 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A    76                                                      
REMARK 465     SER A    77                                                      
REMARK 465     ALA B    76                                                      
REMARK 465     SER B    77                                                      
REMARK 465     MET C   -19                                                      
REMARK 465     GLY C   -18                                                      
REMARK 465     SER C   -17                                                      
REMARK 465     SER C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     GLY C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     VAL C    -5                                                      
REMARK 465     PRO C    -4                                                      
REMARK 465     ARG C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     MET C     2                                                      
REMARK 465     GLU C    38                                                      
REMARK 465     ALA C    39                                                      
REMARK 465     ALA C    40                                                      
REMARK 465     LEU C   159                                                      
REMARK 465     MET D   -19                                                      
REMARK 465     GLY D   -18                                                      
REMARK 465     SER D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     GLY D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     VAL D    -5                                                      
REMARK 465     PRO D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     MET D     2                                                      
REMARK 465     GLU D    38                                                      
REMARK 465     ALA D    39                                                      
REMARK 465     ALA D    40                                                      
REMARK 465     LEU D   159                                                      
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     ASN A   2    CG   OD1  ND2                                       
REMARK 470     GLU A  21    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  27    CG   CD   OE1  NE2                                  
REMARK 470     ASP A  30    CG   OD1  OD2                                       
REMARK 470     GLN A  32    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  36    CD   OE1  OE2                                       
REMARK 470     GLU A  56    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  74    CD   OE1  OE2                                       
REMARK 470     MET B   1    CG   SD   CE                                        
REMARK 470     GLN B  32    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  56    CD   OE1  OE2                                       
REMARK 470     GLU B  74    CG   CD   OE1  OE2                                  
REMARK 470     SER C   3    OG                                                  
REMARK 470     LYS C   8    CD   CE   NZ                                        
REMARK 470     LYS C  19    CG   CD   CE   NZ                                   
REMARK 470     ASP C  23    CG   OD1  OD2                                       
REMARK 470     ARG C  28    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS C  31    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP C  33    CG   OD1  OD2                                       
REMARK 470     LYS C  34    CG   CD   CE   NZ                                   
REMARK 470     GLU C  35    CG   CD   OE1  OE2                                  
REMARK 470     LEU C  36    CG   CD1  CD2                                       
REMARK 470     GLU C  41    CG   CD   OE1  OE2                                  
REMARK 470     THR C  55    OG1  CG2                                            
REMARK 470     ARG C  61    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG C  90    CZ   NH1  NH2                                       
REMARK 470     ARG C 157    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER D   3    OG                                                  
REMARK 470     GLU D   7    CG   CD   OE1  OE2                                  
REMARK 470     LYS D   8    CG   CD   CE   NZ                                   
REMARK 470     LYS D  19    CG   CD   CE   NZ                                   
REMARK 470     ASP D  33    CG   OD1  OD2                                       
REMARK 470     LYS D  34    CG   CD   CE   NZ                                   
REMARK 470     LEU D  36    CG   CD1  CD2                                       
REMARK 470     GLU D  41    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP D 153    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP D 153    CZ3  CH2                                            
REMARK 470     ARG D 157    CD   NE   CZ   NH1  NH2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP B  69   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    MET D 127   N   -  CA  -  CB  ANGL. DEV. = -11.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN B  33       56.54   -119.79                                   
REMARK 500    ASP C  23       73.10   -101.27                                   
REMARK 500    ASP C  33      -88.70    -99.72                                   
REMARK 500    LEU C  36       71.36   -102.49                                   
REMARK 500    ASP C 113     -149.76   -104.90                                   
REMARK 500    GLU D  35       39.19   -148.44                                   
REMARK 500    ASP D 113     -150.78   -102.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5AKO A    1    77  UNP    Q9I0D9   Q9I0D9_PSEAE     1     77             
DBREF  5AKO B    1    77  UNP    Q9I0D9   Q9I0D9_PSEAE     1     77             
DBREF  5AKO C    2   159  UNP    Q9I0E0   Q9I0E0_PSEAE     1    158             
DBREF  5AKO D    2   159  UNP    Q9I0E0   Q9I0E0_PSEAE     1    158             
SEQADV 5AKO MET C  -19  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO GLY C  -18  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO SER C  -17  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO SER C  -16  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO HIS C  -15  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO HIS C  -14  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO HIS C  -13  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO HIS C  -12  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO HIS C  -11  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO HIS C  -10  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO SER C   -9  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO SER C   -8  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO GLY C   -7  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO LEU C   -6  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO VAL C   -5  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO PRO C   -4  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO ARG C   -3  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO GLY C   -2  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO SER C   -1  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO HIS C    0  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO MET C    1  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO MET D  -19  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO GLY D  -18  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO SER D  -17  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO SER D  -16  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO HIS D  -15  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO HIS D  -14  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO HIS D  -13  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO HIS D  -12  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO HIS D  -11  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO HIS D  -10  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO SER D   -9  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO SER D   -8  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO GLY D   -7  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO LEU D   -6  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO VAL D   -5  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO PRO D   -4  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO ARG D   -3  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO GLY D   -2  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO SER D   -1  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO HIS D    0  UNP  Q9I0E0              EXPRESSION TAG                 
SEQADV 5AKO MET D    1  UNP  Q9I0E0              EXPRESSION TAG                 
SEQRES   1 A   77  MET ASN LEU LYS PRO GLN THR LEU MET VAL ALA ILE GLN          
SEQRES   2 A   77  CYS VAL ALA ALA ARG THR ARG GLU LEU ASP ALA GLN LEU          
SEQRES   3 A   77  GLN ASN ASP ASP PRO GLN ASN ALA ALA GLU LEU GLU GLN          
SEQRES   4 A   77  LEU LEU VAL GLY TYR ASP LEU ALA ALA ASP ASP LEU LYS          
SEQRES   5 A   77  ASN ALA TYR GLU GLN ALA LEU GLY GLN TYR SER GLY LEU          
SEQRES   6 A   77  PRO PRO TYR ASP ARG LEU ILE GLU GLU PRO ALA SER              
SEQRES   1 B   77  MET ASN LEU LYS PRO GLN THR LEU MET VAL ALA ILE GLN          
SEQRES   2 B   77  CYS VAL ALA ALA ARG THR ARG GLU LEU ASP ALA GLN LEU          
SEQRES   3 B   77  GLN ASN ASP ASP PRO GLN ASN ALA ALA GLU LEU GLU GLN          
SEQRES   4 B   77  LEU LEU VAL GLY TYR ASP LEU ALA ALA ASP ASP LEU LYS          
SEQRES   5 B   77  ASN ALA TYR GLU GLN ALA LEU GLY GLN TYR SER GLY LEU          
SEQRES   6 B   77  PRO PRO TYR ASP ARG LEU ILE GLU GLU PRO ALA SER              
SEQRES   1 C  179  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  179  LEU VAL PRO ARG GLY SER HIS MET MET SER TYR ASP TYR          
SEQRES   3 C  179  GLU LYS THR SER LEU THR LEU TYR ARG ALA VAL PHE LYS          
SEQRES   4 C  179  ALA ASN TYR ASP GLY ASP VAL GLY ARG TYR LEU HIS PRO          
SEQRES   5 C  179  ASP LYS GLU LEU ALA GLU ALA ALA GLU VAL ALA PRO LEU          
SEQRES   6 C  179  LEU HIS PRO THR PHE ASP SER PRO ASN THR PRO GLY VAL          
SEQRES   7 C  179  PRO ALA ARG ALA PRO ASP ILE VAL ALA GLY ARG ASP GLY          
SEQRES   8 C  179  LEU TYR ALA PRO ASP THR GLY GLY THR SER VAL PHE ASP          
SEQRES   9 C  179  ARG ALA GLY VAL LEU ARG ARG ALA ASP GLY ASP PHE VAL          
SEQRES  10 C  179  ILE PRO ASP GLY THR ASP ILE PRO PRO ASP LEU LYS VAL          
SEQRES  11 C  179  LYS GLN ASP SER TYR ASN LYS ARG LEU GLN ALA THR HIS          
SEQRES  12 C  179  TYR THR ILE MET PRO ALA LYS PRO MET TYR ARG GLU VAL          
SEQRES  13 C  179  LEU MET GLY GLN LEU ASP ASN PHE VAL ARG ASN ALA ILE          
SEQRES  14 C  179  ARG ARG GLN TRP GLU LYS ALA ARG GLY LEU                      
SEQRES   1 D  179  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  179  LEU VAL PRO ARG GLY SER HIS MET MET SER TYR ASP TYR          
SEQRES   3 D  179  GLU LYS THR SER LEU THR LEU TYR ARG ALA VAL PHE LYS          
SEQRES   4 D  179  ALA ASN TYR ASP GLY ASP VAL GLY ARG TYR LEU HIS PRO          
SEQRES   5 D  179  ASP LYS GLU LEU ALA GLU ALA ALA GLU VAL ALA PRO LEU          
SEQRES   6 D  179  LEU HIS PRO THR PHE ASP SER PRO ASN THR PRO GLY VAL          
SEQRES   7 D  179  PRO ALA ARG ALA PRO ASP ILE VAL ALA GLY ARG ASP GLY          
SEQRES   8 D  179  LEU TYR ALA PRO ASP THR GLY GLY THR SER VAL PHE ASP          
SEQRES   9 D  179  ARG ALA GLY VAL LEU ARG ARG ALA ASP GLY ASP PHE VAL          
SEQRES  10 D  179  ILE PRO ASP GLY THR ASP ILE PRO PRO ASP LEU LYS VAL          
SEQRES  11 D  179  LYS GLN ASP SER TYR ASN LYS ARG LEU GLN ALA THR HIS          
SEQRES  12 D  179  TYR THR ILE MET PRO ALA LYS PRO MET TYR ARG GLU VAL          
SEQRES  13 D  179  LEU MET GLY GLN LEU ASP ASN PHE VAL ARG ASN ALA ILE          
SEQRES  14 D  179  ARG ARG GLN TRP GLU LYS ALA ARG GLY LEU                      
FORMUL   5  HOH   *74(H2 O)                                                     
HELIX    1   1 LYS A    4  ASP A   29  1                                  26    
HELIX    2   2 ASN A   33  TYR A   62  1                                  30    
HELIX    3   3 PRO A   67  ILE A   72  1                                   6    
HELIX    4   4 LYS B    4  ASP B   29  1                                  26    
HELIX    5   5 ASN B   33  GLY B   60  1                                  28    
HELIX    6   6 PRO B   67  ILE B   72  1                                   6    
HELIX    7   7 PHE C   18  TYR C   22  5                                   5    
HELIX    8   8 VAL C   26  LEU C   30  5                                   5    
HELIX    9   9 TYR C  133  ARG C  157  1                                  25    
HELIX   10  10 PHE D   18  TYR D   22  5                                   5    
HELIX   11  11 VAL D   26  HIS D   31  5                                   6    
HELIX   12  12 TYR D  133  ARG D  157  1                                  25    
SHEET    1  CA 4 TYR C   4  ASP C   5  0                                        
SHEET    2  CA 4 LEU C 108  ASN C 116 -1  O  VAL C 110   N  ASP C   5           
SHEET    3  CA 4 ALA C 121  PRO C 128 -1  O  ALA C 121   N  ASN C 116           
SHEET    4  CA 4 THR C  80  PHE C  83 -1  O  THR C  80   N  ILE C 126           
SHEET    1  CB 2 LEU C  13  VAL C  17  0                                        
SHEET    2  CB 2 GLY C  94  ILE C  98 -1  O  GLY C  94   N  VAL C  17           
SHEET    1  DA 4 TYR D   4  ASP D   5  0                                        
SHEET    2  DA 4 LEU D 108  ASN D 116 -1  O  VAL D 110   N  ASP D   5           
SHEET    3  DA 4 ALA D 121  PRO D 128 -1  O  ALA D 121   N  ASN D 116           
SHEET    4  DA 4 THR D  80  PHE D  83 -1  O  THR D  80   N  ILE D 126           
SHEET    1  DB 2 LEU D  13  VAL D  17  0                                        
SHEET    2  DB 2 GLY D  94  ILE D  98 -1  O  GLY D  94   N  VAL D  17           
CRYST1   37.725  103.138  114.642  90.00  90.00  90.00 P 21 21 21    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      0.026508  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009696  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008723        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system