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Database: PDB
Entry: 4FGE
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Original site: 4FGE 
HEADER    HYDROLASE                               04-JUN-12   4FGE              
TITLE     STRUCTURE OF THE EFFECTOR PROTEIN TSE1 FROM PSEUDOMONAS AERUGINOSA    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TSE1;                                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 208964;                                              
SOURCE   4 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;                
SOURCE   5 GENE: PA1844;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIL;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET21D                                
KEYWDS    N1PC/P60 SUPERFAMILY, PEPTIDOGLYCAN HYDROLASE, CYTOSOL, HYDROLASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.BENZ,C.SENDLMEIER,T.R.M.BARENDS,A.MEINHART                          
REVDAT   3   25-JUL-12 4FGE    1       JRNL                                     
REVDAT   2   18-JUL-12 4FGE    1       JRNL                                     
REVDAT   1   20-JUN-12 4FGE    0                                                
JRNL        AUTH   J.BENZ,C.SENDLMEIER,T.R.BARENDS,A.MEINHART                   
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE EFFECTOR - IMMUNITY SYSTEM      
JRNL        TITL 2 TSE1/TSI1 FROM PSEUDOMONAS AERUGINOSA.                       
JRNL        REF    PLOS ONE                      V.   7 40453 2012              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   22792331                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0040453                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.62                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 60001                          
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) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3158                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4387                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2530                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 230                          
REMARK   3   BIN FREE R VALUE                    : 0.2840                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4437                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 330                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.02000                                              
REMARK   3    B22 (A**2) : 0.41000                                              
REMARK   3    B33 (A**2) : -0.21000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.67000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.105         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.100         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.069         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.075         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4638 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6302 ; 0.995 ; 1.944       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   624 ; 5.114 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   191 ;31.540 ;24.136       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   749 ;12.427 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;19.426 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   678 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3552 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2122 ; 0.195 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3215 ; 0.297 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   288 ; 0.125 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    57 ; 0.236 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    20 ; 0.112 ; 0.200       
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):  2982 ; 0.452 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4739 ; 0.826 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1656 ; 1.372 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1547 ; 2.218 ; 4.500       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A   149                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.5657   8.0555   7.7846              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1851 T22:  -0.1481                                     
REMARK   3      T33:  -0.1006 T12:   0.0111                                     
REMARK   3      T13:  -0.0032 T23:   0.0266                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1316 L22:   2.3085                                     
REMARK   3      L33:   3.4012 L12:  -0.3984                                     
REMARK   3      L13:  -0.7523 L23:  -0.2468                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0341 S12:   0.2960 S13:   0.4535                       
REMARK   3      S21:  -0.1030 S22:   0.0454 S23:   0.0491                       
REMARK   3      S31:  -0.3402 S32:  -0.1023 S33:  -0.0795                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     4        B   149                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2487 -28.4497  16.9321              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1089 T22:  -0.1936                                     
REMARK   3      T33:  -0.1306 T12:  -0.0253                                     
REMARK   3      T13:   0.0201 T23:   0.0157                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9853 L22:   5.0192                                     
REMARK   3      L33:   4.3709 L12:   0.5941                                     
REMARK   3      L13:  -0.5548 L23:  -1.0273                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1186 S12:  -0.0285 S13:  -0.1268                       
REMARK   3      S21:  -0.0559 S22:  -0.0549 S23:   0.0968                       
REMARK   3      S31:   0.0675 S32:   0.0661 S33:  -0.0637                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     3        C   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5071  -4.3796  26.0948              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1896 T22:  -0.1566                                     
REMARK   3      T33:  -0.1810 T12:  -0.0010                                     
REMARK   3      T13:  -0.0049 T23:  -0.0123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7856 L22:   2.7184                                     
REMARK   3      L33:   3.0802 L12:  -0.0250                                     
REMARK   3      L13:  -0.2838 L23:   0.0037                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1584 S12:  -0.2348 S13:  -0.1281                       
REMARK   3      S21:   0.2733 S22:   0.0261 S23:  -0.0592                       
REMARK   3      S31:   0.1805 S32:  -0.0047 S33:   0.1324                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     4        D   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.2518  -9.1727 -11.6372              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0657 T22:  -0.0887                                     
REMARK   3      T33:  -0.1960 T12:   0.0098                                     
REMARK   3      T13:   0.0078 T23:   0.0179                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0174 L22:   4.8624                                     
REMARK   3      L33:   4.6440 L12:  -0.4136                                     
REMARK   3      L13:  -0.7513 L23:   0.1996                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0743 S12:   0.2928 S13:  -0.1319                       
REMARK   3      S21:  -0.4300 S22:  -0.0209 S23:   0.0279                       
REMARK   3      S31:   0.1778 S32:   0.0310 S33:  -0.0534                       
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 4FGE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072868.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9796                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63172                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.130                              
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   (%): 41.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM KSCN, 1% (V/V) MPD, AND 20% (W/   
REMARK 280  V) PEG 3350, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       50.19000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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 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 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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     ASP A     2                                                      
REMARK 465     ALA A   153                                                      
REMARK 465     SER A   154                                                      
REMARK 465     ALA A   155                                                      
REMARK 465     ALA A   156                                                      
REMARK 465     ALA A   157                                                      
REMARK 465     LEU A   158                                                      
REMARK 465     GLU A   159                                                      
REMARK 465     HIS A   160                                                      
REMARK 465     HIS A   161                                                      
REMARK 465     HIS A   162                                                      
REMARK 465     HIS A   163                                                      
REMARK 465     HIS A   164                                                      
REMARK 465     HIS A   165                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     LEU B   150                                                      
REMARK 465     PRO B   151                                                      
REMARK 465     ARG B   152                                                      
REMARK 465     ALA B   153                                                      
REMARK 465     SER B   154                                                      
REMARK 465     ALA B   155                                                      
REMARK 465     ALA B   156                                                      
REMARK 465     ALA B   157                                                      
REMARK 465     LEU B   158                                                      
REMARK 465     GLU B   159                                                      
REMARK 465     HIS B   160                                                      
REMARK 465     HIS B   161                                                      
REMARK 465     HIS B   162                                                      
REMARK 465     HIS B   163                                                      
REMARK 465     HIS B   164                                                      
REMARK 465     HIS B   165                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ASP C     2                                                      
REMARK 465     ARG C   152                                                      
REMARK 465     ALA C   153                                                      
REMARK 465     SER C   154                                                      
REMARK 465     ALA C   155                                                      
REMARK 465     ALA C   156                                                      
REMARK 465     ALA C   157                                                      
REMARK 465     LEU C   158                                                      
REMARK 465     GLU C   159                                                      
REMARK 465     HIS C   160                                                      
REMARK 465     HIS C   161                                                      
REMARK 465     HIS C   162                                                      
REMARK 465     HIS C   163                                                      
REMARK 465     HIS C   164                                                      
REMARK 465     HIS C   165                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ASP D     2                                                      
REMARK 465     PRO D   151                                                      
REMARK 465     ARG D   152                                                      
REMARK 465     ALA D   153                                                      
REMARK 465     SER D   154                                                      
REMARK 465     ALA D   155                                                      
REMARK 465     ALA D   156                                                      
REMARK 465     ALA D   157                                                      
REMARK 465     LEU D   158                                                      
REMARK 465     GLU D   159                                                      
REMARK 465     HIS D   160                                                      
REMARK 465     HIS D   161                                                      
REMARK 465     HIS D   162                                                      
REMARK 465     HIS D   163                                                      
REMARK 465     HIS D   164                                                      
REMARK 465     HIS D   165                                                      
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    THR A  88      -64.25   -103.55                                   
REMARK 500    LYS A 104      -41.86   -139.70                                   
REMARK 500    THR B  88      -60.76   -104.11                                   
REMARK 500    GLN B 103       17.16     59.76                                   
REMARK 500    LYS B 104      -41.34   -140.29                                   
REMARK 500    CYS B 148       46.86   -107.49                                   
REMARK 500    GLN C 103       43.36     35.44                                   
REMARK 500    LYS C 104      -40.68   -149.13                                   
REMARK 500    GLN C 121       41.40   -107.13                                   
REMARK 500    LYS D 104      -43.12   -146.14                                   
REMARK 500    GLN D 121       40.21   -108.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 394        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH D 356        DISTANCE =  5.07 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4FGD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FGI   RELATED DB: PDB                                   
DBREF  4FGE A    1   154  UNP    Q9I2Q1   Q9I2Q1_PSEAE     1    154             
DBREF  4FGE B    1   154  UNP    Q9I2Q1   Q9I2Q1_PSEAE     1    154             
DBREF  4FGE C    1   154  UNP    Q9I2Q1   Q9I2Q1_PSEAE     1    154             
DBREF  4FGE D    1   154  UNP    Q9I2Q1   Q9I2Q1_PSEAE     1    154             
SEQADV 4FGE ALA A  155  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE ALA A  156  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE ALA A  157  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE LEU A  158  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE GLU A  159  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS A  160  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS A  161  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS A  162  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS A  163  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS A  164  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS A  165  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE ALA B  155  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE ALA B  156  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE ALA B  157  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE LEU B  158  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE GLU B  159  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS B  160  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS B  161  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS B  162  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS B  163  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS B  164  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS B  165  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE ALA C  155  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE ALA C  156  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE ALA C  157  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE LEU C  158  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE GLU C  159  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS C  160  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS C  161  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS C  162  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS C  163  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS C  164  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS C  165  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE ALA D  155  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE ALA D  156  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE ALA D  157  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE LEU D  158  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE GLU D  159  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS D  160  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS D  161  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS D  162  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS D  163  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS D  164  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGE HIS D  165  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQRES   1 A  165  MET ASP SER LEU ASP GLN CYS ILE VAL ASN ALA CYS LYS          
SEQRES   2 A  165  ASN SER TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN          
SEQRES   3 A  165  LYS ASP ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA          
SEQRES   4 A  165  GLU LEU GLY VAL PRO MET PRO ARG GLY ASN ALA ASN ALA          
SEQRES   5 A  165  MET VAL ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA          
SEQRES   6 A  165  SER GLY ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE          
SEQRES   7 A  165  LEU VAL ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS          
SEQRES   8 A  165  VAL ALA VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS          
SEQRES   9 A  165  TYR PRO MET CYS TRP CYS GLY SER ILE ALA GLY ALA VAL          
SEQRES  10 A  165  GLY GLN SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP          
SEQRES  11 A  165  ASN ARG THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR          
SEQRES  12 A  165  SER LEU ALA SER CYS SER LEU PRO ARG ALA SER ALA ALA          
SEQRES  13 A  165  ALA LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 B  165  MET ASP SER LEU ASP GLN CYS ILE VAL ASN ALA CYS LYS          
SEQRES   2 B  165  ASN SER TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN          
SEQRES   3 B  165  LYS ASP ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA          
SEQRES   4 B  165  GLU LEU GLY VAL PRO MET PRO ARG GLY ASN ALA ASN ALA          
SEQRES   5 B  165  MET VAL ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA          
SEQRES   6 B  165  SER GLY ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE          
SEQRES   7 B  165  LEU VAL ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS          
SEQRES   8 B  165  VAL ALA VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS          
SEQRES   9 B  165  TYR PRO MET CYS TRP CYS GLY SER ILE ALA GLY ALA VAL          
SEQRES  10 B  165  GLY GLN SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP          
SEQRES  11 B  165  ASN ARG THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR          
SEQRES  12 B  165  SER LEU ALA SER CYS SER LEU PRO ARG ALA SER ALA ALA          
SEQRES  13 B  165  ALA LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 C  165  MET ASP SER LEU ASP GLN CYS ILE VAL ASN ALA CYS LYS          
SEQRES   2 C  165  ASN SER TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN          
SEQRES   3 C  165  LYS ASP ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA          
SEQRES   4 C  165  GLU LEU GLY VAL PRO MET PRO ARG GLY ASN ALA ASN ALA          
SEQRES   5 C  165  MET VAL ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA          
SEQRES   6 C  165  SER GLY ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE          
SEQRES   7 C  165  LEU VAL ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS          
SEQRES   8 C  165  VAL ALA VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS          
SEQRES   9 C  165  TYR PRO MET CYS TRP CYS GLY SER ILE ALA GLY ALA VAL          
SEQRES  10 C  165  GLY GLN SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP          
SEQRES  11 C  165  ASN ARG THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR          
SEQRES  12 C  165  SER LEU ALA SER CYS SER LEU PRO ARG ALA SER ALA ALA          
SEQRES  13 C  165  ALA LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 D  165  MET ASP SER LEU ASP GLN CYS ILE VAL ASN ALA CYS LYS          
SEQRES   2 D  165  ASN SER TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN          
SEQRES   3 D  165  LYS ASP ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA          
SEQRES   4 D  165  GLU LEU GLY VAL PRO MET PRO ARG GLY ASN ALA ASN ALA          
SEQRES   5 D  165  MET VAL ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA          
SEQRES   6 D  165  SER GLY ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE          
SEQRES   7 D  165  LEU VAL ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS          
SEQRES   8 D  165  VAL ALA VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS          
SEQRES   9 D  165  TYR PRO MET CYS TRP CYS GLY SER ILE ALA GLY ALA VAL          
SEQRES  10 D  165  GLY GLN SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP          
SEQRES  11 D  165  ASN ARG THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR          
SEQRES  12 D  165  SER LEU ALA SER CYS SER LEU PRO ARG ALA SER ALA ALA          
SEQRES  13 D  165  ALA LEU GLU HIS HIS HIS HIS HIS HIS                          
HET     CL  A 201       1                                                       
HET     CL  A 202       1                                                       
HET    SCN  A 203       3                                                       
HET    SCN  B 201       3                                                       
HET    GOL  B 202       6                                                       
HET     CL  C 201       2                                                       
HET    GOL  D 201       6                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     SCN THIOCYANATE ION                                                  
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5   CL    3(CL 1-)                                                     
FORMUL   7  SCN    2(C N S 1-)                                                  
FORMUL   9  GOL    2(C3 H8 O3)                                                  
FORMUL  12  HOH   *330(H2 O)                                                    
HELIX    1   1 ASP A    5  TRP A   16  1                                  12    
HELIX    2   2 PRO A   25  ASP A   28  5                                   4    
HELIX    3   3 ASN A   29  GLY A   42  1                                  14    
HELIX    4   4 ASN A   49  TRP A   61  1                                  13    
HELIX    5   5 SER A   66  GLN A   76  1                                  11    
HELIX    6   6 ARG A  102  LYS A  104  5                                   3    
HELIX    7   7 GLY A  115  GLN A  119  5                                   5    
HELIX    8   8 GLY A  127  VAL A  129  5                                   3    
HELIX    9   9 THR A  133  LEU A  138  5                                   6    
HELIX   10  10 ASP B    5  TRP B   16  1                                  12    
HELIX   11  11 PRO B   25  ASP B   28  5                                   4    
HELIX   12  12 ASN B   29  GLY B   42  1                                  14    
HELIX   13  13 ASN B   49  TRP B   61  1                                  13    
HELIX   14  14 SER B   66  GLN B   76  1                                  11    
HELIX   15  15 ARG B  102  LYS B  104  5                                   3    
HELIX   16  16 GLY B  115  GLN B  119  5                                   5    
HELIX   17  17 GLY B  127  VAL B  129  5                                   3    
HELIX   18  18 THR B  133  ARG B  137  5                                   5    
HELIX   19  19 ASP C    5  ASP C   17  1                                  13    
HELIX   20  20 PRO C   25  ASP C   28  5                                   4    
HELIX   21  21 ASN C   29  GLY C   42  1                                  14    
HELIX   22  22 ASN C   49  TRP C   61  1                                  13    
HELIX   23  23 SER C   66  GLN C   76  1                                  11    
HELIX   24  24 ARG C  102  LYS C  104  5                                   3    
HELIX   25  25 GLY C  115  GLN C  119  5                                   5    
HELIX   26  26 GLY C  127  VAL C  129  5                                   3    
HELIX   27  27 THR C  133  ARG C  137  5                                   5    
HELIX   28  28 ASP D    5  TRP D   16  1                                  12    
HELIX   29  29 PRO D   25  ASP D   28  5                                   4    
HELIX   30  30 ASN D   29  GLY D   42  1                                  14    
HELIX   31  31 ASN D   49  TRP D   61  1                                  13    
HELIX   32  32 SER D   66  GLN D   76  1                                  11    
HELIX   33  33 ARG D  102  LYS D  104  5                                   3    
HELIX   34  34 GLY D  115  GLN D  119  5                                   5    
HELIX   35  35 VAL D  126  TRP D  130  1                                   5    
HELIX   36  36 THR D  133  ARG D  137  5                                   5    
SHEET    1   A 6 THR A  62  LYS A  63  0                                        
SHEET    2   A 6 ASN A 139  VAL A 142 -1  O  VAL A 142   N  THR A  62           
SHEET    3   A 6 VAL A  80  LEU A  84 -1  N  GLY A  83   O  ASN A 139           
SHEET    4   A 6 HIS A  91  TYR A 101 -1  O  VAL A  95   N  VAL A  80           
SHEET    5   A 6 TYR A 105  CYS A 110 -1  O  TYR A 105   N  TYR A 101           
SHEET    6   A 6 SER A 120  SER A 125 -1  O  SER A 120   N  CYS A 110           
SHEET    1   B 6 THR B  62  LEU B  64  0                                        
SHEET    2   B 6 ASN B 139  VAL B 142 -1  O  TYR B 140   N  LEU B  64           
SHEET    3   B 6 VAL B  80  LEU B  84 -1  N  ILE B  81   O  TYR B 141           
SHEET    4   B 6 HIS B  91  TYR B 101 -1  O  VAL B  95   N  VAL B  80           
SHEET    5   B 6 TYR B 105  CYS B 110 -1  O  TYR B 105   N  TYR B 101           
SHEET    6   B 6 SER B 120  SER B 125 -1  O  SER B 120   N  CYS B 110           
SHEET    1   C 6 THR C  62  LEU C  64  0                                        
SHEET    2   C 6 ASN C 139  VAL C 142 -1  O  TYR C 140   N  LEU C  64           
SHEET    3   C 6 VAL C  80  LEU C  84 -1  N  GLY C  83   O  ASN C 139           
SHEET    4   C 6 HIS C  91  TYR C 101 -1  O  VAL C  95   N  VAL C  80           
SHEET    5   C 6 TYR C 105  CYS C 110 -1  O  TYR C 105   N  TYR C 101           
SHEET    6   C 6 SER C 120  SER C 125 -1  O  SER C 120   N  CYS C 110           
SHEET    1   D 6 THR D  62  LYS D  63  0                                        
SHEET    2   D 6 ASN D 139  VAL D 142 -1  O  VAL D 142   N  THR D  62           
SHEET    3   D 6 VAL D  80  LEU D  84 -1  N  ILE D  81   O  TYR D 141           
SHEET    4   D 6 HIS D  91  TYR D 101 -1  O  VAL D  95   N  VAL D  80           
SHEET    5   D 6 TYR D 105  CYS D 110 -1  O  TYR D 105   N  TYR D 101           
SHEET    6   D 6 SER D 120  SER D 125 -1  O  SER D 120   N  CYS D 110           
SITE     1 AC1  4 ASN A  49  TYR A  89  HOH A 305  ALA C  22                    
SITE     1 AC2  2 LYS A  73  SER A 144                                          
SITE     1 AC3  6 SER A 120  GLN A 121  LEU A 123  LYS A 124                    
SITE     2 AC3  6 GLN D 121  LEU D 123                                          
SITE     1 AC4  4 SER B 120  GLN B 121  LEU B 123  GLN C 121                    
SITE     1 AC5  8 ASN B  29  CYS B  30  SER B  31  ASN B  49                    
SITE     2 AC5  8 ALA B  50  ILE B 113  HOH B 304  HOH B 305                    
SITE     1 AC6  7 LEU A  21  ALA A  22  SER C  31  ASN C  49                    
SITE     2 AC6  7 ALA C  50  TYR C  89  HOH C 303                               
SITE     1 AC7  8 ASN D  29  SER D  31  ASN D  49  ALA D  50                    
SITE     2 AC7  8 TYR D  89  ILE D 113  HOH D 302  HOH D 306                    
CRYST1   48.240  100.380   62.180  90.00  99.35  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020730  0.000000  0.003413        0.00000                         
SCALE2      0.000000  0.009962  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016299        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system