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Entry: 3FNM
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HEADER    TRANSFERASE                             25-DEC-08   3FNM              
TITLE     CRYSTAL STRUCTURE OF ACIVICIN-INHIBITED GAMMA-GLUTAMYLTRANSPEPTIDASE  
TITLE    2 REVEALS CRITICAL ROLES FOR ITS C-TERMINUS IN AUTOPROCESSING AND      
TITLE    3 CATALYSIS                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GAMMA-GLUTAMYLTRANSPEPTIDASE (GGT) LARGE SUBUNIT;          
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: RESIDUES 25-379;                                           
COMPND   5 EC: 2.3.2.2;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: GAMMA-GLUTAMYLTRANSPEPTIDASE (GGT) SMALL SUBUNIT;          
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: RESIDUES 380-567;                                          
COMPND  11 EC: 2.3.2.2;                                                         
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;                            
SOURCE   3 ORGANISM_COMMON: CAMPYLOBACTER PYLORI;                               
SOURCE   4 ORGANISM_TAXID: 210;                                                 
SOURCE   5 GENE: HP_1118;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;                            
SOURCE  13 ORGANISM_COMMON: CAMPYLOBACTER PYLORI;                               
SOURCE  14 ORGANISM_TAXID: 210;                                                 
SOURCE  15 GENE: HP_1118;                                                       
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: ROSETTA2;                                  
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    NTN-HYDROLASE, GLUTAMYLTRANSPEPTIDASE, TRANSFERASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.WILLIAMS,S.CULLATI,A.SAND,E.I.BITEROVA,J.J.BARYCKI                  
REVDAT   4   01-NOV-17 3FNM    1       REMARK                                   
REVDAT   3   09-MAY-12 3FNM    1       COMPND                                   
REVDAT   2   13-JUL-11 3FNM    1       VERSN                                    
REVDAT   1   19-MAY-09 3FNM    0                                                
JRNL        AUTH   K.WILLIAMS,S.CULLATI,A.SAND,E.I.BITEROVA,J.J.BARYCKI         
JRNL        TITL   CRYSTAL STRUCTURE OF ACIVICIN-INHIBITED                      
JRNL        TITL 2 GAMMA-GLUTAMYLTRANSPEPTIDASE REVEALS CRITICAL ROLES FOR ITS  
JRNL        TITL 3 C-TERMINUS IN AUTOPROCESSING AND CATALYSIS.                  
JRNL        REF    BIOCHEMISTRY                  V.  48  2459 2009              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   19256527                                                     
JRNL        DOI    10.1021/BI8014955                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 29.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 99222                          
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 10906                           
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) : 7106                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.53                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 720                          
REMARK   3   BIN FREE R VALUE                    : 0.2780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8086                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 534                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.69000                                              
REMARK   3    B22 (A**2) : -1.35000                                             
REMARK   3    B33 (A**2) : 0.73000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.11000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.116         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.111         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.077         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.588         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.958                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8310 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11236 ; 1.500 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1074 ; 6.339 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   333 ;36.691 ;25.285       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1449 ;13.591 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;14.767 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1256 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6214 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4181 ; 0.201 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5811 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   595 ; 0.115 ; 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):    48 ; 0.165 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    25 ; 0.167 ; 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):  5453 ; 0.794 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8522 ; 1.162 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3228 ; 2.066 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2714 ; 3.051 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
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    31        A   104                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.2830 -14.8810  30.9490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0062 T22:   0.1654                                     
REMARK   3      T33:  -0.0034 T12:  -0.0667                                     
REMARK   3      T13:  -0.0550 T23:  -0.0353                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1878 L22:   1.2153                                     
REMARK   3      L33:   1.5811 L12:  -0.1282                                     
REMARK   3      L13:   0.5036 L23:  -0.3361                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0364 S12:   0.0309 S13:  -0.2859                       
REMARK   3      S21:  -0.1485 S22:   0.0976 S23:   0.0871                       
REMARK   3      S31:   0.2896 S32:  -0.2733 S33:  -0.1340                       
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 :   A   105        A   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.4210 -12.9930  39.6230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0060 T22:   0.1746                                     
REMARK   3      T33:   0.0199 T12:  -0.0167                                     
REMARK   3      T13:  -0.0404 T23:  -0.0417                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7225 L22:   1.3828                                     
REMARK   3      L33:   1.8699 L12:  -0.5865                                     
REMARK   3      L13:  -0.0306 L23:   0.2835                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0461 S12:  -0.0675 S13:  -0.0837                       
REMARK   3      S21:  -0.0443 S22:   0.1494 S23:  -0.1951                       
REMARK   3      S31:   0.0991 S32:   0.2300 S33:  -0.1034                       
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 :   A   189        A   354                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.2740  -3.9390  39.5550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0106 T22:   0.1643                                     
REMARK   3      T33:  -0.0599 T12:  -0.0151                                     
REMARK   3      T13:  -0.0598 T23:  -0.0231                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5417 L22:   0.8262                                     
REMARK   3      L33:   1.2302 L12:  -0.1581                                     
REMARK   3      L13:   0.0422 L23:  -0.2766                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0524 S12:  -0.0522 S13:  -0.0707                       
REMARK   3      S21:   0.0720 S22:   0.0988 S23:  -0.0085                       
REMARK   3      S31:  -0.0531 S32:  -0.0301 S33:  -0.0465                       
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 :   A   355        A   372                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.8750  24.4020  37.5860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2722 T22:   0.1936                                     
REMARK   3      T33:   0.0237 T12:   0.0361                                     
REMARK   3      T13:  -0.1047 T23:  -0.0410                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0723 L22:   3.6179                                     
REMARK   3      L33:   4.9675 L12:   1.5822                                     
REMARK   3      L13:  -1.1287 L23:   0.5146                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0674 S12:   0.0317 S13:   0.3312                       
REMARK   3      S21:  -0.0769 S22:   0.0155 S23:   0.2937                       
REMARK   3      S31:  -0.8891 S32:  -0.4993 S33:   0.0519                       
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 :   B   381        B   428                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.0130  -9.4430  38.0720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0122 T22:   0.1871                                     
REMARK   3      T33:   0.0316 T12:  -0.0177                                     
REMARK   3      T13:  -0.0385 T23:  -0.0416                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2313 L22:   0.9593                                     
REMARK   3      L33:   1.9351 L12:  -0.4527                                     
REMARK   3      L13:  -0.1470 L23:  -0.0795                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0009 S12:  -0.1443 S13:  -0.1358                       
REMARK   3      S21:   0.0233 S22:   0.0918 S23:  -0.0971                       
REMARK   3      S31:   0.0407 S32:   0.0185 S33:  -0.0928                       
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 :   B   429        B   548                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.4150   6.2750  29.5810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0606 T22:   0.1824                                     
REMARK   3      T33:  -0.0442 T12:  -0.0185                                     
REMARK   3      T13:  -0.0443 T23:  -0.0284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6152 L22:   0.7511                                     
REMARK   3      L33:   1.3336 L12:   0.0299                                     
REMARK   3      L13:   0.0830 L23:  -0.4767                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0595 S12:   0.0491 S13:  -0.0257                       
REMARK   3      S21:   0.0284 S22:   0.0832 S23:  -0.0011                       
REMARK   3      S31:  -0.2040 S32:  -0.0956 S33:  -0.0238                       
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 :   B   549        B   567                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.5850  -6.3670  20.6570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1948 T22:   0.1799                                     
REMARK   3      T33:   0.1584 T12:  -0.0090                                     
REMARK   3      T13:  -0.0648 T23:  -0.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6366 L22:   4.8881                                     
REMARK   3      L33:   6.5144 L12:   2.5958                                     
REMARK   3      L13:  -0.2108 L23:   1.9018                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2331 S12:   0.9392 S13:  -0.1691                       
REMARK   3      S21:  -0.1871 S22:   0.4874 S23:   0.2283                       
REMARK   3      S31:   0.1570 S32:  -0.2946 S33:  -0.2544                       
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 :   C    32        C   162                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.6460  -8.6010 -14.8900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0256 T22:   0.1346                                     
REMARK   3      T33:   0.0068 T12:   0.0158                                     
REMARK   3      T13:  -0.0274 T23:   0.0082                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0935 L22:   1.3360                                     
REMARK   3      L33:   1.4676 L12:   0.2971                                     
REMARK   3      L13:  -0.2787 L23:  -0.1548                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0437 S12:   0.0631 S13:  -0.1666                       
REMARK   3      S21:  -0.1501 S22:   0.0104 S23:  -0.0281                       
REMARK   3      S31:   0.1088 S32:   0.1327 S33:   0.0333                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   163        C   256                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.0930 -15.1570 -14.9140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0078 T22:   0.0973                                     
REMARK   3      T33:   0.0135 T12:  -0.0403                                     
REMARK   3      T13:  -0.0735 T23:  -0.0083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3692 L22:   2.2398                                     
REMARK   3      L33:   2.3834 L12:   0.5937                                     
REMARK   3      L13:  -0.6592 L23:  -0.5201                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0994 S12:   0.1319 S13:  -0.0891                       
REMARK   3      S21:  -0.1970 S22:   0.1148 S23:   0.2201                       
REMARK   3      S31:   0.2866 S32:  -0.2479 S33:  -0.0154                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   257        C   372                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.7710  15.3360 -11.2320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0281 T22:   0.1611                                     
REMARK   3      T33:  -0.0326 T12:  -0.0443                                     
REMARK   3      T13:  -0.0265 T23:   0.0113                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6320 L22:   1.0356                                     
REMARK   3      L33:   0.9137 L12:   0.0417                                     
REMARK   3      L13:  -0.1457 L23:   0.2080                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0025 S12:  -0.0071 S13:   0.0715                       
REMARK   3      S21:  -0.1697 S22:   0.0713 S23:  -0.1510                       
REMARK   3      S31:  -0.2326 S32:   0.2090 S33:  -0.0737                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   373        C   379                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.3250  24.5830 -26.3890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2579 T22:   0.2588                                     
REMARK   3      T33:   0.2607 T12:  -0.0021                                     
REMARK   3      T13:  -0.0004 T23:   0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.4662 L22:   8.0942                                     
REMARK   3      L33:  63.4707 L12:   7.6837                                     
REMARK   3      L13:   8.2747 L23: -13.1145                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7914 S12:   0.5271 S13:   0.6178                       
REMARK   3      S21:  -0.9442 S22:   0.0523 S23:   0.2635                       
REMARK   3      S31:   2.6617 S32:  -1.2779 S33:   0.7390                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   381        D   458                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.6880  -0.1730 -16.0680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0306 T22:   0.1306                                     
REMARK   3      T33:  -0.0262 T12:   0.0075                                     
REMARK   3      T13:  -0.0513 T23:   0.0087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8068 L22:   1.2045                                     
REMARK   3      L33:   1.1028 L12:   0.3033                                     
REMARK   3      L13:  -0.3066 L23:  -0.0864                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0294 S12:   0.0521 S13:  -0.0572                       
REMARK   3      S21:  -0.1740 S22:   0.0333 S23:   0.0204                       
REMARK   3      S31:  -0.0680 S32:   0.0075 S33:  -0.0039                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   459        D   551                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.2040   9.2890   1.4770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0186 T22:   0.1950                                     
REMARK   3      T33:  -0.0310 T12:  -0.0098                                     
REMARK   3      T13:  -0.0521 T23:   0.0222                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9681 L22:   1.4189                                     
REMARK   3      L33:   0.8247 L12:  -0.2016                                     
REMARK   3      L13:  -0.1507 L23:   0.3115                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0142 S12:  -0.1007 S13:  -0.0379                       
REMARK   3      S21:   0.0892 S22:   0.0444 S23:  -0.0492                       
REMARK   3      S31:  -0.0814 S32:   0.1513 S33:  -0.0302                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   552        D   567                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.9700  -4.8700   2.9370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0452 T22:   0.1908                                     
REMARK   3      T33:   0.1567 T12:  -0.0044                                     
REMARK   3      T13:  -0.0434 T23:   0.0842                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.6917 L22:   2.9537                                     
REMARK   3      L33:   3.1739 L12:  -4.7338                                     
REMARK   3      L13:  -0.0253 L23:  -0.3962                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2354 S12:  -0.6927 S13:  -0.2617                       
REMARK   3      S21:   0.0660 S22:   0.2634 S23:  -0.0926                       
REMARK   3      S31:   0.1565 S32:   0.2861 S33:  -0.0280                       
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 3FNM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-DEC-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000050812.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAR-07                          
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               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 110177                             
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     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.3060                            
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) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER, SOLOMON                                       
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM HEPES, 25% PEG MME2000, 5 MG/ML   
REMARK 280  PROTEIN, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K    
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       52.68800            
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                                                    
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 300 REMARK: THE ENZYME IS A HETEROTETRAMER GENERATED BY THE              
REMARK 300 AUTOCATALYTIC CLEAVAGE OF THE PROENZYME.                             
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: 11620 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 19380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 11390 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 19740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     HIS A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     HIS A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     LEU A    16                                                      
REMARK 465     VAL A    17                                                      
REMARK 465     PRO A    18                                                      
REMARK 465     ARG A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     HIS A    22                                                      
REMARK 465     MET A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     SER A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     TYR A    29                                                      
REMARK 465     PRO A    30                                                      
REMARK 465     GLN A   373                                                      
REMARK 465     LEU A   374                                                      
REMARK 465     HIS A   375                                                      
REMARK 465     GLU A   376                                                      
REMARK 465     GLY A   377                                                      
REMARK 465     SER A   378                                                      
REMARK 465     ASN A   379                                                      
REMARK 465     MET C     3                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     HIS C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     HIS C     9                                                      
REMARK 465     HIS C    10                                                      
REMARK 465     HIS C    11                                                      
REMARK 465     HIS C    12                                                      
REMARK 465     SER C    13                                                      
REMARK 465     SER C    14                                                      
REMARK 465     GLY C    15                                                      
REMARK 465     LEU C    16                                                      
REMARK 465     VAL C    17                                                      
REMARK 465     PRO C    18                                                      
REMARK 465     ARG C    19                                                      
REMARK 465     GLY C    20                                                      
REMARK 465     SER C    21                                                      
REMARK 465     HIS C    22                                                      
REMARK 465     MET C    23                                                      
REMARK 465     ALA C    24                                                      
REMARK 465     SER C    25                                                      
REMARK 465     ALA C    26                                                      
REMARK 465     ALA C    27                                                      
REMARK 465     SER C    28                                                      
REMARK 465     TYR C    29                                                      
REMARK 465     PRO C    30                                                      
REMARK 465     PRO C    31                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS B 551    CG   CD   CE   NZ                                   
REMARK 470     LYS B 553    CG   CD   CE   NZ                                   
REMARK 470     LYS D 553    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS C 118   C     LYS C 118   O       0.196                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG D 448   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  36      -68.48   -121.85                                   
REMARK 500    ALA A  79      -54.05   -145.08                                   
REMARK 500    ASP A 359       37.67   -143.74                                   
REMARK 500    MET A 371       14.31     53.58                                   
REMARK 500    ASN B 400     -101.79     85.25                                   
REMARK 500    ALA B 406       -3.36     65.77                                   
REMARK 500    ASN B 446       -7.87     77.63                                   
REMARK 500    PHE B 465      -53.09   -121.77                                   
REMARK 500    TRP B 507      -60.44     78.32                                   
REMARK 500    ASP B 542       80.19   -161.12                                   
REMARK 500    PRO B 563        3.37    -65.56                                   
REMARK 500    LYS C  36      -63.06   -122.14                                   
REMARK 500    ALA C  79      -53.36   -144.89                                   
REMARK 500    ASP C 117     -168.78    -75.01                                   
REMARK 500    LYS C 125       -6.31     78.90                                   
REMARK 500    ASN D 400     -100.95     83.08                                   
REMARK 500    ASN D 446       -6.92     76.00                                   
REMARK 500    TRP D 507      -61.02     74.20                                   
REMARK 500    ASP D 542       82.56   -160.42                                   
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 AVN B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AVN D 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2NQO   RELATED DB: PDB                                   
REMARK 900 APOENZYME                                                            
REMARK 900 RELATED ID: 2QMG   RELATED DB: PDB                                   
REMARK 900 GLUTAMATE-BOUND ENZYME                                               
DBREF  3FNM A   25   379  UNP    O25743   O25743_HELPY    25    379             
DBREF  3FNM B  380   567  UNP    O25743   O25743_HELPY   380    567             
DBREF  3FNM C   25   379  UNP    O25743   O25743_HELPY    25    379             
DBREF  3FNM D  380   567  UNP    O25743   O25743_HELPY   380    567             
SEQADV 3FNM MET A    3  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM GLY A    4  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM SER A    5  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM SER A    6  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM HIS A    7  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM HIS A    8  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM HIS A    9  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM HIS A   10  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM HIS A   11  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM HIS A   12  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM SER A   13  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM SER A   14  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM GLY A   15  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM LEU A   16  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM VAL A   17  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM PRO A   18  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM ARG A   19  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM GLY A   20  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM SER A   21  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM HIS A   22  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM MET A   23  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM ALA A   24  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM MET C    3  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM GLY C    4  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM SER C    5  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM SER C    6  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM HIS C    7  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM HIS C    8  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM HIS C    9  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM HIS C   10  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM HIS C   11  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM HIS C   12  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM SER C   13  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM SER C   14  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM GLY C   15  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM LEU C   16  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM VAL C   17  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM PRO C   18  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM ARG C   19  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM GLY C   20  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM SER C   21  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM HIS C   22  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM MET C   23  UNP  O25743              EXPRESSION TAG                 
SEQADV 3FNM ALA C   24  UNP  O25743              EXPRESSION TAG                 
SEQRES   1 A  377  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  377  LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA ALA SER          
SEQRES   3 A  377  TYR PRO PRO ILE LYS ASN THR LYS VAL GLY LEU ALA LEU          
SEQRES   4 A  377  SER SER HIS PRO LEU ALA SER GLU ILE GLY GLN LYS VAL          
SEQRES   5 A  377  LEU GLU GLU GLY GLY ASN ALA ILE ASP ALA ALA VAL ALA          
SEQRES   6 A  377  ILE GLY PHE ALA LEU ALA VAL VAL HIS PRO ALA ALA GLY          
SEQRES   7 A  377  ASN ILE GLY GLY GLY GLY PHE ALA VAL ILE HIS LEU ALA          
SEQRES   8 A  377  ASN GLY GLU ASN VAL ALA LEU ASP PHE ARG GLU LYS ALA          
SEQRES   9 A  377  PRO LEU LYS ALA THR LYS ASN MET PHE LEU ASP LYS GLN          
SEQRES  10 A  377  GLY ASN VAL VAL PRO LYS LEU SER GLU ASP GLY TYR LEU          
SEQRES  11 A  377  ALA ALA GLY VAL PRO GLY THR VAL ALA GLY MET GLU ALA          
SEQRES  12 A  377  MET LEU LYS LYS TYR GLY THR LYS LYS LEU SER GLN LEU          
SEQRES  13 A  377  ILE ASP PRO ALA ILE LYS LEU ALA GLU ASN GLY TYR ALA          
SEQRES  14 A  377  ILE SER GLN ARG GLN ALA GLU THR LEU LYS GLU ALA ARG          
SEQRES  15 A  377  GLU ARG PHE LEU LYS TYR SER SER SER LYS LYS TYR PHE          
SEQRES  16 A  377  PHE LYS LYS GLY HIS LEU ASP TYR GLN GLU GLY ASP LEU          
SEQRES  17 A  377  PHE VAL GLN LYS ASP LEU ALA LYS THR LEU ASN GLN ILE          
SEQRES  18 A  377  LYS THR LEU GLY ALA LYS GLY PHE TYR GLN GLY GLN VAL          
SEQRES  19 A  377  ALA GLU LEU ILE GLU LYS ASP MET LYS LYS ASN GLY GLY          
SEQRES  20 A  377  ILE ILE THR LYS GLU ASP LEU ALA SER TYR ASN VAL LYS          
SEQRES  21 A  377  TRP ARG LYS PRO VAL VAL GLY SER TYR ARG GLY TYR LYS          
SEQRES  22 A  377  ILE ILE SER MET SER PRO PRO SER SER GLY GLY THR HIS          
SEQRES  23 A  377  LEU ILE GLN ILE LEU ASN VAL MET GLU ASN ALA ASP LEU          
SEQRES  24 A  377  SER ALA LEU GLY TYR GLY ALA SER LYS ASN ILE HIS ILE          
SEQRES  25 A  377  ALA ALA GLU ALA MET ARG GLN ALA TYR ALA ASP ARG SER          
SEQRES  26 A  377  VAL TYR MET GLY ASP ALA ASP PHE VAL SER VAL PRO VAL          
SEQRES  27 A  377  ASP LYS LEU ILE ASN LYS ALA TYR ALA LYS LYS ILE PHE          
SEQRES  28 A  377  ASP THR ILE GLN PRO ASP THR VAL THR PRO SER SER GLN          
SEQRES  29 A  377  ILE LYS PRO GLY MET GLY GLN LEU HIS GLU GLY SER ASN          
SEQRES   1 B  188  THR THR HIS TYR SER VAL ALA ASP ARG TRP GLY ASN ALA          
SEQRES   2 B  188  VAL SER VAL THR TYR THR ILE ASN ALA SER TYR GLY SER          
SEQRES   3 B  188  ALA ALA SER ILE ASP GLY ALA GLY PHE LEU LEU ASN ASN          
SEQRES   4 B  188  GLU MET ASP ASP PHE SER ILE LYS PRO GLY ASN PRO ASN          
SEQRES   5 B  188  LEU TYR GLY LEU VAL GLY GLY ASP ALA ASN ALA ILE GLU          
SEQRES   6 B  188  ALA ASN LYS ARG PRO LEU SER SER MET SER PRO THR ILE          
SEQRES   7 B  188  VAL LEU LYS ASN ASN LYS VAL PHE LEU VAL VAL GLY SER          
SEQRES   8 B  188  PRO GLY GLY SER ARG ILE ILE THR THR VAL LEU GLN VAL          
SEQRES   9 B  188  ILE SER ASN VAL ILE ASP TYR ASN MET ASN ILE SER GLU          
SEQRES  10 B  188  ALA VAL SER ALA PRO ARG PHE HIS MET GLN TRP LEU PRO          
SEQRES  11 B  188  ASP GLU LEU ARG ILE GLU LYS PHE GLY MET PRO ALA ASP          
SEQRES  12 B  188  VAL LYS ASP ASN LEU THR LYS MET GLY TYR GLN ILE VAL          
SEQRES  13 B  188  THR LYS PRO VAL MET GLY ASP VAL ASN ALA ILE GLN VAL          
SEQRES  14 B  188  LEU PRO LYS THR LYS GLY SER VAL PHE TYR GLY SER THR          
SEQRES  15 B  188  ASP PRO ARG LYS GLU PHE                                      
SEQRES   1 C  377  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  377  LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA ALA SER          
SEQRES   3 C  377  TYR PRO PRO ILE LYS ASN THR LYS VAL GLY LEU ALA LEU          
SEQRES   4 C  377  SER SER HIS PRO LEU ALA SER GLU ILE GLY GLN LYS VAL          
SEQRES   5 C  377  LEU GLU GLU GLY GLY ASN ALA ILE ASP ALA ALA VAL ALA          
SEQRES   6 C  377  ILE GLY PHE ALA LEU ALA VAL VAL HIS PRO ALA ALA GLY          
SEQRES   7 C  377  ASN ILE GLY GLY GLY GLY PHE ALA VAL ILE HIS LEU ALA          
SEQRES   8 C  377  ASN GLY GLU ASN VAL ALA LEU ASP PHE ARG GLU LYS ALA          
SEQRES   9 C  377  PRO LEU LYS ALA THR LYS ASN MET PHE LEU ASP LYS GLN          
SEQRES  10 C  377  GLY ASN VAL VAL PRO LYS LEU SER GLU ASP GLY TYR LEU          
SEQRES  11 C  377  ALA ALA GLY VAL PRO GLY THR VAL ALA GLY MET GLU ALA          
SEQRES  12 C  377  MET LEU LYS LYS TYR GLY THR LYS LYS LEU SER GLN LEU          
SEQRES  13 C  377  ILE ASP PRO ALA ILE LYS LEU ALA GLU ASN GLY TYR ALA          
SEQRES  14 C  377  ILE SER GLN ARG GLN ALA GLU THR LEU LYS GLU ALA ARG          
SEQRES  15 C  377  GLU ARG PHE LEU LYS TYR SER SER SER LYS LYS TYR PHE          
SEQRES  16 C  377  PHE LYS LYS GLY HIS LEU ASP TYR GLN GLU GLY ASP LEU          
SEQRES  17 C  377  PHE VAL GLN LYS ASP LEU ALA LYS THR LEU ASN GLN ILE          
SEQRES  18 C  377  LYS THR LEU GLY ALA LYS GLY PHE TYR GLN GLY GLN VAL          
SEQRES  19 C  377  ALA GLU LEU ILE GLU LYS ASP MET LYS LYS ASN GLY GLY          
SEQRES  20 C  377  ILE ILE THR LYS GLU ASP LEU ALA SER TYR ASN VAL LYS          
SEQRES  21 C  377  TRP ARG LYS PRO VAL VAL GLY SER TYR ARG GLY TYR LYS          
SEQRES  22 C  377  ILE ILE SER MET SER PRO PRO SER SER GLY GLY THR HIS          
SEQRES  23 C  377  LEU ILE GLN ILE LEU ASN VAL MET GLU ASN ALA ASP LEU          
SEQRES  24 C  377  SER ALA LEU GLY TYR GLY ALA SER LYS ASN ILE HIS ILE          
SEQRES  25 C  377  ALA ALA GLU ALA MET ARG GLN ALA TYR ALA ASP ARG SER          
SEQRES  26 C  377  VAL TYR MET GLY ASP ALA ASP PHE VAL SER VAL PRO VAL          
SEQRES  27 C  377  ASP LYS LEU ILE ASN LYS ALA TYR ALA LYS LYS ILE PHE          
SEQRES  28 C  377  ASP THR ILE GLN PRO ASP THR VAL THR PRO SER SER GLN          
SEQRES  29 C  377  ILE LYS PRO GLY MET GLY GLN LEU HIS GLU GLY SER ASN          
SEQRES   1 D  188  THR THR HIS TYR SER VAL ALA ASP ARG TRP GLY ASN ALA          
SEQRES   2 D  188  VAL SER VAL THR TYR THR ILE ASN ALA SER TYR GLY SER          
SEQRES   3 D  188  ALA ALA SER ILE ASP GLY ALA GLY PHE LEU LEU ASN ASN          
SEQRES   4 D  188  GLU MET ASP ASP PHE SER ILE LYS PRO GLY ASN PRO ASN          
SEQRES   5 D  188  LEU TYR GLY LEU VAL GLY GLY ASP ALA ASN ALA ILE GLU          
SEQRES   6 D  188  ALA ASN LYS ARG PRO LEU SER SER MET SER PRO THR ILE          
SEQRES   7 D  188  VAL LEU LYS ASN ASN LYS VAL PHE LEU VAL VAL GLY SER          
SEQRES   8 D  188  PRO GLY GLY SER ARG ILE ILE THR THR VAL LEU GLN VAL          
SEQRES   9 D  188  ILE SER ASN VAL ILE ASP TYR ASN MET ASN ILE SER GLU          
SEQRES  10 D  188  ALA VAL SER ALA PRO ARG PHE HIS MET GLN TRP LEU PRO          
SEQRES  11 D  188  ASP GLU LEU ARG ILE GLU LYS PHE GLY MET PRO ALA ASP          
SEQRES  12 D  188  VAL LYS ASP ASN LEU THR LYS MET GLY TYR GLN ILE VAL          
SEQRES  13 D  188  THR LYS PRO VAL MET GLY ASP VAL ASN ALA ILE GLN VAL          
SEQRES  14 D  188  LEU PRO LYS THR LYS GLY SER VAL PHE TYR GLY SER THR          
SEQRES  15 D  188  ASP PRO ARG LYS GLU PHE                                      
HET    AVN  B   1      10                                                       
HET    AVN  D   1      10                                                       
HETNAM     AVN (2S)-AMINO[(5S)-3-CHLORO-4,5-DIHYDROISOXAZOL-5-                  
HETNAM   2 AVN  YL]ACETIC ACID                                                  
HETSYN     AVN ACIVICIN                                                         
FORMUL   5  AVN    2(C5 H7 CL N2 O3)                                            
FORMUL   7  HOH   *534(H2 O)                                                    
HELIX    1   1 HIS A   44  GLU A   57  1                                  14    
HELIX    2   2 ASN A   60  HIS A   76  1                                  17    
HELIX    3   3 GLY A  130  ALA A  134  5                                   5    
HELIX    4   4 GLY A  138  GLY A  151  1                                  14    
HELIX    5   5 LYS A  154  GLY A  169  1                                  16    
HELIX    6   6 SER A  173  LEU A  188  1                                  16    
HELIX    7   7 TYR A  190  PHE A  197  1                                   8    
HELIX    8   8 GLN A  213  GLY A  227  1                                  15    
HELIX    9   9 ALA A  228  GLN A  233  1                                   6    
HELIX   10  10 GLN A  233  ASN A  247  1                                  15    
HELIX   11  11 THR A  252  TYR A  259  1                                   8    
HELIX   12  12 SER A  284  GLU A  297  1                                  14    
HELIX   13  13 ASN A  298  ALA A  299  5                                   2    
HELIX   14  14 ASP A  300  LEU A  304  5                                   5    
HELIX   15  15 ALA A  308  MET A  330  1                                  23    
HELIX   16  16 PRO A  339  ILE A  344  1                                   6    
HELIX   17  17 ASN A  345  THR A  355  1                                  11    
HELIX   18  18 PRO A  363  ILE A  367  5                                   5    
HELIX   19  19 LYS A  368  GLY A  372  5                                   5    
HELIX   20  20 ASN B  418  PHE B  423  5                                   6    
HELIX   21  21 GLY B  472  SER B  474  5                                   3    
HELIX   22  22 ARG B  475  ASP B  489  1                                  15    
HELIX   23  23 ASN B  493  ALA B  500  1                                   8    
HELIX   24  24 PRO B  520  MET B  530  1                                  11    
HELIX   25  25 HIS C   44  GLU C   57  1                                  14    
HELIX   26  26 ASN C   60  HIS C   76  1                                  17    
HELIX   27  27 GLY C  130  ALA C  134  5                                   5    
HELIX   28  28 GLY C  138  GLY C  151  1                                  14    
HELIX   29  29 LYS C  154  ILE C  159  1                                   6    
HELIX   30  30 ILE C  159  GLY C  169  1                                  11    
HELIX   31  31 SER C  173  LEU C  188  1                                  16    
HELIX   32  32 TYR C  190  PHE C  197  1                                   8    
HELIX   33  33 LYS C  200  HIS C  202  5                                   3    
HELIX   34  34 GLN C  213  GLY C  227  1                                  15    
HELIX   35  35 ALA C  228  GLN C  233  1                                   6    
HELIX   36  36 GLN C  233  ASN C  247  1                                  15    
HELIX   37  37 THR C  252  TYR C  259  1                                   8    
HELIX   38  38 SER C  284  GLU C  297  1                                  14    
HELIX   39  39 ASN C  298  ALA C  299  5                                   2    
HELIX   40  40 ASP C  300  LEU C  304  5                                   5    
HELIX   41  41 ALA C  308  MET C  330  1                                  23    
HELIX   42  42 PRO C  339  ILE C  344  1                                   6    
HELIX   43  43 ASN C  345  ILE C  356  1                                  12    
HELIX   44  44 PRO C  363  ILE C  367  5                                   5    
HELIX   45  45 LYS C  368  GLN C  373  5                                   6    
HELIX   46  46 ASN D  418  PHE D  423  5                                   6    
HELIX   47  47 GLY D  472  SER D  474  5                                   3    
HELIX   48  48 ARG D  475  ASP D  489  1                                  15    
HELIX   49  49 ASN D  493  ALA D  500  1                                   8    
HELIX   50  50 PRO D  520  GLY D  531  1                                  12    
SHEET    1   A 7 ILE A  32  ASN A  34  0                                        
SHEET    2   A 7 SER B 555  SER B 560 -1  O  PHE B 557   N  ASN A  34           
SHEET    3   A 7 ALA B 545  PRO B 550 -1  N  LEU B 549   O  VAL B 556           
SHEET    4   A 7 LYS B 463  VAL B 468 -1  N  PHE B 465   O  VAL B 548           
SHEET    5   A 7 THR B 456  LYS B 460 -1  N  VAL B 458   O  LEU B 466           
SHEET    6   A 7 TYR A 274  SER A 278 -1  N  ILE A 277   O  ILE B 457           
SHEET    7   A 7 VAL A 267  TYR A 271 -1  N  GLY A 269   O  ILE A 276           
SHEET    1   B 6 GLY A  38  LEU A  41  0                                        
SHEET    2   B 6 THR B 381  ASP B 387 -1  O  SER B 384   N  LEU A  41           
SHEET    3   B 6 ALA B 392  THR B 398 -1  O  VAL B 395   N  TYR B 383           
SHEET    4   B 6 GLY A  85  HIS A  91 -1  N  VAL A  89   O  SER B 394           
SHEET    5   B 6 ASN A  97  PHE A 102 -1  O  LEU A 100   N  ALA A  88           
SHEET    6   B 6 LYS A 262  ARG A 264 -1  O  LYS A 262   N  ASP A 101           
SHEET    1   C 2 TYR A 170  ALA A 171  0                                        
SHEET    2   C 2 LEU A 210  PHE A 211 -1  O  PHE A 211   N  TYR A 170           
SHEET    1   D 2 PHE A 198  LYS A 199  0                                        
SHEET    2   D 2 LEU A 203  ASP A 204 -1  O  LEU A 203   N  LYS A 199           
SHEET    1   E 2 LEU B 512  ILE B 514  0                                        
SHEET    2   E 2 ILE B 534  THR B 536  1  O  VAL B 535   N  ILE B 514           
SHEET    1   F 7 LYS C  33  ASN C  34  0                                        
SHEET    2   F 7 SER D 555  SER D 560 -1  O  PHE D 557   N  ASN C  34           
SHEET    3   F 7 ALA D 545  PRO D 550 -1  N  GLN D 547   O  TYR D 558           
SHEET    4   F 7 LYS D 463  VAL D 468 -1  N  VAL D 467   O  ILE D 546           
SHEET    5   F 7 THR D 456  LYS D 460 -1  N  VAL D 458   O  PHE D 465           
SHEET    6   F 7 TYR C 274  SER C 278 -1  N  ILE C 277   O  ILE D 457           
SHEET    7   F 7 VAL C 267  TYR C 271 -1  N  VAL C 267   O  SER C 278           
SHEET    1   G 6 GLY C  38  LEU C  41  0                                        
SHEET    2   G 6 THR D 381  ASP D 387 -1  O  SER D 384   N  LEU C  41           
SHEET    3   G 6 ALA D 392  THR D 398 -1  O  VAL D 395   N  TYR D 383           
SHEET    4   G 6 GLY C  85  HIS C  91 -1  N  VAL C  89   O  SER D 394           
SHEET    5   G 6 ASN C  97  PHE C 102 -1  O  LEU C 100   N  ALA C  88           
SHEET    6   G 6 LYS C 262  ARG C 264 -1  O  ARG C 264   N  ALA C  99           
SHEET    1   H 2 TYR C 170  ALA C 171  0                                        
SHEET    2   H 2 LEU C 210  PHE C 211 -1  O  PHE C 211   N  TYR C 170           
SHEET    1   I 2 PHE C 198  LYS C 199  0                                        
SHEET    2   I 2 LEU C 203  ASP C 204 -1  O  LEU C 203   N  LYS C 199           
SHEET    1   J 2 LEU D 512  ILE D 514  0                                        
SHEET    2   J 2 ILE D 534  THR D 536  1  O  VAL D 535   N  ILE D 514           
LINK         OG1 THR B 380                 C4  AVN B   1     1555   1555  1.34  
LINK         OG1 THR D 380                 C4  AVN D   1     1555   1555  1.35  
CISPEP   1 PRO A  281    PRO A  282          0        14.89                     
CISPEP   2 LEU B  508    PRO B  509          0        -3.87                     
CISPEP   3 PRO C  281    PRO C  282          0        14.02                     
CISPEP   4 LEU D  508    PRO D  509          0         2.58                     
SITE     1 AC1 14 ARG A 103  THR B 380  THR B 398  ASN B 400                    
SITE     2 AC1 14 GLU B 419  ASP B 422  TYR B 433  SER B 451                    
SITE     3 AC1 14 SER B 452  MET B 453  GLY B 472  GLY B 473                    
SITE     4 AC1 14 ILE B 476  HOH B 579                                          
SITE     1 AC2 14 ARG C 103  HOH D  27  THR D 380  THR D 398                    
SITE     2 AC2 14 ASN D 400  GLU D 419  ASP D 422  TYR D 433                    
SITE     3 AC2 14 SER D 451  SER D 452  MET D 453  GLY D 472                    
SITE     4 AC2 14 GLY D 473  ILE D 476                                          
CRYST1   54.711  105.376   91.927  90.00  91.69  90.00 P 1 21 1      4          
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      0.018278  0.000000  0.000539        0.00000                         
SCALE2      0.000000  0.009490  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010883        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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