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Entry: 2B8T
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HEADER    TRANSFERASE                             10-OCT-05   2B8T              
TITLE     CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM U.UREALYTICUM IN           
TITLE    2 COMPLEX WITH THYMIDINE                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THYMIDINE KINASE;                                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 2.7.1.21;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: UREAPLASMA PARVUM;                              
SOURCE   3 ORGANISM_TAXID: 134821;                                              
SOURCE   4 GENE: TDK;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-14B                                   
KEYWDS    DEOXYRIBONUCLEOSIDE KINASE, ZINC-BINDING DOMAIN, TK1, UU-TK,          
KEYWDS   2 THYMIDINE, TRANSFERASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.KOSINSKA,C.CARNROT,S.ERIKSSON,L.WANG,H.EKLUND                       
REVDAT   2   24-FEB-09 2B8T    1       VERSN                                    
REVDAT   1   20-DEC-05 2B8T    0                                                
JRNL        AUTH   U.KOSINSKA,C.CARNROT,S.ERIKSSON,L.WANG,H.EKLUND              
JRNL        TITL   STRUCTURE OF THE SUBSTRATE COMPLEX OF THYMIDINE              
JRNL        TITL 2 KINASE FROM UREAPLASMA UREALYTICUM AND                       
JRNL        TITL 3 INVESTIGATIONS OF POSSIBLE DRUG TARGETS FOR THE              
JRNL        TITL 4 ENZYME                                                       
JRNL        REF    FEBS LETT.                    V. 272  6365 2005              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   16336273                                                     
JRNL        DOI    10.1111/J.1742-4658.2005.05030.X                             
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 26.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 51687                          
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) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2769                            
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) : 3373                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.05                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 194                          
REMARK   3   BIN FREE R VALUE                    : 0.3330                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6380                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 80                                      
REMARK   3   SOLVENT ATOMS            : 230                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.94000                                             
REMARK   3    B22 (A**2) : 1.83000                                              
REMARK   3    B33 (A**2) : -0.94000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.16000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.207         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.173         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.134         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.921         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6600 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8913 ; 1.040 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   791 ; 5.178 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   315 ;32.991 ;24.286       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1144 ;13.424 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;12.463 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   976 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4978 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2793 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4575 ; 0.301 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   368 ; 0.125 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    43 ; 0.140 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.114 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4120 ; 0.367 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6434 ; 0.631 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2832 ; 0.912 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2479 ; 1.395 ; 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                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     12       A      49      5                      
REMARK   3           1     B     12       B      49      5                      
REMARK   3           1     C     12       C      49      5                      
REMARK   3           1     D     12       D      49      5                      
REMARK   3           2     A     69       A     213      5                      
REMARK   3           2     B     69       B     213      5                      
REMARK   3           2     C     69       C     213      5                      
REMARK   3           2     D     69       D     213      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    732 ;  0.19 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    732 ;  0.19 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):    732 ;  0.18 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):    732 ;  0.25 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    736 ;  0.56 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):    736 ;  0.63 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    C    (A):    736 ;  0.59 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    D    (A):    736 ;  0.65 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    732 ;  0.41 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):    732 ;  0.43 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):    732 ;  0.33 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):    732 ;  0.38 ;  2.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):    736 ;  0.95 ; 10.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):    736 ;  0.86 ; 10.00           
REMARK   3   LOOSE THERMAL      1    C (A**2):    736 ;  0.93 ; 10.00           
REMARK   3   LOOSE THERMAL      1    D (A**2):    736 ;  0.94 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 15                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    12        A    49                          
REMARK   3    RESIDUE RANGE :   A    69        A   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.3557  -8.6339  27.1632              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1597 T22:  -0.1135                                     
REMARK   3      T33:  -0.0830 T12:   0.0032                                     
REMARK   3      T13:  -0.0250 T23:   0.0272                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2816 L22:   1.8658                                     
REMARK   3      L33:   1.2389 L12:  -0.4011                                     
REMARK   3      L13:  -0.3242 L23:  -0.3421                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0710 S12:  -0.0321 S13:  -0.3674                       
REMARK   3      S21:  -0.0245 S22:  -0.0015 S23:   0.1640                       
REMARK   3      S31:   0.1376 S32:  -0.1932 S33:  -0.0695                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    50        A    68                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.6395   0.9466  35.7198              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1307 T22:   0.1218                                     
REMARK   3      T33:   0.0147 T12:  -0.1137                                     
REMARK   3      T13:  -0.0265 T23:   0.0164                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2095 L22:   2.4850                                     
REMARK   3      L33:  13.5932 L12:  -2.3286                                     
REMARK   3      L13:  -2.5893 L23:   3.3006                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0378 S12:  -0.4610 S13:   0.1318                       
REMARK   3      S21:   0.2198 S22:   0.0921 S23:  -0.4011                       
REMARK   3      S31:  -0.3453 S32:   0.0445 S33:  -0.1298                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   151        A   202                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.3730  12.8632  39.1810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0337 T22:  -0.0551                                     
REMARK   3      T33:  -0.0381 T12:   0.0555                                     
REMARK   3      T13:   0.0244 T23:  -0.0998                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8795 L22:   1.8074                                     
REMARK   3      L33:   5.4031 L12:   0.5102                                     
REMARK   3      L13:  -1.5875 L23:  -2.1066                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0801 S12:  -0.6234 S13:   0.7695                       
REMARK   3      S21:   0.1591 S22:   0.0211 S23:   0.0896                       
REMARK   3      S31:  -0.5242 S32:  -0.1340 S33:  -0.1012                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   203        A   213                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.7976  11.2879  51.7534              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0864 T22:   0.1906                                     
REMARK   3      T33:   0.0175 T12:   0.0046                                     
REMARK   3      T13:   0.0525 T23:  -0.2452                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  16.2404 L22:  32.6134                                     
REMARK   3      L33:   7.8055 L12:   8.3730                                     
REMARK   3      L13:   3.5967 L23:  -4.3715                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1286 S12:  -1.7334 S13:   1.5273                       
REMARK   3      S21:  -0.3242 S22:  -0.4497 S23:   0.1948                       
REMARK   3      S31:  -0.9721 S32:  -0.2616 S33:   0.5784                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    12        B    50                          
REMARK   3    RESIDUE RANGE :   B    69        B   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2028  13.8675   7.0462              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0548 T22:  -0.0388                                     
REMARK   3      T33:   0.0109 T12:   0.0651                                     
REMARK   3      T13:   0.0288 T23:   0.0864                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0449 L22:   2.0942                                     
REMARK   3      L33:   2.0015 L12:   0.2352                                     
REMARK   3      L13:  -0.2402 L23:   0.7642                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1337 S12:   0.3588 S13:   0.6218                       
REMARK   3      S21:  -0.1912 S22:   0.0870 S23:   0.0350                       
REMARK   3      S31:  -0.5829 S32:  -0.1463 S33:  -0.2207                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   151        B   202                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.5399  -7.8824  -4.6565              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0068 T22:   0.1093                                     
REMARK   3      T33:  -0.1181 T12:  -0.0108                                     
REMARK   3      T13:  -0.0417 T23:  -0.0943                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9982 L22:   2.6591                                     
REMARK   3      L33:   8.0392 L12:  -0.2112                                     
REMARK   3      L13:  -1.5894 L23:  -2.0439                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0022 S12:   0.7963 S13:  -0.5102                       
REMARK   3      S21:  -0.3634 S22:  -0.0519 S23:   0.2059                       
REMARK   3      S31:   0.4689 S32:  -0.5302 S33:   0.0541                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   203        B   213                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6491 -15.1081  -9.0856              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4103 T22:   0.2058                                     
REMARK   3      T33:   0.0474 T12:   0.1277                                     
REMARK   3      T13:  -0.1075 T23:  -0.2038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8194 L22:  10.6337                                     
REMARK   3      L33:   4.2125 L12:   3.3822                                     
REMARK   3      L13:  -2.0917 L23:  -3.1456                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3742 S12:   1.3108 S13:  -0.9911                       
REMARK   3      S21:  -1.2337 S22:  -0.4760 S23:   0.3215                       
REMARK   3      S31:   1.3933 S32:  -0.1089 S33:   0.1017                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    12        C    49                          
REMARK   3    RESIDUE RANGE :   C    69        C   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.4083   0.8403  36.9784              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1601 T22:  -0.0650                                     
REMARK   3      T33:  -0.1666 T12:   0.0080                                     
REMARK   3      T13:  -0.0047 T23:   0.0195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8631 L22:   1.3904                                     
REMARK   3      L33:   1.6626 L12:   0.0480                                     
REMARK   3      L13:  -0.1515 L23:   0.1002                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0825 S12:  -0.3653 S13:   0.0675                       
REMARK   3      S21:   0.1548 S22:  -0.0549 S23:  -0.0120                       
REMARK   3      S31:  -0.1370 S32:   0.1512 S33:  -0.0276                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    50        C    51                          
REMARK   3    RESIDUE RANGE :   C    60        C    68                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.2416  -7.2563  32.6239              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1504 T22:   0.1494                                     
REMARK   3      T33:  -0.0589 T12:   0.0389                                     
REMARK   3      T13:  -0.0618 T23:   0.0911                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2423 L22:   0.4712                                     
REMARK   3      L33:  15.3041 L12:   1.2949                                     
REMARK   3      L13:  -2.9420 L23:   0.1057                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0642 S12:  -0.7408 S13:  -0.7673                       
REMARK   3      S21:  -0.0056 S22:   0.2959 S23:   0.0396                       
REMARK   3      S31:   0.8697 S32:   0.4192 S33:  -0.2317                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   151        C   202                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4316 -23.1258  32.8321              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0733 T22:  -0.1808                                     
REMARK   3      T33:   0.0735 T12:   0.0392                                     
REMARK   3      T13:  -0.0118 T23:   0.1093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1777 L22:   2.5028                                     
REMARK   3      L33:   6.7947 L12:  -0.3206                                     
REMARK   3      L13:  -0.1348 L23:  -1.0277                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0700 S12:  -0.2657 S13:  -0.7704                       
REMARK   3      S21:   0.0937 S22:  -0.0351 S23:  -0.0618                       
REMARK   3      S31:   0.5971 S32:   0.1577 S33:  -0.0349                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   203        C   213                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.9404 -25.9047  33.8669              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0201 T22:  -0.1481                                     
REMARK   3      T33:   0.4198 T12:  -0.0117                                     
REMARK   3      T13:  -0.0111 T23:   0.1781                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3487 L22:  18.5814                                     
REMARK   3      L33:  21.3696 L12:   4.6467                                     
REMARK   3      L13:   3.4301 L23:  11.7954                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1348 S12:  -0.5004 S13:  -1.4212                       
REMARK   3      S21:   0.0551 S22:  -0.1555 S23:   0.0813                       
REMARK   3      S31:   1.2799 S32:  -0.1358 S33:   0.0208                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    12        D    49                          
REMARK   3    RESIDUE RANGE :   D    69        D   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.6624  -5.9601   6.9238              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1196 T22:  -0.0875                                     
REMARK   3      T33:  -0.1613 T12:   0.0482                                     
REMARK   3      T13:   0.0061 T23:   0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1018 L22:   1.4249                                     
REMARK   3      L33:   3.5610 L12:  -0.2958                                     
REMARK   3      L13:   0.0913 L23:   0.0902                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0439 S12:   0.2412 S13:  -0.1432                       
REMARK   3      S21:  -0.2591 S22:  -0.0533 S23:  -0.1022                       
REMARK   3      S31:   0.1335 S32:   0.2165 S33:   0.0093                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    54        D    66                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.7111  -4.6044  15.7533              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1131 T22:   0.0280                                     
REMARK   3      T33:  -0.0512 T12:   0.0391                                     
REMARK   3      T13:   0.0552 T23:   0.0358                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6452 L22:   9.0359                                     
REMARK   3      L33:  16.6142 L12:   0.3052                                     
REMARK   3      L13:   0.8210 L23:  12.1543                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2928 S12:   0.3152 S13:   0.0344                       
REMARK   3      S21:  -0.8647 S22:   0.2132 S23:  -0.4597                       
REMARK   3      S31:  -0.8847 S32:   1.0784 S33:  -0.5060                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   151        D   201                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.0235  18.0556  11.2159              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0999 T22:  -0.0273                                     
REMARK   3      T33:   0.1336 T12:  -0.1271                                     
REMARK   3      T13:   0.0289 T23:   0.0906                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4836 L22:   4.9133                                     
REMARK   3      L33:   9.9747 L12:  -0.1613                                     
REMARK   3      L13:  -1.0802 L23:  -0.6579                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0171 S12:   0.2871 S13:   0.7824                       
REMARK   3      S21:  -0.2820 S22:  -0.0772 S23:  -0.7370                       
REMARK   3      S31:  -0.8846 S32:   1.0554 S33:   0.0943                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   203        D   213                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0839  29.9267   1.6253              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4817 T22:   0.0406                                     
REMARK   3      T33:   0.7019 T12:   0.1050                                     
REMARK   3      T13:   0.1332 T23:   0.2728                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8941 L22:   6.3485                                     
REMARK   3      L33:   2.1065 L12:   6.6157                                     
REMARK   3      L13:   3.8108 L23:   3.6569                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6026 S12:   0.8188 S13:   1.8930                       
REMARK   3      S21:   0.5778 S22:  -0.7694 S23:  -0.6744                       
REMARK   3      S31:  -0.2806 S32:  -0.7857 S33:   0.1668                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2B8T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-OCT-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB034818.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.931                              
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)             
REMARK 200  OPTICS                         : TOROIDAL MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PRODC                              
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54484                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.950                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : 0.08200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.42400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1XMR                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG3350, 0.3 M AMMONIUM              
REMARK 280  FORMATE, PH 6.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  287K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       57.82450            
REMARK 290   SMTRY3   2  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 300 REMARK: THE CONTENTS IN THE ASYMMETRIC UNIT REPRESENTS THE           
REMARK 300 BIOLOGICAL ASSEMBLY I.E. A TETRAMER.                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14360 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 35550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     PHE A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     LYS A    10                                                      
REMARK 465     LYS A   217                                                      
REMARK 465     LYS A   218                                                      
REMARK 465     ARG A   219                                                      
REMARK 465     ASN A   220                                                      
REMARK 465     LYS A   221                                                      
REMARK 465     ASN A   222                                                      
REMARK 465     ILE A   223                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     ASN B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     PHE B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     LYS B     9                                                      
REMARK 465     LYS B    10                                                      
REMARK 465     ASP B    51                                                      
REMARK 465     THR B    52                                                      
REMARK 465     ARG B    53                                                      
REMARK 465     SER B    54                                                      
REMARK 465     ILE B    55                                                      
REMARK 465     ARG B    56                                                      
REMARK 465     ASN B    57                                                      
REMARK 465     ILE B    58                                                      
REMARK 465     GLN B    59                                                      
REMARK 465     SER B    60                                                      
REMARK 465     ARG B    61                                                      
REMARK 465     THR B    62                                                      
REMARK 465     GLY B    63                                                      
REMARK 465     THR B    64                                                      
REMARK 465     SER B    65                                                      
REMARK 465     LYS B   215                                                      
REMARK 465     ASN B   216                                                      
REMARK 465     LYS B   217                                                      
REMARK 465     LYS B   218                                                      
REMARK 465     ARG B   219                                                      
REMARK 465     ASN B   220                                                      
REMARK 465     LYS B   221                                                      
REMARK 465     ASN B   222                                                      
REMARK 465     ILE B   223                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     VAL C     4                                                      
REMARK 465     ASN C     5                                                      
REMARK 465     ALA C     6                                                      
REMARK 465     PHE C     7                                                      
REMARK 465     SER C     8                                                      
REMARK 465     LYS C     9                                                      
REMARK 465     LYS C    10                                                      
REMARK 465     THR C    52                                                      
REMARK 465     ARG C    53                                                      
REMARK 465     SER C    54                                                      
REMARK 465     ILE C    55                                                      
REMARK 465     ARG C    56                                                      
REMARK 465     ASN C    57                                                      
REMARK 465     ILE C    58                                                      
REMARK 465     GLN C    59                                                      
REMARK 465     LYS C   218                                                      
REMARK 465     ARG C   219                                                      
REMARK 465     ASN C   220                                                      
REMARK 465     LYS C   221                                                      
REMARK 465     ASN C   222                                                      
REMARK 465     ILE C   223                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     LYS D     3                                                      
REMARK 465     VAL D     4                                                      
REMARK 465     ASN D     5                                                      
REMARK 465     ALA D     6                                                      
REMARK 465     PHE D     7                                                      
REMARK 465     SER D     8                                                      
REMARK 465     LYS D     9                                                      
REMARK 465     LYS D    10                                                      
REMARK 465     ILE D    11                                                      
REMARK 465     ILE D    50                                                      
REMARK 465     ASP D    51                                                      
REMARK 465     THR D    52                                                      
REMARK 465     ARG D    53                                                      
REMARK 465     ASN D   220                                                      
REMARK 465     LYS D   221                                                      
REMARK 465     ASN D   222                                                      
REMARK 465     ILE D   223                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS D 217    CG   CD   CE   NZ                                   
REMARK 470     LYS D 218    CG   CD   CE   NZ                                   
REMARK 470     ARG D 219    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS A 183     -128.43   -118.36                                   
REMARK 500    ASP B 168       47.90   -147.62                                   
REMARK 500    CYS B 183     -131.77   -114.34                                   
REMARK 500    ASP C 102     -168.39   -100.10                                   
REMARK 500    CYS C 183     -122.53   -122.82                                   
REMARK 500    ASP D 102     -168.57   -100.01                                   
REMARK 500    CYS D 183     -132.71   -109.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1218  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 153   SG                                                     
REMARK 620 2 CYS A 156   SG  106.6                                              
REMARK 620 3 HIS A 194   ND1 114.5 114.4                                        
REMARK 620 4 CYS A 191   SG  115.8 111.4  94.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B2218  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 194   ND1                                                    
REMARK 620 2 CYS B 156   SG  110.5                                              
REMARK 620 3 CYS B 153   SG  106.6 113.7                                        
REMARK 620 4 CYS B 191   SG  100.5 111.2 113.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C3218  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 156   SG                                                     
REMARK 620 2 CYS C 153   SG  114.4                                              
REMARK 620 3 HIS C 194   ND1 109.2 112.9                                        
REMARK 620 4 CYS C 191   SG  113.0 116.0  88.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D4218  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 156   SG                                                     
REMARK 620 2 HIS D 194   ND1 106.7                                              
REMARK 620 3 CYS D 153   SG  107.9 115.6                                        
REMARK 620 4 CYS D 191   SG  113.3  93.7 118.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1218                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2218                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 3218                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 4218                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THM A 4970                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THM B 5970                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THM C 6970                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THM D 7970                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS D 5006                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1XMR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THYMIDINE KINASE WITH DTTP FROM U.              
REMARK 900 UREALYTICUM                                                          
DBREF  2B8T A    1   223  UNP    Q9PPP5   KITH_UREPA       1    223             
DBREF  2B8T B    1   223  UNP    Q9PPP5   KITH_UREPA       1    223             
DBREF  2B8T C    1   223  UNP    Q9PPP5   KITH_UREPA       1    223             
DBREF  2B8T D    1   223  UNP    Q9PPP5   KITH_UREPA       1    223             
SEQADV 2B8T PHE A   16  UNP  Q9PPP5    LEU    16 ENGINEERED                     
SEQADV 2B8T PHE B   16  UNP  Q9PPP5    LEU    16 ENGINEERED                     
SEQADV 2B8T PHE C   16  UNP  Q9PPP5    LEU    16 ENGINEERED                     
SEQADV 2B8T PHE D   16  UNP  Q9PPP5    LEU    16 ENGINEERED                     
SEQRES   1 A  223  MET ALA LYS VAL ASN ALA PHE SER LYS LYS ILE GLY TRP          
SEQRES   2 A  223  ILE GLU PHE ILE THR GLY PRO MET PHE ALA GLY LYS THR          
SEQRES   3 A  223  ALA GLU LEU ILE ARG ARG LEU HIS ARG LEU GLU TYR ALA          
SEQRES   4 A  223  ASP VAL LYS TYR LEU VAL PHE LYS PRO LYS ILE ASP THR          
SEQRES   5 A  223  ARG SER ILE ARG ASN ILE GLN SER ARG THR GLY THR SER          
SEQRES   6 A  223  LEU PRO SER VAL GLU VAL GLU SER ALA PRO GLU ILE LEU          
SEQRES   7 A  223  ASN TYR ILE MET SER ASN SER PHE ASN ASP GLU THR LYS          
SEQRES   8 A  223  VAL ILE GLY ILE ASP GLU VAL GLN PHE PHE ASP ASP ARG          
SEQRES   9 A  223  ILE CYS GLU VAL ALA ASN ILE LEU ALA GLU ASN GLY PHE          
SEQRES  10 A  223  VAL VAL ILE ILE SER GLY LEU ASP LYS ASN PHE LYS GLY          
SEQRES  11 A  223  GLU PRO PHE GLY PRO ILE ALA LYS LEU PHE THR TYR ALA          
SEQRES  12 A  223  ASP LYS ILE THR LYS LEU THR ALA ILE CYS ASN GLU CYS          
SEQRES  13 A  223  GLY ALA GLU ALA THR HIS SER LEU ARG LYS ILE ASP GLY          
SEQRES  14 A  223  LYS HIS ALA ASP TYR ASN ASP ASP ILE VAL LYS ILE GLY          
SEQRES  15 A  223  CYS GLN GLU PHE TYR SER ALA VAL CYS ARG HIS HIS HIS          
SEQRES  16 A  223  LYS VAL PRO ASN ARG PRO TYR LEU ASN SER ASN SER GLU          
SEQRES  17 A  223  GLU PHE ILE LYS PHE PHE LYS ASN LYS LYS ARG ASN LYS          
SEQRES  18 A  223  ASN ILE                                                      
SEQRES   1 B  223  MET ALA LYS VAL ASN ALA PHE SER LYS LYS ILE GLY TRP          
SEQRES   2 B  223  ILE GLU PHE ILE THR GLY PRO MET PHE ALA GLY LYS THR          
SEQRES   3 B  223  ALA GLU LEU ILE ARG ARG LEU HIS ARG LEU GLU TYR ALA          
SEQRES   4 B  223  ASP VAL LYS TYR LEU VAL PHE LYS PRO LYS ILE ASP THR          
SEQRES   5 B  223  ARG SER ILE ARG ASN ILE GLN SER ARG THR GLY THR SER          
SEQRES   6 B  223  LEU PRO SER VAL GLU VAL GLU SER ALA PRO GLU ILE LEU          
SEQRES   7 B  223  ASN TYR ILE MET SER ASN SER PHE ASN ASP GLU THR LYS          
SEQRES   8 B  223  VAL ILE GLY ILE ASP GLU VAL GLN PHE PHE ASP ASP ARG          
SEQRES   9 B  223  ILE CYS GLU VAL ALA ASN ILE LEU ALA GLU ASN GLY PHE          
SEQRES  10 B  223  VAL VAL ILE ILE SER GLY LEU ASP LYS ASN PHE LYS GLY          
SEQRES  11 B  223  GLU PRO PHE GLY PRO ILE ALA LYS LEU PHE THR TYR ALA          
SEQRES  12 B  223  ASP LYS ILE THR LYS LEU THR ALA ILE CYS ASN GLU CYS          
SEQRES  13 B  223  GLY ALA GLU ALA THR HIS SER LEU ARG LYS ILE ASP GLY          
SEQRES  14 B  223  LYS HIS ALA ASP TYR ASN ASP ASP ILE VAL LYS ILE GLY          
SEQRES  15 B  223  CYS GLN GLU PHE TYR SER ALA VAL CYS ARG HIS HIS HIS          
SEQRES  16 B  223  LYS VAL PRO ASN ARG PRO TYR LEU ASN SER ASN SER GLU          
SEQRES  17 B  223  GLU PHE ILE LYS PHE PHE LYS ASN LYS LYS ARG ASN LYS          
SEQRES  18 B  223  ASN ILE                                                      
SEQRES   1 C  223  MET ALA LYS VAL ASN ALA PHE SER LYS LYS ILE GLY TRP          
SEQRES   2 C  223  ILE GLU PHE ILE THR GLY PRO MET PHE ALA GLY LYS THR          
SEQRES   3 C  223  ALA GLU LEU ILE ARG ARG LEU HIS ARG LEU GLU TYR ALA          
SEQRES   4 C  223  ASP VAL LYS TYR LEU VAL PHE LYS PRO LYS ILE ASP THR          
SEQRES   5 C  223  ARG SER ILE ARG ASN ILE GLN SER ARG THR GLY THR SER          
SEQRES   6 C  223  LEU PRO SER VAL GLU VAL GLU SER ALA PRO GLU ILE LEU          
SEQRES   7 C  223  ASN TYR ILE MET SER ASN SER PHE ASN ASP GLU THR LYS          
SEQRES   8 C  223  VAL ILE GLY ILE ASP GLU VAL GLN PHE PHE ASP ASP ARG          
SEQRES   9 C  223  ILE CYS GLU VAL ALA ASN ILE LEU ALA GLU ASN GLY PHE          
SEQRES  10 C  223  VAL VAL ILE ILE SER GLY LEU ASP LYS ASN PHE LYS GLY          
SEQRES  11 C  223  GLU PRO PHE GLY PRO ILE ALA LYS LEU PHE THR TYR ALA          
SEQRES  12 C  223  ASP LYS ILE THR LYS LEU THR ALA ILE CYS ASN GLU CYS          
SEQRES  13 C  223  GLY ALA GLU ALA THR HIS SER LEU ARG LYS ILE ASP GLY          
SEQRES  14 C  223  LYS HIS ALA ASP TYR ASN ASP ASP ILE VAL LYS ILE GLY          
SEQRES  15 C  223  CYS GLN GLU PHE TYR SER ALA VAL CYS ARG HIS HIS HIS          
SEQRES  16 C  223  LYS VAL PRO ASN ARG PRO TYR LEU ASN SER ASN SER GLU          
SEQRES  17 C  223  GLU PHE ILE LYS PHE PHE LYS ASN LYS LYS ARG ASN LYS          
SEQRES  18 C  223  ASN ILE                                                      
SEQRES   1 D  223  MET ALA LYS VAL ASN ALA PHE SER LYS LYS ILE GLY TRP          
SEQRES   2 D  223  ILE GLU PHE ILE THR GLY PRO MET PHE ALA GLY LYS THR          
SEQRES   3 D  223  ALA GLU LEU ILE ARG ARG LEU HIS ARG LEU GLU TYR ALA          
SEQRES   4 D  223  ASP VAL LYS TYR LEU VAL PHE LYS PRO LYS ILE ASP THR          
SEQRES   5 D  223  ARG SER ILE ARG ASN ILE GLN SER ARG THR GLY THR SER          
SEQRES   6 D  223  LEU PRO SER VAL GLU VAL GLU SER ALA PRO GLU ILE LEU          
SEQRES   7 D  223  ASN TYR ILE MET SER ASN SER PHE ASN ASP GLU THR LYS          
SEQRES   8 D  223  VAL ILE GLY ILE ASP GLU VAL GLN PHE PHE ASP ASP ARG          
SEQRES   9 D  223  ILE CYS GLU VAL ALA ASN ILE LEU ALA GLU ASN GLY PHE          
SEQRES  10 D  223  VAL VAL ILE ILE SER GLY LEU ASP LYS ASN PHE LYS GLY          
SEQRES  11 D  223  GLU PRO PHE GLY PRO ILE ALA LYS LEU PHE THR TYR ALA          
SEQRES  12 D  223  ASP LYS ILE THR LYS LEU THR ALA ILE CYS ASN GLU CYS          
SEQRES  13 D  223  GLY ALA GLU ALA THR HIS SER LEU ARG LYS ILE ASP GLY          
SEQRES  14 D  223  LYS HIS ALA ASP TYR ASN ASP ASP ILE VAL LYS ILE GLY          
SEQRES  15 D  223  CYS GLN GLU PHE TYR SER ALA VAL CYS ARG HIS HIS HIS          
SEQRES  16 D  223  LYS VAL PRO ASN ARG PRO TYR LEU ASN SER ASN SER GLU          
SEQRES  17 D  223  GLU PHE ILE LYS PHE PHE LYS ASN LYS LYS ARG ASN LYS          
SEQRES  18 D  223  ASN ILE                                                      
HET     ZN  A1218       1                                                       
HET     ZN  B2218       1                                                       
HET     ZN  C3218       1                                                       
HET     ZN  D4218       1                                                       
HET    THM  A4970      17                                                       
HET    THM  B5970      17                                                       
HET    THM  C6970      17                                                       
HET    THM  D7970      17                                                       
HET    TRS  D5006       8                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     THM THYMIDINE                                                        
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     THM DEOXYTHYMIDINE; 2'-DEOXYTHYMIDINE                                
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   9  THM    4(C10 H14 N2 O5)                                             
FORMUL  13  TRS    C4 H12 N O3 1+                                               
FORMUL  14  HOH   *230(H2 O)                                                    
HELIX    1   1 GLY A   24  ALA A   39  1                                  16    
HELIX    2   2 ASP A   51  ILE A   55  5                                   5    
HELIX    3   3 ALA A   74  SER A   83  1                                  10    
HELIX    4   4 GLU A   97  PHE A  101  5                                   5    
HELIX    5   5 ASP A  102  ASP A  103  5                                   2    
HELIX    6   6 ARG A  104  ASN A  115  1                                  12    
HELIX    7   7 PRO A  135  ALA A  143  1                                   9    
HELIX    8   8 CYS A  191  HIS A  195  5                                   5    
HELIX    9   9 ASN A  206  ASN A  216  1                                  11    
HELIX   10  10 GLY B   24  ALA B   39  1                                  16    
HELIX   11  11 ALA B   74  SER B   83  1                                  10    
HELIX   12  12 GLU B   97  PHE B  101  5                                   5    
HELIX   13  13 ASP B  102  ASP B  103  5                                   2    
HELIX   14  14 ARG B  104  ASN B  115  1                                  12    
HELIX   15  15 PRO B  135  ALA B  143  1                                   9    
HELIX   16  16 CYS B  191  HIS B  195  5                                   5    
HELIX   17  17 ASN B  206  PHE B  214  1                                   9    
HELIX   18  18 GLY C   24  ARG C   35  1                                  12    
HELIX   19  19 LEU C   36  ASP C   40  5                                   5    
HELIX   20  20 ALA C   74  MET C   82  1                                   9    
HELIX   21  21 GLU C   97  PHE C  101  5                                   5    
HELIX   22  22 ASP C  102  ASP C  103  5                                   2    
HELIX   23  23 ARG C  104  ASN C  115  1                                  12    
HELIX   24  24 PRO C  135  ALA C  143  1                                   9    
HELIX   25  25 CYS C  191  HIS C  195  5                                   5    
HELIX   26  26 ASN C  206  ASN C  216  1                                  11    
HELIX   27  27 GLY D   24  ALA D   39  1                                  16    
HELIX   28  28 ALA D   74  MET D   82  1                                   9    
HELIX   29  29 GLU D   97  PHE D  101  5                                   5    
HELIX   30  30 ASP D  102  ASP D  103  5                                   2    
HELIX   31  31 ARG D  104  ASN D  115  1                                  12    
HELIX   32  32 PRO D  135  ALA D  143  1                                   9    
HELIX   33  33 ASN D  206  ASN D  216  1                                  11    
SHEET    1   A 6 VAL A  69  VAL A  71  0                                        
SHEET    2   A 6 TYR A  43  PRO A  48  1  N  VAL A  45   O  VAL A  69           
SHEET    3   A 6 VAL A  92  ILE A  95  1  O  GLY A  94   N  PHE A  46           
SHEET    4   A 6 VAL A 118  SER A 122  1  O  SER A 122   N  ILE A  95           
SHEET    5   A 6 TRP A  13  THR A  18  1  N  GLU A  15   O  ILE A 121           
SHEET    6   A 6 LYS A 145  LYS A 148  1  O  THR A 147   N  THR A  18           
SHEET    1   B 2 ALA A 151  ILE A 152  0                                        
SHEET    2   B 2 GLU A 159  ALA A 160 -1  O  ALA A 160   N  ALA A 151           
SHEET    1   C 3 LYS A 170  HIS A 171  0                                        
SHEET    2   C 3 HIS A 162  ILE A 167 -1  N  ILE A 167   O  LYS A 170           
SHEET    3   C 3 TYR A 187  VAL A 190 -1  O  SER A 188   N  LEU A 164           
SHEET    1   D 6 VAL B  69  VAL B  71  0                                        
SHEET    2   D 6 TYR B  43  PRO B  48  1  N  LYS B  47   O  VAL B  69           
SHEET    3   D 6 VAL B  92  ILE B  95  1  O  GLY B  94   N  LEU B  44           
SHEET    4   D 6 VAL B 118  SER B 122  1  O  VAL B 118   N  ILE B  93           
SHEET    5   D 6 TRP B  13  THR B  18  1  N  ILE B  17   O  ILE B 121           
SHEET    6   D 6 LYS B 145  LYS B 148  1  O  THR B 147   N  THR B  18           
SHEET    1   E 2 ALA B 151  ILE B 152  0                                        
SHEET    2   E 2 GLU B 159  ALA B 160 -1  O  ALA B 160   N  ALA B 151           
SHEET    1   F 2 HIS B 162  ARG B 165  0                                        
SHEET    2   F 2 TYR B 187  VAL B 190 -1  O  SER B 188   N  LEU B 164           
SHEET    1   G 6 SER C  68  VAL C  71  0                                        
SHEET    2   G 6 TYR C  43  PRO C  48  1  N  VAL C  45   O  VAL C  69           
SHEET    3   G 6 VAL C  92  ILE C  95  1  O  GLY C  94   N  LEU C  44           
SHEET    4   G 6 VAL C 118  SER C 122  1  O  VAL C 118   N  ILE C  93           
SHEET    5   G 6 TRP C  13  THR C  18  1  N  GLU C  15   O  ILE C 121           
SHEET    6   G 6 LYS C 145  LYS C 148  1  O  THR C 147   N  THR C  18           
SHEET    1   H 2 ALA C 151  ILE C 152  0                                        
SHEET    2   H 2 GLU C 159  ALA C 160 -1  O  ALA C 160   N  ALA C 151           
SHEET    1   I 3 LYS C 170  HIS C 171  0                                        
SHEET    2   I 3 HIS C 162  ILE C 167 -1  N  ILE C 167   O  LYS C 170           
SHEET    3   I 3 TYR C 187  VAL C 190 -1  O  SER C 188   N  LEU C 164           
SHEET    1   J 6 VAL D  69  VAL D  71  0                                        
SHEET    2   J 6 TYR D  43  PRO D  48  1  N  VAL D  45   O  VAL D  69           
SHEET    3   J 6 VAL D  92  ILE D  95  1  O  GLY D  94   N  LEU D  44           
SHEET    4   J 6 VAL D 118  SER D 122  1  O  SER D 122   N  ILE D  95           
SHEET    5   J 6 TRP D  13  THR D  18  1  N  ILE D  17   O  ILE D 121           
SHEET    6   J 6 LYS D 145  LYS D 148  1  O  THR D 147   N  THR D  18           
SHEET    1   K 2 ASN D  57  GLN D  59  0                                        
SHEET    2   K 2 SER D  65  PRO D  67 -1  O  LEU D  66   N  ILE D  58           
SHEET    1   L 2 ALA D 151  ILE D 152  0                                        
SHEET    2   L 2 GLU D 159  ALA D 160 -1  O  ALA D 160   N  ALA D 151           
SHEET    1   M 3 LYS D 170  HIS D 171  0                                        
SHEET    2   M 3 HIS D 162  ILE D 167 -1  N  ILE D 167   O  LYS D 170           
SHEET    3   M 3 TYR D 187  VAL D 190 -1  O  SER D 188   N  LEU D 164           
LINK        ZN    ZN A1218                 SG  CYS A 153     1555   1555  2.41  
LINK        ZN    ZN A1218                 SG  CYS A 156     1555   1555  2.41  
LINK        ZN    ZN A1218                 ND1 HIS A 194     1555   1555  2.11  
LINK        ZN    ZN A1218                 SG  CYS A 191     1555   1555  2.33  
LINK        ZN    ZN B2218                 ND1 HIS B 194     1555   1555  2.14  
LINK        ZN    ZN B2218                 SG  CYS B 156     1555   1555  2.36  
LINK        ZN    ZN B2218                 SG  CYS B 153     1555   1555  2.35  
LINK        ZN    ZN B2218                 SG  CYS B 191     1555   1555  2.39  
LINK        ZN    ZN C3218                 SG  CYS C 156     1555   1555  2.21  
LINK        ZN    ZN C3218                 SG  CYS C 153     1555   1555  2.30  
LINK        ZN    ZN C3218                 ND1 HIS C 194     1555   1555  2.15  
LINK        ZN    ZN C3218                 SG  CYS C 191     1555   1555  2.39  
LINK        ZN    ZN D4218                 SG  CYS D 156     1555   1555  2.35  
LINK        ZN    ZN D4218                 ND1 HIS D 194     1555   1555  2.13  
LINK        ZN    ZN D4218                 SG  CYS D 153     1555   1555  2.30  
LINK        ZN    ZN D4218                 SG  CYS D 191     1555   1555  2.31  
SITE     1 AC1  4 CYS A 153  CYS A 156  CYS A 191  HIS A 194                    
SITE     1 AC2  4 CYS B 153  CYS B 156  CYS B 191  HIS B 194                    
SITE     1 AC3  4 CYS C 153  CYS C 156  CYS C 191  HIS C 194                    
SITE     1 AC4  4 CYS D 153  CYS D 156  CYS D 191  HIS D 194                    
SITE     1 AC5 14 GLU A  97  PHE A 100  LEU A 124  ASN A 127                    
SITE     2 AC5 14 PHE A 128  PHE A 133  SER A 163  ARG A 165                    
SITE     3 AC5 14 ILE A 178  VAL A 179  LYS A 180  ILE A 181                    
SITE     4 AC5 14 GLY A 182  TYR A 187                                          
SITE     1 AC6 14 GLU B  97  PHE B 100  LEU B 124  ASN B 127                    
SITE     2 AC6 14 PHE B 128  PHE B 133  SER B 163  ARG B 165                    
SITE     3 AC6 14 ILE B 178  VAL B 179  LYS B 180  ILE B 181                    
SITE     4 AC6 14 GLY B 182  TYR B 187                                          
SITE     1 AC7 14 GLU C  97  PHE C 100  LEU C 124  ASN C 127                    
SITE     2 AC7 14 PHE C 128  PHE C 133  SER C 163  ARG C 165                    
SITE     3 AC7 14 ILE C 178  VAL C 179  LYS C 180  ILE C 181                    
SITE     4 AC7 14 GLY C 182  TYR C 187                                          
SITE     1 AC8 14 GLU D  97  PHE D 100  LEU D 124  ASN D 127                    
SITE     2 AC8 14 PHE D 128  PHE D 133  SER D 163  ARG D 165                    
SITE     3 AC8 14 ILE D 178  VAL D 179  LYS D 180  GLY D 182                    
SITE     4 AC8 14 TYR D 187  HOH D8015                                          
SITE     1 AC9 11 PRO D  20  MET D  21  PHE D  22  ALA D  23                    
SITE     2 AC9 11 GLY D  24  LYS D  25  THR D  26  ARG D  61                    
SITE     3 AC9 11 HOH D7980  HOH D8015  HOH D8023                               
CRYST1   57.158  115.649   64.474  90.00 101.02  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017495  0.000000  0.003407        0.00000                         
SCALE2      0.000000  0.008647  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015801        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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