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Database: PDB
Entry: 4BJQ
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HEADER    TRANSFERASE                             19-APR-13   4BJQ              
TITLE     CRYSTAL STRUCTURE OF E. COLI PENICILLIN BINDING PROTEIN 3,            
TITLE    2 DOMAIN V88-S165                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PENICILLIN BINDING PROTEIN TRANSPEPTIDASE DOMAIN PROTEIN;  
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 FRAGMENT: RESIDUES 88-165;                                           
COMPND   5 EC: 2.4.1.129;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE, TRANSPEPTIDASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.SAUVAGE,M.JORIS,R.HERMAN,F.KERFF,M.ROCABOY,P.CHARLIER               
REVDAT   2   11-JUN-14 4BJQ    1       JRNL                                     
REVDAT   1   07-MAY-14 4BJQ    0                                                
JRNL        AUTH   E.SAUVAGE,A.DEROUAUX,C.FRAIPONT,M.JORIS,R.HERMAN,M.ROCABOY,  
JRNL        AUTH 2 M.SCHLOESSER,J.DUMAS,F.KERFF,M.NGUYEN-DISTECHE,P.CHARLIER    
JRNL        TITL   CRYSTAL STRUCTURE OF PENICILLIN-BINDING PROTEIN 3 (PBP3)     
JRNL        TITL 2 FROM ESCHERICHIA COLI.                                       
JRNL        REF    PLOS ONE                      V.   9 98042 2014              
JRNL        REFN                   ISSN 1932-6203                               
JRNL        PMID   24875494                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0098042                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.41                          
REMARK   3   NUMBER OF REFLECTIONS             : 43316                          
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) : 0.21099                         
REMARK   3   R VALUE            (WORKING SET) : 0.20823                         
REMARK   3   FREE R VALUE                     : 0.26252                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2309                            
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) : 2.100                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.154                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3462                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.28                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.307                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 194                          
REMARK   3   BIN FREE R VALUE                    : 0.408                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4886                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 48                                      
REMARK   3   SOLVENT ATOMS            : 533                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.944                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01                                                
REMARK   3    B22 (A**2) : 0.03                                                 
REMARK   3    B33 (A**2) : -0.02                                                
REMARK   3    B12 (A**2) : -0.01                                                
REMARK   3    B13 (A**2) : 0.03                                                 
REMARK   3    B23 (A**2) : -0.01                                                
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.234         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.208         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.146         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.115        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5029 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6809 ; 1.195 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   613 ; 5.283 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   224 ;32.156 ;23.929       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   885 ;17.062 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;22.569 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   733 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3764 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3101 ; 0.525 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4958 ; 1.014 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1928 ; 1.614 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1851 ; 2.714 ; 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  : 8                                          
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    88        A   165                          
REMARK   3    ORIGIN FOR THE GROUP (A):  56.0660  40.9850 100.4800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0860 T22:   0.0755                                     
REMARK   3      T33:   0.0232 T12:   0.0105                                     
REMARK   3      T13:   0.0118 T23:  -0.0302                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7194 L22:   0.9689                                     
REMARK   3      L33:   0.0997 L12:  -0.3240                                     
REMARK   3      L13:   0.0014 L23:  -0.2785                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0024 S12:   0.0212 S13:   0.0478                       
REMARK   3      S21:  -0.0072 S22:   0.0163 S23:   0.0204                       
REMARK   3      S31:   0.0166 S32:   0.0091 S33:  -0.0187                       
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    88        B   165                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.3620 -18.9410  51.3770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0637 T22:   0.0979                                     
REMARK   3      T33:   0.0361 T12:   0.0167                                     
REMARK   3      T13:   0.0214 T23:  -0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7024 L22:   1.0675                                     
REMARK   3      L33:   0.2248 L12:  -0.4791                                     
REMARK   3      L13:  -0.2969 L23:   0.3076                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0165 S12:  -0.0098 S13:   0.0199                       
REMARK   3      S21:   0.0171 S22:   0.0131 S23:   0.0515                       
REMARK   3      S31:   0.0315 S32:   0.0089 S33:  -0.0296                       
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    88        C   165                          
REMARK   3    ORIGIN FOR THE GROUP (A):  65.9870  28.8880 108.6570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0858 T22:   0.0575                                     
REMARK   3      T33:   0.0501 T12:   0.0106                                     
REMARK   3      T13:   0.0092 T23:  -0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2049 L22:   0.6367                                     
REMARK   3      L33:   0.4935 L12:  -0.6208                                     
REMARK   3      L13:   0.3472 L23:  -0.5193                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0533 S12:  -0.1311 S13:  -0.0716                       
REMARK   3      S21:  -0.0618 S22:   0.0365 S23:   0.0348                       
REMARK   3      S31:   0.0643 S32:  -0.0077 S33:   0.0167                       
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    88        D   200                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.7580  18.2370  95.9820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0620 T22:   0.0683                                     
REMARK   3      T33:   0.0394 T12:  -0.0172                                     
REMARK   3      T13:   0.0307 T23:  -0.0174                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8003 L22:   0.4759                                     
REMARK   3      L33:   0.3821 L12:   0.2808                                     
REMARK   3      L13:  -0.1029 L23:   0.0911                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0850 S12:   0.0296 S13:  -0.0656                       
REMARK   3      S21:   0.0104 S22:   0.0340 S23:   0.0424                       
REMARK   3      S31:  -0.0465 S32:   0.0036 S33:   0.0509                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     5                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E    88        E   164                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.4220 -33.3060  42.9450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0601 T22:   0.1001                                     
REMARK   3      T33:   0.0376 T12:   0.0223                                     
REMARK   3      T13:   0.0250 T23:   0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2508 L22:   1.5049                                     
REMARK   3      L33:   0.5802 L12:  -0.0249                                     
REMARK   3      L13:  -0.1855 L23:   0.7240                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0408 S12:  -0.0241 S13:  -0.0217                       
REMARK   3      S21:  -0.1106 S22:   0.0121 S23:  -0.0794                       
REMARK   3      S31:  -0.0341 S32:   0.0016 S33:   0.0288                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     6                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F    88        F   165                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.7520  -4.8930  55.6080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0430 T22:   0.0939                                     
REMARK   3      T33:   0.0476 T12:  -0.0011                                     
REMARK   3      T13:   0.0230 T23:   0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8540 L22:   0.3355                                     
REMARK   3      L33:   0.8565 L12:   0.3914                                     
REMARK   3      L13:  -0.4015 L23:  -0.2780                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0539 S12:  -0.0087 S13:  -0.0277                       
REMARK   3      S21:   0.0026 S22:  -0.0446 S23:  -0.0820                       
REMARK   3      S31:  -0.0032 S32:  -0.0473 S33:  -0.0093                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     7                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G    88        G   164                          
REMARK   3    ORIGIN FOR THE GROUP (A):  61.7420 -10.8810  65.8230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0618 T22:   0.0964                                     
REMARK   3      T33:   0.0211 T12:  -0.0321                                     
REMARK   3      T13:  -0.0017 T23:   0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4798 L22:   0.7053                                     
REMARK   3      L33:   0.3284 L12:   0.7131                                     
REMARK   3      L13:  -0.4905 L23:  -0.0357                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1267 S12:  -0.0614 S13:  -0.1209                       
REMARK   3      S21:   0.0641 S22:  -0.1181 S23:  -0.0070                       
REMARK   3      S31:   0.0250 S32:  -0.0715 S33:  -0.0086                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     8                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    88        H   164                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.8160  28.5780  86.0090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0656 T22:   0.0885                                     
REMARK   3      T33:   0.0502 T12:  -0.0571                                     
REMARK   3      T13:   0.0188 T23:  -0.0157                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0825 L22:   2.5549                                     
REMARK   3      L33:   0.6096 L12:   1.1134                                     
REMARK   3      L13:  -0.5738 L23:  -0.9541                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1777 S12:   0.1125 S13:  -0.0729                       
REMARK   3      S21:  -0.1415 S22:   0.1635 S23:  -0.2469                       
REMARK   3      S31:   0.0405 S32:  -0.0291 S33:   0.0142                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 4BJQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-APR-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-56581.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-SEP-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM 315R)                 
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45669                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.10                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.5                               
REMARK 200  DATA REDUNDANCY                : 3.7                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.20                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.8                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.51                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.50                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELX                                                 
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9430 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.7 KCAL/MOL                        
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: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9180 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9340 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -56.04800            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9340 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       56.04800            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9330 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H                                  
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     SER E   165                                                      
REMARK 465     SER G   165                                                      
REMARK 465     SER H   165                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH2  ARG G   135     O    TYR H   138     2645     2.11            
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 F 131       64.04     64.00                                   
REMARK 500    ALA G 130      -73.75    -51.94                                   
REMARK 500    PHE H 136      117.78   -160.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS D1166                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1166                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1166                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E1165                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1166                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1167                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1167                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1167                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E1166                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4BJP   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF E. COLI PENICILLIN BINDING PROTEIN             
REMARK 900   3                                                                  
DBREF  4BJQ A   88   165  UNP    J2XFH0   J2XFH0_ECOLX    88    165             
DBREF  4BJQ B   88   165  UNP    J2XFH0   J2XFH0_ECOLX    88    165             
DBREF  4BJQ C   88   165  UNP    J2XFH0   J2XFH0_ECOLX    88    165             
DBREF  4BJQ D   88   165  UNP    J2XFH0   J2XFH0_ECOLX    88    165             
DBREF  4BJQ E   88   165  UNP    J2XFH0   J2XFH0_ECOLX    88    165             
DBREF  4BJQ F   88   165  UNP    J2XFH0   J2XFH0_ECOLX    88    165             
DBREF  4BJQ G   88   165  UNP    J2XFH0   J2XFH0_ECOLX    88    165             
DBREF  4BJQ H   88   165  UNP    J2XFH0   J2XFH0_ECOLX    88    165             
SEQRES   1 A   78  VAL LYS ALA ILE TRP ALA ASP PRO LYS GLU VAL HIS ASP          
SEQRES   2 A   78  ALA GLY GLY ILE SER VAL GLY ASP ARG TRP LYS ALA LEU          
SEQRES   3 A   78  ALA ASN ALA LEU ASN ILE PRO LEU ASP GLN LEU SER ALA          
SEQRES   4 A   78  ARG ILE ASN ALA ASN PRO LYS GLY ARG PHE ILE TYR LEU          
SEQRES   5 A   78  ALA ARG GLN VAL ASN PRO ASP MET ALA ASP TYR ILE LYS          
SEQRES   6 A   78  LYS LEU LYS LEU PRO GLY ILE HIS LEU ARG GLU GLU SER          
SEQRES   1 B   78  VAL LYS ALA ILE TRP ALA ASP PRO LYS GLU VAL HIS ASP          
SEQRES   2 B   78  ALA GLY GLY ILE SER VAL GLY ASP ARG TRP LYS ALA LEU          
SEQRES   3 B   78  ALA ASN ALA LEU ASN ILE PRO LEU ASP GLN LEU SER ALA          
SEQRES   4 B   78  ARG ILE ASN ALA ASN PRO LYS GLY ARG PHE ILE TYR LEU          
SEQRES   5 B   78  ALA ARG GLN VAL ASN PRO ASP MET ALA ASP TYR ILE LYS          
SEQRES   6 B   78  LYS LEU LYS LEU PRO GLY ILE HIS LEU ARG GLU GLU SER          
SEQRES   1 C   78  VAL LYS ALA ILE TRP ALA ASP PRO LYS GLU VAL HIS ASP          
SEQRES   2 C   78  ALA GLY GLY ILE SER VAL GLY ASP ARG TRP LYS ALA LEU          
SEQRES   3 C   78  ALA ASN ALA LEU ASN ILE PRO LEU ASP GLN LEU SER ALA          
SEQRES   4 C   78  ARG ILE ASN ALA ASN PRO LYS GLY ARG PHE ILE TYR LEU          
SEQRES   5 C   78  ALA ARG GLN VAL ASN PRO ASP MET ALA ASP TYR ILE LYS          
SEQRES   6 C   78  LYS LEU LYS LEU PRO GLY ILE HIS LEU ARG GLU GLU SER          
SEQRES   1 D   78  VAL LYS ALA ILE TRP ALA ASP PRO LYS GLU VAL HIS ASP          
SEQRES   2 D   78  ALA GLY GLY ILE SER VAL GLY ASP ARG TRP LYS ALA LEU          
SEQRES   3 D   78  ALA ASN ALA LEU ASN ILE PRO LEU ASP GLN LEU SER ALA          
SEQRES   4 D   78  ARG ILE ASN ALA ASN PRO LYS GLY ARG PHE ILE TYR LEU          
SEQRES   5 D   78  ALA ARG GLN VAL ASN PRO ASP MET ALA ASP TYR ILE LYS          
SEQRES   6 D   78  LYS LEU LYS LEU PRO GLY ILE HIS LEU ARG GLU GLU SER          
SEQRES   1 E   78  VAL LYS ALA ILE TRP ALA ASP PRO LYS GLU VAL HIS ASP          
SEQRES   2 E   78  ALA GLY GLY ILE SER VAL GLY ASP ARG TRP LYS ALA LEU          
SEQRES   3 E   78  ALA ASN ALA LEU ASN ILE PRO LEU ASP GLN LEU SER ALA          
SEQRES   4 E   78  ARG ILE ASN ALA ASN PRO LYS GLY ARG PHE ILE TYR LEU          
SEQRES   5 E   78  ALA ARG GLN VAL ASN PRO ASP MET ALA ASP TYR ILE LYS          
SEQRES   6 E   78  LYS LEU LYS LEU PRO GLY ILE HIS LEU ARG GLU GLU SER          
SEQRES   1 F   78  VAL LYS ALA ILE TRP ALA ASP PRO LYS GLU VAL HIS ASP          
SEQRES   2 F   78  ALA GLY GLY ILE SER VAL GLY ASP ARG TRP LYS ALA LEU          
SEQRES   3 F   78  ALA ASN ALA LEU ASN ILE PRO LEU ASP GLN LEU SER ALA          
SEQRES   4 F   78  ARG ILE ASN ALA ASN PRO LYS GLY ARG PHE ILE TYR LEU          
SEQRES   5 F   78  ALA ARG GLN VAL ASN PRO ASP MET ALA ASP TYR ILE LYS          
SEQRES   6 F   78  LYS LEU LYS LEU PRO GLY ILE HIS LEU ARG GLU GLU SER          
SEQRES   1 G   78  VAL LYS ALA ILE TRP ALA ASP PRO LYS GLU VAL HIS ASP          
SEQRES   2 G   78  ALA GLY GLY ILE SER VAL GLY ASP ARG TRP LYS ALA LEU          
SEQRES   3 G   78  ALA ASN ALA LEU ASN ILE PRO LEU ASP GLN LEU SER ALA          
SEQRES   4 G   78  ARG ILE ASN ALA ASN PRO LYS GLY ARG PHE ILE TYR LEU          
SEQRES   5 G   78  ALA ARG GLN VAL ASN PRO ASP MET ALA ASP TYR ILE LYS          
SEQRES   6 G   78  LYS LEU LYS LEU PRO GLY ILE HIS LEU ARG GLU GLU SER          
SEQRES   1 H   78  VAL LYS ALA ILE TRP ALA ASP PRO LYS GLU VAL HIS ASP          
SEQRES   2 H   78  ALA GLY GLY ILE SER VAL GLY ASP ARG TRP LYS ALA LEU          
SEQRES   3 H   78  ALA ASN ALA LEU ASN ILE PRO LEU ASP GLN LEU SER ALA          
SEQRES   4 H   78  ARG ILE ASN ALA ASN PRO LYS GLY ARG PHE ILE TYR LEU          
SEQRES   5 H   78  ALA ARG GLN VAL ASN PRO ASP MET ALA ASP TYR ILE LYS          
SEQRES   6 H   78  LYS LEU LYS LEU PRO GLY ILE HIS LEU ARG GLU GLU SER          
HET    TRS  D1166       8                                                       
HET    SO4  A1166       5                                                       
HET    SO4  C1166       5                                                       
HET    SO4  E1165       5                                                       
HET    SO4  B1166       5                                                       
HET    SO4  A1167       5                                                       
HET    SO4  B1167       5                                                       
HET    SO4  D1167       5                                                       
HET    SO4  E1166       5                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   2  SO4    8(O4 S 2-)                                                   
FORMUL   3  TRS    C4 H12 N O3 1+                                               
FORMUL   4  HOH   *533(H2 O)                                                    
HELIX    1   1 ASP A   94  ALA A  101  1                                   8    
HELIX    2   2 SER A  105  ASN A  118  1                                  14    
HELIX    3   3 PRO A  120  ALA A  130  1                                  11    
HELIX    4   4 ASN A  144  LEU A  154  1                                  11    
HELIX    5   5 ASP B   94  ALA B  101  1                                   8    
HELIX    6   6 SER B  105  ASN B  118  1                                  14    
HELIX    7   7 PRO B  120  ALA B  130  1                                  11    
HELIX    8   8 ASN B  144  LEU B  154  1                                  11    
HELIX    9   9 ASP C   94  ALA C  101  1                                   8    
HELIX   10  10 SER C  105  LEU C  117  1                                  13    
HELIX   11  11 PRO C  120  ALA C  130  1                                  11    
HELIX   12  12 ASN C  144  LEU C  154  1                                  11    
HELIX   13  13 ASP D   94  ALA D  101  1                                   8    
HELIX   14  14 SER D  105  ASN D  118  1                                  14    
HELIX   15  15 PRO D  120  ASN D  129  1                                  10    
HELIX   16  16 ASN D  144  LYS D  153  1                                  10    
HELIX   17  17 ASP E   94  ALA E  101  1                                   8    
HELIX   18  18 SER E  105  LEU E  117  1                                  13    
HELIX   19  19 PRO E  120  ALA E  130  1                                  11    
HELIX   20  20 ASN E  144  LEU E  154  1                                  11    
HELIX   21  21 ASP F   94  ALA F  101  1                                   8    
HELIX   22  22 SER F  105  LEU F  117  1                                  13    
HELIX   23  23 PRO F  120  ASN F  129  1                                  10    
HELIX   24  24 ASN F  144  LEU F  154  1                                  11    
HELIX   25  25 ASP G   94  ALA G  101  1                                   8    
HELIX   26  26 SER G  105  ASN G  118  1                                  14    
HELIX   27  27 PRO G  120  ALA G  130  1                                  11    
HELIX   28  28 ASN G  144  LEU G  154  1                                  11    
HELIX   29  29 ASP H   94  ALA H  101  1                                   8    
HELIX   30  30 SER H  105  LEU H  117  1                                  13    
HELIX   31  31 PRO H  120  ALA H  130  1                                  11    
HELIX   32  32 ASN H  144  LEU H  154  1                                  11    
SHEET    1  CA 3 ILE C 137  VAL C 143  0                                        
SHEET    2  CA 3 LYS A  89  ALA A  93 -1  O  LYS A  89   N  VAL C 143           
SHEET    3  CA 3 ILE C 159  GLU C 163 -1  O  HIS C 160   N  TRP A  92           
SHEET    1  AA 3 ILE A 137  VAL A 143  0                                        
SHEET    2  AA 3 LYS C  89  ALA C  93 -1  O  LYS C  89   N  VAL A 143           
SHEET    3  AA 3 ILE A 159  GLU A 163 -1  O  HIS A 160   N  TRP C  92           
SHEET    1  EA 3 ILE E 137  VAL E 143  0                                        
SHEET    2  EA 3 LYS B  89  ALA B  93 -1  O  LYS B  89   N  VAL E 143           
SHEET    3  EA 3 ILE E 159  GLU E 163 -1  O  HIS E 160   N  TRP B  92           
SHEET    1  BA 4 ILE B 159  GLU B 163  0                                        
SHEET    2  BA 4 LYS E  89  ALA E  93 -1  O  ALA E  90   N  ARG B 162           
SHEET    3  BA 4 ILE B 137  VAL B 143 -1  O  ILE B 137   N  ALA E  93           
SHEET    4  BA 4 GLU F 163  GLU F 164 -1  O  GLU F 163   N  ARG B 141           
SHEET    1  HA 3 ILE H 137  VAL H 143  0                                        
SHEET    2  HA 3 LYS D  89  ALA D  93 -1  O  LYS D  89   N  VAL H 143           
SHEET    3  HA 3 ILE H 159  GLU H 163 -1  O  HIS H 160   N  TRP D  92           
SHEET    1  DA 3 ILE D 137  ALA D 140  0                                        
SHEET    2  DA 3 LYS H  89  ALA H  93 -1  O  ILE H  91   N  LEU D 139           
SHEET    3  DA 3 ILE D 159  GLU D 163 -1  O  HIS D 160   N  TRP H  92           
SITE     1 AC1  6 ASN A 144  HOH A2060  LYS D 152  HIS D 160                    
SITE     2 AC1  6 LEU D 161  HOH D2071                                          
SITE     1 AC2  6 GLY A 103  ILE A 104  SER A 105  ARG A 109                    
SITE     2 AC2  6 HOH A2021  ASN C 129                                          
SITE     1 AC3  5 ASN A 129  GLY C 103  ILE C 104  SER C 105                    
SITE     2 AC3  5 ARG C 109                                                     
SITE     1 AC4  6 ASN B 129  GLY E 103  ILE E 104  SER E 105                    
SITE     2 AC4  6 ARG E 109  HOH E2006                                          
SITE     1 AC5  1 ARG B 141                                                     
SITE     1 AC6  1 ARG A 141                                                     
SITE     1 AC7  5 GLY B 103  ILE B 104  SER B 105  ARG B 109                    
SITE     2 AC7  5 ASN E 129                                                     
SITE     1 AC8  6 ARG C 141  ALA D 140  ARG D 141  HOH D2049                    
SITE     2 AC8  6 HOH D2050  LYS E 111                                          
SITE     1 AC9  5 LYS C 111  ARG E 141  ALA F 140  ARG F 141                    
SITE     2 AC9  5 HOH F2045                                                     
CRYST1   56.048   55.959   82.285  89.13  76.49  65.99 P 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      0.017842 -0.007947 -0.005022        0.00000                         
SCALE2      0.000000  0.019563  0.001766        0.00000                         
SCALE3      0.000000  0.000000  0.012550        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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