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Entry: 1GU0
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HEADER    LYASE                                   22-JAN-02   1GU0              
TITLE     CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINASE FROM                      
TITLE    2 STREPTOMYCES COELICOLOR                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3-DEHYDROQUINATE DEHYDRATASE;                              
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   4 SYNONYM: TYPE II 3-DEHYDROQUINATE HYDRATASE,                         
COMPND   5  3-DEHYDROQUINASE, TYPE II DHQASE;                                   
COMPND   6 EC: 4.2.1.10;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR;                        
SOURCE   3 ORGANISM_TAXID: 1902;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR: PTB361;                                    
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDHQ                                      
KEYWDS    LYASE, TYPE II DEHYDROQUINASE, SHIKIMATE PATHWAY,                     
KEYWDS   2 DODECAMERIC QUATERNARY STRUCTURE, TETRAHEDRAL SYMMETRY               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.W.ROSZAK,T.KRELL,D.ROBINSON,I.S.HUNTER,J.R.COGGINS,                 
AUTHOR   2 A.J.LAPTHORN                                                         
REVDAT   2   24-FEB-09 1GU0    1       VERSN                                    
REVDAT   1   12-APR-02 1GU0    0                                                
JRNL        AUTH   A.W.ROSZAK,D.ROBINSON,T.KRELL,I.S.HUNTER,                    
JRNL        AUTH 2 M.FREDRICKSON,C.ABELL,J.R.COGGINS,A.J.LAPTHORN               
JRNL        TITL   THE STRUCTURE AND MECHANISM OF THE TYPE II                   
JRNL        TITL 2 DEHYDROQUINASE FROM STREPTOMYCES COELICOLOR                  
JRNL        REF    STRUCTURE                     V.  10   493 2002              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   11937054                                                     
JRNL        DOI    10.1016/S0969-2126(02)00747-5                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.0  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 66.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 6768                           
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) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 12147                           
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6768                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2770                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 738                          
REMARK   3   BIN FREE R VALUE                    : 0.3140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13327                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 1740                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.249         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.202         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.203         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.428         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13631 ; 0.018 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A): 12259 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 18585 ; 2.056 ; 1.925       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES): 28290 ; 0.953 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2117 ; 0.118 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15736 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2736 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3238 ; 0.236 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 12353 ; 0.223 ; 0.300       
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):  1427 ; 0.265 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):    13 ; 0.157 ; 0.500       
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):    10 ; 0.380 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    22 ; 0.230 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    44 ; 0.341 ; 0.500       
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):  8848 ; 1.178 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14091 ; 1.921 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4783 ; 2.411 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4494 ; 3.549 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D E F H I J K L           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      2       A     150      4                      
REMARK   3           1     B      2       B     150      4                      
REMARK   3           1     C      2       C     150      4                      
REMARK   3           1     D      2       D     150      4                      
REMARK   3           1     E      2       E     150      4                      
REMARK   3           1     F      2       F     150      4                      
REMARK   3           1     H      2       H     150      4                      
REMARK   3           1     I      2       I     150      4                      
REMARK   3           1     J      2       J     150      4                      
REMARK   3           1     K      2       K     150      4                      
REMARK   3           1     L      2       L     150      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
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     2        A   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.5850  59.2130  13.9240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1229 T22:   0.2776                                     
REMARK   3      T33:   0.3219 T12:  -0.0126                                     
REMARK   3      T13:   0.0401 T23:   0.0568                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1051 L22:   1.0431                                     
REMARK   3      L33:   0.6546 L12:   0.0234                                     
REMARK   3      L13:   0.0321 L23:  -0.3617                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0169 S12:  -0.0043 S13:   0.0053                       
REMARK   3      S21:  -0.0404 S22:  -0.0473 S23:  -0.1243                       
REMARK   3      S31:  -0.1880 S32:   0.0401 S33:   0.0304                       
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     2        B   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.3360  31.1720   1.6590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1265 T22:   0.3195                                     
REMARK   3      T33:   0.3064 T12:   0.0080                                     
REMARK   3      T13:   0.0941 T23:   0.0284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5475 L22:   1.5935                                     
REMARK   3      L33:   0.4548 L12:   0.3196                                     
REMARK   3      L13:   0.7359 L23:  -0.1031                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0043 S12:   0.1120 S13:  -0.0579                       
REMARK   3      S21:  -0.2974 S22:  -0.0108 S23:  -0.2260                       
REMARK   3      S31:   0.0441 S32:   0.1326 S33:   0.0065                       
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     2        C   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.5660  38.1940  21.7880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0041 T22:   0.4191                                     
REMARK   3      T33:   0.4894 T12:  -0.0199                                     
REMARK   3      T13:   0.0321 T23:   0.1250                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3805 L22:   0.8437                                     
REMARK   3      L33:   1.0427 L12:  -0.2967                                     
REMARK   3      L13:  -0.0215 L23:   0.0392                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0040 S12:  -0.0135 S13:   0.0002                       
REMARK   3      S21:   0.0062 S22:  -0.0924 S23:  -0.3024                       
REMARK   3      S31:  -0.0351 S32:   0.3176 S33:   0.0884                       
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     2        D   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.0260  65.4940  28.3430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1848 T22:   0.2592                                     
REMARK   3      T33:   0.3173 T12:   0.0334                                     
REMARK   3      T13:   0.0216 T23:   0.0274                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5667 L22:   0.2193                                     
REMARK   3      L33:   1.0251 L12:   0.1273                                     
REMARK   3      L13:  -0.3872 L23:  -0.4262                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0582 S12:   0.0475 S13:   0.1314                       
REMARK   3      S21:   0.0940 S22:   0.0219 S23:   0.0000                       
REMARK   3      S31:  -0.2593 S32:  -0.0274 S33:  -0.0802                       
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     2        E   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.7800  55.0110  57.1940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2456 T22:   0.2670                                     
REMARK   3      T33:   0.2857 T12:  -0.0116                                     
REMARK   3      T13:  -0.0074 T23:  -0.0215                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0491 L22:   0.3290                                     
REMARK   3      L33:   0.1992 L12:   0.1171                                     
REMARK   3      L13:   0.2581 L23:   0.2698                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0400 S12:  -0.0414 S13:   0.0345                       
REMARK   3      S21:   0.1609 S22:  -0.0418 S23:   0.0098                       
REMARK   3      S31:  -0.0590 S32:  -0.0308 S33:   0.0018                       
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     2        F   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.2150  45.4980  38.0430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0716 T22:   0.2951                                     
REMARK   3      T33:   0.3314 T12:   0.0330                                     
REMARK   3      T13:   0.0190 T23:  -0.0123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5260 L22:   0.8535                                     
REMARK   3      L33:   0.5838 L12:   0.1306                                     
REMARK   3      L13:   0.0440 L23:  -0.0045                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0427 S12:  -0.0426 S13:   0.0338                       
REMARK   3      S21:   0.0190 S22:  -0.0462 S23:   0.1752                       
REMARK   3      S31:  -0.0958 S32:  -0.1191 S33:   0.0035                       
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     2        G   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2570  14.2770   8.7030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0822 T22:   0.2811                                     
REMARK   3      T33:   0.2705 T12:   0.0158                                     
REMARK   3      T13:   0.0080 T23:  -0.0059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0644 L22:   0.6983                                     
REMARK   3      L33:   1.0733 L12:  -0.1598                                     
REMARK   3      L13:  -0.4638 L23:   0.3169                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0399 S12:   0.0528 S13:   0.0133                       
REMARK   3      S21:  -0.1143 S22:  -0.0517 S23:   0.0300                       
REMARK   3      S31:   0.0139 S32:  -0.0078 S33:   0.0118                       
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     2        H   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.1270  23.6550  27.3950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0037 T22:   0.3137                                     
REMARK   3      T33:   0.3255 T12:   0.0104                                     
REMARK   3      T13:  -0.0019 T23:  -0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4246 L22:   0.9799                                     
REMARK   3      L33:   0.8643 L12:  -0.4863                                     
REMARK   3      L13:  -0.2181 L23:  -0.0533                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0023 S12:   0.0204 S13:  -0.0317                       
REMARK   3      S21:  -0.0142 S22:   0.0097 S23:   0.1709                       
REMARK   3      S31:  -0.0148 S32:  -0.1927 S33:  -0.0120                       
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 :   I     2        I   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.9470   3.6730  37.4620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0458 T22:   0.2575                                     
REMARK   3      T33:   0.2697 T12:  -0.0176                                     
REMARK   3      T13:   0.0077 T23:   0.0101                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2259 L22:   0.4906                                     
REMARK   3      L33:   0.8437 L12:  -0.1421                                     
REMARK   3      L13:  -0.0050 L23:  -0.2886                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0135 S12:  -0.0239 S13:  -0.0426                       
REMARK   3      S21:  -0.0075 S22:  -0.0217 S23:  -0.0236                       
REMARK   3      S31:   0.1077 S32:  -0.0159 S33:   0.0352                       
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 :   J     2        J   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.2660  31.0330  45.0590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0552 T22:   0.4389                                     
REMARK   3      T33:   0.4959 T12:  -0.0285                                     
REMARK   3      T13:  -0.0588 T23:   0.1060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5361 L22:   0.6348                                     
REMARK   3      L33:   0.9525 L12:   0.1384                                     
REMARK   3      L13:  -0.0768 L23:  -0.3965                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0592 S12:  -0.0584 S13:   0.0710                       
REMARK   3      S21:   0.0558 S22:  -0.0669 S23:  -0.3527                       
REMARK   3      S31:  -0.0690 S32:   0.3413 S33:   0.1260                       
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 :   K     2        K   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.1510  10.0180  52.2740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0810 T22:   0.2856                                     
REMARK   3      T33:   0.2898 T12:   0.0201                                     
REMARK   3      T13:  -0.0283 T23:   0.0550                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0758 L22:   0.8864                                     
REMARK   3      L33:   0.6823 L12:   0.0268                                     
REMARK   3      L13:  -0.0081 L23:  -0.2084                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0557 S12:   0.0025 S13:   0.0470                       
REMARK   3      S21:   0.0721 S22:  -0.0133 S23:  -0.1140                       
REMARK   3      S31:   0.0475 S32:   0.0850 S33:   0.0690                       
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 :   L     2        L   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.5620  38.0700  64.6020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2473 T22:   0.3023                                     
REMARK   3      T33:   0.3062 T12:  -0.0061                                     
REMARK   3      T13:  -0.0958 T23:  -0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3924 L22:   1.8874                                     
REMARK   3      L33:   0.3744 L12:  -0.3804                                     
REMARK   3      L13:  -0.1953 L23:  -0.1329                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0462 S12:  -0.0734 S13:   0.1072                       
REMARK   3      S21:   0.4087 S22:   0.0000 S23:  -0.2046                       
REMARK   3      S31:  -0.0653 S32:   0.1204 S33:   0.0462                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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 1GU0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JAN-02.                  
REMARK 100 THE PDBE ID CODE IS EBI-8600.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-MAR-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 429534                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 75.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.82                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: AMORE                                                 
REMARK 200 STARTING MODEL: 2DHQ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 56.3                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM/POTASSIUM               
REMARK 280  PHOSPHATE, TRIS BUFFER                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       58.10000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.60000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       69.20000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.60000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       58.10000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       69.20000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L                                  
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     PRO A     1                                                      
REMARK 465     ALA A   151                                                      
REMARK 465     GLY A   152                                                      
REMARK 465     SER A   153                                                      
REMARK 465     ALA A   154                                                      
REMARK 465     ARG A   155                                                      
REMARK 465     ALA A   156                                                      
REMARK 465     PRO B     1                                                      
REMARK 465     ALA B   151                                                      
REMARK 465     GLY B   152                                                      
REMARK 465     SER B   153                                                      
REMARK 465     ALA B   154                                                      
REMARK 465     ARG B   155                                                      
REMARK 465     ALA B   156                                                      
REMARK 465     PRO C     1                                                      
REMARK 465     ALA C   151                                                      
REMARK 465     GLY C   152                                                      
REMARK 465     SER C   153                                                      
REMARK 465     ALA C   154                                                      
REMARK 465     ARG C   155                                                      
REMARK 465     ALA C   156                                                      
REMARK 465     PRO D     1                                                      
REMARK 465     ALA D   151                                                      
REMARK 465     GLY D   152                                                      
REMARK 465     SER D   153                                                      
REMARK 465     ALA D   154                                                      
REMARK 465     ARG D   155                                                      
REMARK 465     ALA D   156                                                      
REMARK 465     PRO E     1                                                      
REMARK 465     ALA E   151                                                      
REMARK 465     GLY E   152                                                      
REMARK 465     SER E   153                                                      
REMARK 465     ALA E   154                                                      
REMARK 465     ARG E   155                                                      
REMARK 465     ALA E   156                                                      
REMARK 465     PRO F     1                                                      
REMARK 465     ALA F   151                                                      
REMARK 465     GLY F   152                                                      
REMARK 465     SER F   153                                                      
REMARK 465     ALA F   154                                                      
REMARK 465     ARG F   155                                                      
REMARK 465     ALA F   156                                                      
REMARK 465     PRO G     1                                                      
REMARK 465     ALA G   151                                                      
REMARK 465     GLY G   152                                                      
REMARK 465     SER G   153                                                      
REMARK 465     ALA G   154                                                      
REMARK 465     ARG G   155                                                      
REMARK 465     ALA G   156                                                      
REMARK 465     PRO H     1                                                      
REMARK 465     ALA H   151                                                      
REMARK 465     GLY H   152                                                      
REMARK 465     SER H   153                                                      
REMARK 465     ALA H   154                                                      
REMARK 465     ARG H   155                                                      
REMARK 465     ALA H   156                                                      
REMARK 465     PRO I     1                                                      
REMARK 465     ALA I   151                                                      
REMARK 465     GLY I   152                                                      
REMARK 465     SER I   153                                                      
REMARK 465     ALA I   154                                                      
REMARK 465     ARG I   155                                                      
REMARK 465     ALA I   156                                                      
REMARK 465     PRO J     1                                                      
REMARK 465     ALA J   151                                                      
REMARK 465     GLY J   152                                                      
REMARK 465     SER J   153                                                      
REMARK 465     ALA J   154                                                      
REMARK 465     ARG J   155                                                      
REMARK 465     ALA J   156                                                      
REMARK 465     PRO K     1                                                      
REMARK 465     ALA K   151                                                      
REMARK 465     GLY K   152                                                      
REMARK 465     SER K   153                                                      
REMARK 465     ALA K   154                                                      
REMARK 465     ARG K   155                                                      
REMARK 465     ALA K   156                                                      
REMARK 465     PRO L     1                                                      
REMARK 465     ALA L   151                                                      
REMARK 465     GLY L   152                                                      
REMARK 465     SER L   153                                                      
REMARK 465     ALA L   154                                                      
REMARK 465     ARG L   155                                                      
REMARK 465     ALA L   156                                                      
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     GLN A  24    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  26    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  27    CG1  CG2  CD1                                       
REMARK 470     GLN B  24    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  26    CG   CD   OE1  OE2                                  
REMARK 470     ILE B  27    CG1  CG2  CD1                                       
REMARK 470     GLN C  24    CG   CD   OE1  NE2                                  
REMARK 470     GLU C  26    CG   CD   OE1  OE2                                  
REMARK 470     ILE C  27    CG1  CG2  CD1                                       
REMARK 470     GLN D  24    CG   CD   OE1  NE2                                  
REMARK 470     GLU D  26    CG   CD   OE1  OE2                                  
REMARK 470     ILE D  27    CG1  CG2  CD1                                       
REMARK 470     GLN E  24    CG   CD   OE1  NE2                                  
REMARK 470     GLU E  26    CG   CD   OE1  OE2                                  
REMARK 470     ILE E  27    CG1  CG2  CD1                                       
REMARK 470     GLN F  24    CG   CD   OE1  NE2                                  
REMARK 470     GLU F  26    CG   CD   OE1  OE2                                  
REMARK 470     ILE F  27    CG1  CG2  CD1                                       
REMARK 470     GLU G  26    CG   CD   OE1  OE2                                  
REMARK 470     GLN H  24    CG   CD   OE1  NE2                                  
REMARK 470     GLU H  26    CG   CD   OE1  OE2                                  
REMARK 470     ILE H  27    CG1  CG2  CD1                                       
REMARK 470     GLN I  24    CG   CD   OE1  NE2                                  
REMARK 470     GLU I  26    CG   CD   OE1  OE2                                  
REMARK 470     ILE I  27    CG1  CG2  CD1                                       
REMARK 470     GLN J  24    CG   CD   OE1  NE2                                  
REMARK 470     GLU J  26    CG   CD   OE1  OE2                                  
REMARK 470     ILE J  27    CG1  CG2  CD1                                       
REMARK 470     GLN K  24    CG   CD   OE1  NE2                                  
REMARK 470     GLU K  26    CG   CD   OE1  OE2                                  
REMARK 470     ILE K  27    CG1  CG2  CD1                                       
REMARK 470     GLN L  24    CG   CD   OE1  NE2                                  
REMARK 470     GLU L  26    CG   CD   OE1  OE2                                  
REMARK 470     ILE L  27    CG1  CG2  CD1                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    CYS B    74  -  O    HOH B  2075              1.92            
REMARK 500   OE2  GLU C    61  -  O    HOH C  2043              2.17            
REMARK 500   ND2  ASN E     6  -  O    HOH E  2006              2.01            
REMARK 500   OE2  GLU E   114  -  O    HOH E  2138              2.08            
REMARK 500   O    GLY F    21  -  O    HOH F  2025              2.07            
REMARK 500   NE2  GLN F    22  -  O    HOH F  2028              1.87            
REMARK 500   O    PHE F    53  -  O    HOH F  2074              2.00            
REMARK 500   O    ALA F    93  -  O    HOH F  2106              1.91            
REMARK 500   N    CYS F    97  -  O    HOH F  2106              2.16            
REMARK 500   ND2  ASN G     6  -  O    HOH G  2012              1.89            
REMARK 500   OD2  ASP G    31  -  O    HOH G  2052              1.82            
REMARK 500   OD2  ASP G    64  -  O    HOH G  2108              2.18            
REMARK 500   OE2  GLU G   143  -  O    HOH G  2172              2.08            
REMARK 500   NE2  GLN H    22  -  O    HOH H  2036              1.61            
REMARK 500   O    ASP H   127  -  O    HOH H  2161              2.17            
REMARK 500   NH2  ARG I     2  -  O    ARG I    70              1.74            
REMARK 500   NE2  GLN J   124  -  O    HOH J  2083              2.19            
REMARK 500   NH2  ARG K     2  -  C    LEU K    71              2.17            
REMARK 500   OE2  GLU K    61  -  O    HOH K  2091              2.15            
REMARK 500   O    ILE K   107  -  O    HOH K  2114              2.07            
REMARK 500   OG   SER K   108  -  O    HOH K  2115              2.07            
REMARK 500   NE2  HIS K   111  -  O    HOH K  2118              1.93            
REMARK 500   OE1  GLN L   124  -  O    HOH L  2104              2.09            
REMARK 500   O    HOH A  2008  -  O    HOH A  2024              2.14            
REMARK 500   O    HOH A  2013  -  O    HOH A  2039              2.02            
REMARK 500   O    HOH A  2021  -  O    HOH A  2053              2.15            
REMARK 500   O    HOH A  2115  -  O    HOH A  2122              2.12            
REMARK 500   O    HOH A  2119  -  O    HOH D  2133              2.19            
REMARK 500   O    HOH B  2057  -  O    HOH B  2066              2.07            
REMARK 500   O    HOH B  2076  -  O    HOH B  2087              2.16            
REMARK 500   O    HOH B  2076  -  O    HOH B  2089              2.13            
REMARK 500   O    HOH B  2106  -  O    HOH B  2114              2.05            
REMARK 500   O    HOH B  2106  -  O    HOH B  2110              1.99            
REMARK 500   O    HOH C  2080  -  O    HOH C  2083              2.10            
REMARK 500   O    HOH D  2029  -  O    HOH D  2070              2.19            
REMARK 500   O    HOH D  2051  -  O    HOH A  2088              2.04            
REMARK 500   O    HOH D  2123  -  O    HOH D  2126              2.08            
REMARK 500   O    HOH D  2131  -  O    HOH D  2133              1.94            
REMARK 500   O    HOH E  2040  -  O    HOH E  2098              2.05            
REMARK 500   O    HOH E  2117  -  O    HOH E  2120              2.18            
REMARK 500   O    HOH E  2144  -  O    HOH E  2150              1.94            
REMARK 500   O    HOH F  2031  -  O    HOH F  2082              2.11            
REMARK 500   O    HOH F  2032  -  O    HOH F  2087              1.81            
REMARK 500   O    HOH F  2069  -  O    HOH F  2073              2.17            
REMARK 500   O    HOH F  2100  -  O    HOH F  2131              2.12            
REMARK 500   O    HOH F  2125  -  O    HOH F  2129              1.76            
REMARK 500   O    HOH F  2129  -  O    HOH H  2133              2.14            
REMARK 500   O    HOH G  2003  -  O    HOH G  2008              2.19            
REMARK 500   O    HOH G  2014  -  O    HOH G  2027              2.20            
REMARK 500   O    HOH G  2028  -  O    HOH G  2030              2.18            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      75 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                                                                      
REMARK 500   O    HOH E  2024     O    HOH A  2026     2565      2.09           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    TRP I  65   CG    TRP I  65   CD1     0.090                       
REMARK 500    VAL I 103   CB    VAL I 103   CG2    -0.126                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS       2 BOND DEVIATIONS                               
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    ASP A  31   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 127   CB  -  CG  -  OD2 ANGL. DEV. =   8.6 DEGREES          
REMARK 500    ARG A 144   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ASP B  35   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP B 127   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP C  52   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG C  70   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ASP C 127   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG D  70   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG D 117   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASP D 127   CB  -  CG  -  OD2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    ASP E  31   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP E  35   CB  -  CG  -  OD2 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ASP E 127   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP F  92   CB  -  CG  -  OD2 ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ASP F 127   CB  -  CG  -  OD2 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ARG F 144   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP G  31   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP G 127   CB  -  CG  -  OD2 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ASP H  52   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG H  54   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG H  54   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG H  70   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ASP H  98   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP H 127   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP I  35   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG I 125   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP I 127   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP J  92   CB  -  CG  -  OD1 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    ASP J 127   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP K  92   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG K 117   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG K 117   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP K 127   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ASP L  52   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 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 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 A  16      -17.00     77.25                                   
REMARK 500    ARG A  23     -103.41    -97.96                                   
REMARK 500    PRO A  25       85.81    -63.91                                   
REMARK 500    GLU A  26      -55.55    171.77                                   
REMARK 500    ALA A  81     -125.95     46.60                                   
REMARK 500    ARG A 113     -167.16   -102.67                                   
REMARK 500    ASN B  16      -13.84     78.31                                   
REMARK 500    ARG B  23      -94.97   -100.58                                   
REMARK 500    PRO B  25       84.81    -64.56                                   
REMARK 500    GLU B  26      -58.62    172.48                                   
REMARK 500    ALA B  81     -135.93     55.36                                   
REMARK 500    ARG B 113     -164.78   -101.30                                   
REMARK 500    ASN C  16      -13.41     75.53                                   
REMARK 500    ARG C  23     -102.11    -96.48                                   
REMARK 500    PRO C  25       78.64    -60.90                                   
REMARK 500    GLU C  26      -52.66    173.98                                   
REMARK 500    ALA C  81     -126.81     48.06                                   
REMARK 500    ASN D  16      -15.98     75.95                                   
REMARK 500    ARG D  23      -94.11   -100.45                                   
REMARK 500    PRO D  25       83.29    -65.27                                   
REMARK 500    GLU D  26      -51.66    172.34                                   
REMARK 500    ALA D  81     -133.38     53.53                                   
REMARK 500    ARG D 113     -164.08   -101.53                                   
REMARK 500    ASN E  16      -10.16     74.98                                   
REMARK 500    ARG E  23     -100.75    -95.77                                   
REMARK 500    PRO E  25       78.01    -63.47                                   
REMARK 500    GLU E  26      -57.97    176.22                                   
REMARK 500    ALA E  81     -140.81     52.92                                   
REMARK 500    ASN F  16       -5.51     70.83                                   
REMARK 500    ARG F  23     -104.50   -100.76                                   
REMARK 500    PRO F  25       82.82    -61.66                                   
REMARK 500    GLU F  26      -54.26    168.26                                   
REMARK 500    ALA F  81     -134.29     55.33                                   
REMARK 500    ASN G  16      -16.24     77.29                                   
REMARK 500    PRO G  25     -100.41    -76.58                                   
REMARK 500    ALA G  81     -138.40     55.67                                   
REMARK 500    ARG G 113     -162.37   -106.13                                   
REMARK 500    ASN H  16      -12.35     77.85                                   
REMARK 500    ARG H  23      -90.03   -100.22                                   
REMARK 500    PRO H  25       86.73    -62.69                                   
REMARK 500    GLU H  26      -53.77    168.96                                   
REMARK 500    ALA H  81     -130.89     48.19                                   
REMARK 500    ARG H 113     -162.74   -101.27                                   
REMARK 500    ASN I  16       -9.26     79.93                                   
REMARK 500    ARG I  23      -93.86    -93.98                                   
REMARK 500    PRO I  25       83.29    -64.23                                   
REMARK 500    GLU I  26      -54.66    171.34                                   
REMARK 500    ALA I  81     -132.74     45.18                                   
REMARK 500    ARG I 113     -163.83   -104.24                                   
REMARK 500    ASN J  16       -2.86     86.81                                   
REMARK 500    ARG J  23     -100.26    -93.49                                   
REMARK 500    PRO J  25       82.21    -64.20                                   
REMARK 500    GLU J  26      -54.03    171.80                                   
REMARK 500    ALA J  81     -135.79     57.78                                   
REMARK 500    ARG J 113     -159.31   -101.69                                   
REMARK 500    ASN K  16       -8.73     75.90                                   
REMARK 500    ARG K  23      -98.83    -97.74                                   
REMARK 500    PRO K  25       84.51    -63.21                                   
REMARK 500    GLU K  26      -48.85    168.79                                   
REMARK 500    ALA K  81     -134.36     57.24                                   
REMARK 500    ARG K 113     -155.52   -103.28                                   
REMARK 500    ASN L  16       -9.14     69.78                                   
REMARK 500    ARG L  23      -96.11    -97.47                                   
REMARK 500    PRO L  25       81.72    -64.35                                   
REMARK 500    GLU L  26      -53.69    173.21                                   
REMARK 500    ALA L  81     -135.12     53.26                                   
REMARK 500    ARG L 113     -167.86   -100.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS D 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS G 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS J 200                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1D0I   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINASE                         
REMARK 900  FROM STREPTOMYCES COELICOLOR COMPLEXED WITH                         
REMARK 900  PHOSPHATE IONS                                                      
REMARK 900 RELATED ID: 1GQN   RELATED DB: PDB                                   
REMARK 900  NATIVE 3-DEHYDROQUINASE FROM SALMONELLA TYPHI                       
REMARK 900 RELATED ID: 1GQO   RELATED DB: PDB                                   
REMARK 900  TYPE II DEHYDROQUINASE FROM BACILLUS SUBTILIS                       
REMARK 900 RELATED ID: 1GTZ   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF STREPTOMYCES COELICOLOR TYPE II                        
REMARK 900  DEHYDROQUINASE R23A MUTANT IN COMPLEX WITH                          
REMARK 900  DEHYDROSHIKIMATE                                                    
REMARK 900 RELATED ID: 1GU1   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINASE                         
REMARK 900  FROM STREPTOMYCES COELICOLOR COMPLEXED WITH 2                       
REMARK 900  ,3-ANYDRO-QUINIC ACID                                               
REMARK 900 RELATED ID: 2DHQ   RELATED DB: PDB                                   
REMARK 900  3-DEHYDROQUINATE DEHYDRATASE FROM MYCOBACTERIUM                     
REMARK 900   TUBERCULOSIS                                                       
REMARK 900 RELATED ID: 1QFE   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF TYPE I 3-DEHYDROQUINATE                            
REMARK 900  DEHYDRATASE FROM SALMONELLA TYPHI                                   
REMARK 900 RELATED ID: 1GUY   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS FOR THERMOPHILIC PROTEIN                           
REMARK 900  STABILITY: STRUCTURES OF THERMOPHILIC AND                           
REMARK 900  MESOPHILIC MALATE DEHYDROGENASES                                    
REMARK 900 RELATED ID: 1GVZ   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS FOR THERMOPHILIC PROTEIN                           
REMARK 900  STABILITY: STRUCTURES OF THERMOPHILIC AND                           
REMARK 900  MESOPHILIC MALATE DEHYDROGENASES                                    
REMARK 900 RELATED ID: 1GV1   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS FOR THERMOPHILIC PROTEIN                           
REMARK 900  STABILITY: STRUCTURES OF THERMOPHILIC AND                           
REMARK 900  MESOPHILIC MALATE DEHYDROGENASES                                    
DBREF  1GU0 A    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1GU0 B    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1GU0 C    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1GU0 D    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1GU0 E    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1GU0 F    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1GU0 G    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1GU0 H    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1GU0 I    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1GU0 J    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1GU0 K    1   156  UNP    P15474   AROQ_STRCO       1    156             
DBREF  1GU0 L    1   156  UNP    P15474   AROQ_STRCO       1    156             
SEQRES   1 A  156  PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU ASN          
SEQRES   2 A  156  GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO GLU          
SEQRES   3 A  156  ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA LEU          
SEQRES   4 A  156  CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL ASP          
SEQRES   5 A  156  PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP TRP          
SEQRES   6 A  156  ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL ILE          
SEQRES   7 A  156  ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE LEU          
SEQRES   8 A  156  ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL GLU          
SEQRES   9 A  156  VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE ARG          
SEQRES  10 A  156  HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL VAL          
SEQRES  11 A  156  ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL GLU          
SEQRES  12 A  156  ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG ALA          
SEQRES   1 B  156  PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU ASN          
SEQRES   2 B  156  GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO GLU          
SEQRES   3 B  156  ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA LEU          
SEQRES   4 B  156  CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL ASP          
SEQRES   5 B  156  PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP TRP          
SEQRES   6 B  156  ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL ILE          
SEQRES   7 B  156  ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE LEU          
SEQRES   8 B  156  ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL GLU          
SEQRES   9 B  156  VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE ARG          
SEQRES  10 B  156  HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL VAL          
SEQRES  11 B  156  ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL GLU          
SEQRES  12 B  156  ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG ALA          
SEQRES   1 C  156  PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU ASN          
SEQRES   2 C  156  GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO GLU          
SEQRES   3 C  156  ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA LEU          
SEQRES   4 C  156  CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL ASP          
SEQRES   5 C  156  PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP TRP          
SEQRES   6 C  156  ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL ILE          
SEQRES   7 C  156  ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE LEU          
SEQRES   8 C  156  ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL GLU          
SEQRES   9 C  156  VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE ARG          
SEQRES  10 C  156  HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL VAL          
SEQRES  11 C  156  ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL GLU          
SEQRES  12 C  156  ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG ALA          
SEQRES   1 D  156  PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU ASN          
SEQRES   2 D  156  GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO GLU          
SEQRES   3 D  156  ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA LEU          
SEQRES   4 D  156  CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL ASP          
SEQRES   5 D  156  PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP TRP          
SEQRES   6 D  156  ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL ILE          
SEQRES   7 D  156  ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE LEU          
SEQRES   8 D  156  ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL GLU          
SEQRES   9 D  156  VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE ARG          
SEQRES  10 D  156  HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL VAL          
SEQRES  11 D  156  ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL GLU          
SEQRES  12 D  156  ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG ALA          
SEQRES   1 E  156  PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU ASN          
SEQRES   2 E  156  GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO GLU          
SEQRES   3 E  156  ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA LEU          
SEQRES   4 E  156  CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL ASP          
SEQRES   5 E  156  PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP TRP          
SEQRES   6 E  156  ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL ILE          
SEQRES   7 E  156  ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE LEU          
SEQRES   8 E  156  ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL GLU          
SEQRES   9 E  156  VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE ARG          
SEQRES  10 E  156  HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL VAL          
SEQRES  11 E  156  ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL GLU          
SEQRES  12 E  156  ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG ALA          
SEQRES   1 F  156  PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU ASN          
SEQRES   2 F  156  GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO GLU          
SEQRES   3 F  156  ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA LEU          
SEQRES   4 F  156  CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL ASP          
SEQRES   5 F  156  PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP TRP          
SEQRES   6 F  156  ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL ILE          
SEQRES   7 F  156  ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE LEU          
SEQRES   8 F  156  ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL GLU          
SEQRES   9 F  156  VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE ARG          
SEQRES  10 F  156  HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL VAL          
SEQRES  11 F  156  ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL GLU          
SEQRES  12 F  156  ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG ALA          
SEQRES   1 G  156  PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU ASN          
SEQRES   2 G  156  GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO GLU          
SEQRES   3 G  156  ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA LEU          
SEQRES   4 G  156  CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL ASP          
SEQRES   5 G  156  PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP TRP          
SEQRES   6 G  156  ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL ILE          
SEQRES   7 G  156  ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE LEU          
SEQRES   8 G  156  ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL GLU          
SEQRES   9 G  156  VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE ARG          
SEQRES  10 G  156  HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL VAL          
SEQRES  11 G  156  ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL GLU          
SEQRES  12 G  156  ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG ALA          
SEQRES   1 H  156  PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU ASN          
SEQRES   2 H  156  GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO GLU          
SEQRES   3 H  156  ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA LEU          
SEQRES   4 H  156  CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL ASP          
SEQRES   5 H  156  PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP TRP          
SEQRES   6 H  156  ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL ILE          
SEQRES   7 H  156  ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE LEU          
SEQRES   8 H  156  ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL GLU          
SEQRES   9 H  156  VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE ARG          
SEQRES  10 H  156  HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL VAL          
SEQRES  11 H  156  ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL GLU          
SEQRES  12 H  156  ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG ALA          
SEQRES   1 I  156  PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU ASN          
SEQRES   2 I  156  GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO GLU          
SEQRES   3 I  156  ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA LEU          
SEQRES   4 I  156  CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL ASP          
SEQRES   5 I  156  PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP TRP          
SEQRES   6 I  156  ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL ILE          
SEQRES   7 I  156  ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE LEU          
SEQRES   8 I  156  ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL GLU          
SEQRES   9 I  156  VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE ARG          
SEQRES  10 I  156  HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL VAL          
SEQRES  11 I  156  ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL GLU          
SEQRES  12 I  156  ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG ALA          
SEQRES   1 J  156  PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU ASN          
SEQRES   2 J  156  GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO GLU          
SEQRES   3 J  156  ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA LEU          
SEQRES   4 J  156  CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL ASP          
SEQRES   5 J  156  PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP TRP          
SEQRES   6 J  156  ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL ILE          
SEQRES   7 J  156  ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE LEU          
SEQRES   8 J  156  ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL GLU          
SEQRES   9 J  156  VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE ARG          
SEQRES  10 J  156  HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL VAL          
SEQRES  11 J  156  ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL GLU          
SEQRES  12 J  156  ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG ALA          
SEQRES   1 K  156  PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU ASN          
SEQRES   2 K  156  GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO GLU          
SEQRES   3 K  156  ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA LEU          
SEQRES   4 K  156  CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL ASP          
SEQRES   5 K  156  PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP TRP          
SEQRES   6 K  156  ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL ILE          
SEQRES   7 K  156  ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE LEU          
SEQRES   8 K  156  ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL GLU          
SEQRES   9 K  156  VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE ARG          
SEQRES  10 K  156  HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL VAL          
SEQRES  11 K  156  ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL GLU          
SEQRES  12 K  156  ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG ALA          
SEQRES   1 L  156  PRO ARG SER LEU ALA ASN ALA PRO ILE MET ILE LEU ASN          
SEQRES   2 L  156  GLY PRO ASN LEU ASN LEU LEU GLY GLN ARG GLN PRO GLU          
SEQRES   3 L  156  ILE TYR GLY SER ASP THR LEU ALA ASP VAL GLU ALA LEU          
SEQRES   4 L  156  CYS VAL LYS ALA ALA ALA ALA HIS GLY GLY THR VAL ASP          
SEQRES   5 L  156  PHE ARG GLN SER ASN HIS GLU GLY GLU LEU VAL ASP TRP          
SEQRES   6 L  156  ILE HIS GLU ALA ARG LEU ASN HIS CYS GLY ILE VAL ILE          
SEQRES   7 L  156  ASN PRO ALA ALA TYR SER HIS THR SER VAL ALA ILE LEU          
SEQRES   8 L  156  ASP ALA LEU ASN THR CYS ASP GLY LEU PRO VAL VAL GLU          
SEQRES   9 L  156  VAL HIS ILE SER ASN ILE HIS GLN ARG GLU PRO PHE ARG          
SEQRES  10 L  156  HIS HIS SER TYR VAL SER GLN ARG ALA ASP GLY VAL VAL          
SEQRES  11 L  156  ALA GLY CYS GLY VAL GLN GLY TYR VAL PHE GLY VAL GLU          
SEQRES  12 L  156  ARG ILE ALA ALA LEU ALA GLY ALA GLY SER ALA ARG ALA          
HET    TRS  A 200       8                                                       
HET    TRS  D 200       8                                                       
HET    TRS  G 200       8                                                       
HET    TRS  J 200       8                                                       
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     TRS TRIS BUFFER                                                      
FORMUL  13  TRS    4(C4 H12 N O3 1+)                                            
FORMUL  17  HOH   *1740(H2 O1)                                                  
HELIX    1   1 ASN A   16  LEU A   20  5                                   5    
HELIX    2   2 THR A   32  HIS A   47  1                                  16    
HELIX    3   3 HIS A   58  HIS A   73  1                                  16    
HELIX    4   4 PRO A   80  THR A   86  5                                   7    
HELIX    5   5 SER A   87  THR A   96  1                                  10    
HELIX    6   6 ASN A  109  ARG A  113  5                                   5    
HELIX    7   7 GLU A  114  HIS A  119  5                                   6    
HELIX    8   8 TYR A  121  ARG A  125  5                                   5    
HELIX    9   9 VAL A  135  GLY A  150  1                                  16    
HELIX   10  10 ASN B   16  LEU B   20  5                                   5    
HELIX   11  11 THR B   32  HIS B   47  1                                  16    
HELIX   12  12 HIS B   58  HIS B   73  1                                  16    
HELIX   13  13 ALA B   82  SER B   87  1                                   6    
HELIX   14  14 SER B   87  CYS B   97  1                                  11    
HELIX   15  15 ASN B  109  ARG B  113  5                                   5    
HELIX   16  16 GLU B  114  HIS B  118  5                                   5    
HELIX   17  17 TYR B  121  ARG B  125  5                                   5    
HELIX   18  18 VAL B  135  GLY B  150  1                                  16    
HELIX   19  19 ASN C   16  LEU C   20  5                                   5    
HELIX   20  20 THR C   32  HIS C   47  1                                  16    
HELIX   21  21 HIS C   58  HIS C   73  1                                  16    
HELIX   22  22 ALA C   82  SER C   87  1                                   6    
HELIX   23  23 SER C   87  THR C   96  1                                  10    
HELIX   24  24 ASN C  109  ARG C  113  5                                   5    
HELIX   25  25 GLU C  114  HIS C  118  5                                   5    
HELIX   26  26 SER C  120  ARG C  125  5                                   6    
HELIX   27  27 VAL C  135  GLY C  150  1                                  16    
HELIX   28  28 ASN D   16  LEU D   20  5                                   5    
HELIX   29  29 THR D   32  ALA D   46  1                                  15    
HELIX   30  30 HIS D   58  HIS D   73  1                                  16    
HELIX   31  31 PRO D   80  HIS D   85  5                                   6    
HELIX   32  32 SER D   87  THR D   96  1                                  10    
HELIX   33  33 ASN D  109  ARG D  113  5                                   5    
HELIX   34  34 GLU D  114  HIS D  119  5                                   6    
HELIX   35  35 TYR D  121  ARG D  125  5                                   5    
HELIX   36  36 VAL D  135  GLY D  150  1                                  16    
HELIX   37  37 ASN E   16  LEU E   20  5                                   5    
HELIX   38  38 THR E   32  ALA E   46  1                                  15    
HELIX   39  39 HIS E   58  HIS E   73  1                                  16    
HELIX   40  40 ALA E   82  SER E   87  1                                   6    
HELIX   41  41 SER E   87  THR E   96  1                                  10    
HELIX   42  42 ASN E  109  ARG E  113  5                                   5    
HELIX   43  43 GLU E  114  HIS E  118  5                                   5    
HELIX   44  44 TYR E  121  ARG E  125  5                                   5    
HELIX   45  45 VAL E  135  GLY E  150  1                                  16    
HELIX   46  46 ASN F   16  LEU F   20  5                                   5    
HELIX   47  47 THR F   32  HIS F   47  1                                  16    
HELIX   48  48 HIS F   58  HIS F   73  1                                  16    
HELIX   49  49 ALA F   82  SER F   87  1                                   6    
HELIX   50  50 SER F   87  THR F   96  1                                  10    
HELIX   51  51 ASN F  109  ARG F  113  5                                   5    
HELIX   52  52 GLU F  114  HIS F  118  5                                   5    
HELIX   53  53 TYR F  121  ARG F  125  5                                   5    
HELIX   54  54 VAL F  135  GLY F  150  1                                  16    
HELIX   55  55 ASN G   16  LEU G   20  5                                   5    
HELIX   56  56 THR G   32  HIS G   47  1                                  16    
HELIX   57  57 HIS G   58  HIS G   73  1                                  16    
HELIX   58  58 ALA G   82  SER G   87  1                                   6    
HELIX   59  59 SER G   87  THR G   96  1                                  10    
HELIX   60  60 ASN G  109  ARG G  113  5                                   5    
HELIX   61  61 GLU G  114  HIS G  119  5                                   6    
HELIX   62  62 TYR G  121  ARG G  125  5                                   5    
HELIX   63  63 VAL G  135  GLY G  150  1                                  16    
HELIX   64  64 ASN H   16  LEU H   20  5                                   5    
HELIX   65  65 THR H   32  HIS H   47  1                                  16    
HELIX   66  66 HIS H   58  HIS H   73  1                                  16    
HELIX   67  67 PRO H   80  HIS H   85  5                                   6    
HELIX   68  68 SER H   87  THR H   96  1                                  10    
HELIX   69  69 ASN H  109  ARG H  113  5                                   5    
HELIX   70  70 GLU H  114  HIS H  118  5                                   5    
HELIX   71  71 TYR H  121  ARG H  125  5                                   5    
HELIX   72  72 VAL H  135  GLY H  150  1                                  16    
HELIX   73  73 ASN I   16  LEU I   20  5                                   5    
HELIX   74  74 THR I   32  HIS I   47  1                                  16    
HELIX   75  75 HIS I   58  HIS I   73  1                                  16    
HELIX   76  76 ALA I   82  SER I   87  1                                   6    
HELIX   77  77 SER I   87  THR I   96  1                                  10    
HELIX   78  78 ASN I  109  ARG I  113  5                                   5    
HELIX   79  79 GLU I  114  HIS I  119  5                                   6    
HELIX   80  80 TYR I  121  ARG I  125  5                                   5    
HELIX   81  81 VAL I  135  GLY I  150  1                                  16    
HELIX   82  82 ASN J   16  LEU J   20  5                                   5    
HELIX   83  83 THR J   32  HIS J   47  1                                  16    
HELIX   84  84 HIS J   58  HIS J   73  1                                  16    
HELIX   85  85 ALA J   82  SER J   87  1                                   6    
HELIX   86  86 SER J   87  THR J   96  1                                  10    
HELIX   87  87 ASN J  109  ARG J  113  5                                   5    
HELIX   88  88 GLU J  114  HIS J  119  5                                   6    
HELIX   89  89 TYR J  121  ARG J  125  5                                   5    
HELIX   90  90 VAL J  135  GLY J  150  1                                  16    
HELIX   91  91 ASN K   16  LEU K   20  5                                   5    
HELIX   92  92 THR K   32  HIS K   47  1                                  16    
HELIX   93  93 HIS K   58  HIS K   73  1                                  16    
HELIX   94  94 ALA K   82  SER K   87  1                                   6    
HELIX   95  95 SER K   87  THR K   96  1                                  10    
HELIX   96  96 ASN K  109  ARG K  113  5                                   5    
HELIX   97  97 GLU K  114  HIS K  118  5                                   5    
HELIX   98  98 TYR K  121  ARG K  125  5                                   5    
HELIX   99  99 VAL K  135  GLY K  150  1                                  16    
HELIX  100 100 ASN L   16  LEU L   20  5                                   5    
HELIX  101 101 THR L   32  HIS L   47  1                                  16    
HELIX  102 102 HIS L   58  HIS L   73  1                                  16    
HELIX  103 103 PRO L   80  THR L   86  5                                   7    
HELIX  104 104 SER L   87  ASN L   95  1                                   9    
HELIX  105 105 ASN L  109  ARG L  113  5                                   5    
HELIX  106 106 GLU L  114  HIS L  118  5                                   5    
HELIX  107 107 TYR L  121  ARG L  125  5                                   5    
HELIX  108 108 VAL L  135  GLY L  150  1                                  16    
SHEET    1  AA10 VAL A  51  GLN A  55  0                                        
SHEET    2  AA10 ILE A   9  ASN A  13  1  O  ILE A   9   N  ASP A  52           
SHEET    3  AA10 ILE A  76  ASN A  79  1  O  VAL A  77   N  LEU A  12           
SHEET    4  AA10 VAL A 102  HIS A 106  1  O  VAL A 103   N  ILE A  78           
SHEET    5  AA10 GLY A 128  ALA A 131  1  O  GLY A 128   N  GLU A 104           
SHEET    6  AA10 GLY D 128  ALA D 131 -1  O  VAL D 129   N  ALA A 131           
SHEET    7  AA10 VAL D 102  HIS D 106  1  O  GLU D 104   N  VAL D 130           
SHEET    8  AA10 GLY D  75  ASN D  79  1  O  ILE D  76   N  VAL D 103           
SHEET    9  AA10 ILE D   9  ASN D  13  1  O  MET D  10   N  VAL D  77           
SHEET   10  AA10 VAL D  51  GLN D  55  1  O  ASP D  52   N  ILE D  11           
SHEET    1  BA10 VAL B  51  GLN B  55  0                                        
SHEET    2  BA10 ILE B   9  ASN B  13  1  O  ILE B   9   N  ASP B  52           
SHEET    3  BA10 GLY B  75  ASN B  79  1  O  GLY B  75   N  MET B  10           
SHEET    4  BA10 VAL B 102  HIS B 106  1  O  VAL B 103   N  ILE B  78           
SHEET    5  BA10 GLY B 128  ALA B 131  1  O  GLY B 128   N  GLU B 104           
SHEET    6  BA10 GLY G 128  ALA G 131 -1  O  VAL G 129   N  ALA B 131           
SHEET    7  BA10 VAL G 102  HIS G 106  1  O  GLU G 104   N  VAL G 130           
SHEET    8  BA10 GLY G  75  ASN G  79  1  O  ILE G  76   N  VAL G 103           
SHEET    9  BA10 ILE G   9  ASN G  13  1  O  MET G  10   N  VAL G  77           
SHEET   10  BA10 VAL G  51  GLN G  55  1  O  ASP G  52   N  ILE G  11           
SHEET    1  CA10 VAL C  51  GLN C  55  0                                        
SHEET    2  CA10 ILE C   9  ASN C  13  1  O  ILE C   9   N  ASP C  52           
SHEET    3  CA10 ILE C  76  ASN C  79  1  O  VAL C  77   N  LEU C  12           
SHEET    4  CA10 VAL C 102  HIS C 106  1  O  VAL C 103   N  ILE C  78           
SHEET    5  CA10 GLY C 128  ALA C 131  1  O  GLY C 128   N  GLU C 104           
SHEET    6  CA10 GLY J 128  ALA J 131 -1  O  VAL J 129   N  ALA C 131           
SHEET    7  CA10 VAL J 102  HIS J 106  1  O  GLU J 104   N  VAL J 130           
SHEET    8  CA10 ILE J  76  ASN J  79  1  O  ILE J  76   N  VAL J 103           
SHEET    9  CA10 ILE J   9  ASN J  13  1  O  MET J  10   N  VAL J  77           
SHEET   10  CA10 VAL J  51  GLN J  55  1  O  ASP J  52   N  ILE J  11           
SHEET    1  EA10 VAL E  51  GLN E  55  0                                        
SHEET    2  EA10 ILE E   9  ASN E  13  1  O  ILE E   9   N  ASP E  52           
SHEET    3  EA10 ILE E  76  ASN E  79  1  O  VAL E  77   N  LEU E  12           
SHEET    4  EA10 VAL E 102  HIS E 106  1  O  VAL E 103   N  ILE E  78           
SHEET    5  EA10 GLY E 128  ALA E 131  1  O  GLY E 128   N  GLU E 104           
SHEET    6  EA10 GLY L 128  ALA L 131 -1  O  VAL L 129   N  ALA E 131           
SHEET    7  EA10 VAL L 102  HIS L 106  1  O  GLU L 104   N  VAL L 130           
SHEET    8  EA10 GLY L  75  ASN L  79  1  O  ILE L  76   N  VAL L 103           
SHEET    9  EA10 ILE L   9  ASN L  13  1  O  MET L  10   N  VAL L  77           
SHEET   10  EA10 VAL L  51  GLN L  55  1  O  ASP L  52   N  ILE L  11           
SHEET    1  FA10 VAL F  51  GLN F  55  0                                        
SHEET    2  FA10 ILE F   9  ASN F  13  1  O  ILE F   9   N  ASP F  52           
SHEET    3  FA10 ILE F  76  ASN F  79  1  O  VAL F  77   N  LEU F  12           
SHEET    4  FA10 VAL F 102  HIS F 106  1  O  VAL F 103   N  ILE F  78           
SHEET    5  FA10 GLY F 128  ALA F 131  1  O  GLY F 128   N  GLU F 104           
SHEET    6  FA10 GLY H 128  ALA H 131 -1  O  VAL H 129   N  ALA F 131           
SHEET    7  FA10 VAL H 102  HIS H 106  1  O  GLU H 104   N  VAL H 130           
SHEET    8  FA10 GLY H  75  ASN H  79  1  O  ILE H  76   N  VAL H 103           
SHEET    9  FA10 ILE H   9  ASN H  13  1  O  MET H  10   N  VAL H  77           
SHEET   10  FA10 VAL H  51  GLN H  55  1  O  ASP H  52   N  ILE H  11           
SHEET    1  IA10 VAL I  51  GLN I  55  0                                        
SHEET    2  IA10 ILE I   9  ASN I  13  1  O  ILE I   9   N  ASP I  52           
SHEET    3  IA10 ILE I  76  ASN I  79  1  O  VAL I  77   N  LEU I  12           
SHEET    4  IA10 VAL I 102  HIS I 106  1  O  VAL I 103   N  ILE I  78           
SHEET    5  IA10 GLY I 128  ALA I 131  1  O  GLY I 128   N  GLU I 104           
SHEET    6  IA10 GLY K 128  ALA K 131 -1  O  VAL K 129   N  ALA I 131           
SHEET    7  IA10 VAL K 102  HIS K 106  1  O  GLU K 104   N  VAL K 130           
SHEET    8  IA10 GLY K  75  ASN K  79  1  O  ILE K  76   N  VAL K 103           
SHEET    9  IA10 ILE K   9  ASN K  13  1  O  MET K  10   N  VAL K  77           
SHEET   10  IA10 VAL K  51  GLN K  55  1  O  ASP K  52   N  ILE K  11           
CISPEP   1 GLN G   24    PRO G   25          0         8.87                     
SITE     1 AC1  9 GLU A  59  THR A  86  SER A  87  GLU B  59                    
SITE     2 AC1  9 THR B  86  SER B  87  GLU C  59  THR C  86                    
SITE     3 AC1  9 SER C  87                                                     
SITE     1 AC2  6 GLU D  59  THR D  86  GLU E  59  THR E  86                    
SITE     2 AC2  6 GLU F  59  THR F  86                                          
SITE     1 AC3  9 GLU G  59  THR G  86  SER G  87  GLU H  59                    
SITE     2 AC3  9 THR H  86  SER H  87  GLU I  59  THR I  86                    
SITE     3 AC3  9 SER I  87                                                     
SITE     1 AC4  8 GLU J  59  THR J  86  SER J  87  GLU K  59                    
SITE     2 AC4  8 THR K  86  SER K  87  GLU L  59  THR L  86                    
CRYST1  116.200  138.400  141.200  90.00  90.00  90.00 P 21 21 21   48          
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      0.008606  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007225  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007082        0.00000                         
MTRIX1   1  0.007080  0.921540 -0.388220        8.23507    1                    
MTRIX2   1 -0.392020 -0.354600 -0.848870       85.55029    1                    
MTRIX3   1 -0.919930  0.158200  0.358750       40.90844    1                    
MTRIX1   2  0.008240 -0.397640 -0.917500       71.29705    1                    
MTRIX2   2  0.913590 -0.370050  0.168590       17.09995    1                    
MTRIX3   2  0.406560 -0.839610  0.360230       61.55885    1                    
MTRIX1   3 -0.999960  0.005020 -0.007760       54.49592    1                    
MTRIX2   3  0.009090  0.685100 -0.728390       34.82314    1                    
MTRIX3   3  0.001660 -0.728430 -0.685120       81.04834    1                    
MTRIX1   4  0.003520  0.918590 -0.395200        8.57029    1                    
MTRIX2   4  0.381440  0.364090  0.849670      -16.58185    1                    
MTRIX3   4  0.924390 -0.153730 -0.349100       24.99649    1                    
MTRIX1   5 -0.013030  0.399360  0.916700      -16.52143    1                    
MTRIX2   5 -0.919220 -0.365590  0.146200       67.34712    1                    
MTRIX3   5  0.393520 -0.840750  0.371860       39.30995    1                    
MTRIX1   6 -0.009830 -0.919910  0.392010       46.49717    1                    
MTRIX2   6  0.396350 -0.363500 -0.843070       64.12280    1                    
MTRIX3   6  0.918050  0.147090  0.368180       -9.06398    1                    
MTRIX1   7  0.007070 -0.398380 -0.917190       71.15918    1                    
MTRIX2   7 -0.917020  0.363190 -0.164820       52.28157    1                    
MTRIX3   7  0.398780  0.842250 -0.362760        5.18036    1                    
MTRIX1   8 -0.999900 -0.007460 -0.011850       54.99685    1                    
MTRIX2   8 -0.003480 -0.687640  0.726050       34.61080    1                    
MTRIX3   8 -0.013560  0.726020  0.687540      -14.26512    1                    
MTRIX1   9 -0.016030  0.396540  0.917880      -16.17982    1                    
MTRIX2   9  0.919130  0.367240 -0.142610        1.61710    1                    
MTRIX3   9 -0.393630  0.841360 -0.370350       27.03639    1                    
MTRIX1  10  0.999740  0.002640  0.022490       -0.76468    1                    
MTRIX2  10  0.002810 -0.999970 -0.007250       69.52921    1                    
MTRIX3  10  0.022470  0.007310 -0.999720       65.31114    1                    
MTRIX1  11 -0.002560 -0.921180  0.389130       46.60988    1                    
MTRIX2  11  0.412630  0.355430  0.838690        5.75645    1                    
MTRIX3  11  0.910890 -0.158420 -0.381020       76.06654    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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