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Database: PDB
Entry: 4EBN
LinkDB: 4EBN
Original site: 4EBN 
HEADER    HYDROLASE/ANTIBIOTIC                    23-MAR-12   4EBN              
TITLE     BLAC AMOXICILLIN ACYL-INTERMEDIATE COMPLEX                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-LACTAMASE;                                            
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: PENICILLINASE;                                              
COMPND   5 EC: 3.5.2.6;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 STRAIN: H37RV;                                                       
SOURCE   5 GENE: BLAA, BLAC, MT2128, MTCY49.07C, RV2068C;                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    AMBLER CLASS A BETA-LACTAMASE, BETA-LACTAMASE, SERINE HYDROLASE,      
KEYWDS   2 ESTERASE, HYDROLASE-ANTIBIOTIC COMPLEX, STRUCTURAL GENOMICS, TB      
KEYWDS   3 STRUCTURAL GENOMICS CONSORTIUM, TBSGC                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.MIRE,TB STRUCTURAL GENOMICS CONSORTIUM (TBSGC)                    
REVDAT   2   13-SEP-23 4EBN    1       REMARK SEQADV LINK                       
REVDAT   1   03-APR-13 4EBN    0                                                
JRNL        AUTH   J.A.MIRE,P.PAI,N.SIDDIQI,D.H.RUSSELL,E.J.RUBIN,              
JRNL        AUTH 2 J.C.SACCHETTINI                                              
JRNL        TITL   FAROPENEM IS EFFECTIVE AGAINST MYCOBACTERIUM TUBERCULOSIS IN 
JRNL        TITL 2 VITRO AND IN VIVO                                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.26                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 36951                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1839                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 47.2695 -  6.6955    1.00     2775   158  0.1939 0.2047        
REMARK   3     2  6.6955 -  5.3167    1.00     2728   155  0.2293 0.2515        
REMARK   3     3  5.3167 -  4.6453    1.00     2692   169  0.1766 0.1932        
REMARK   3     4  4.6453 -  4.2209    1.00     2744   131  0.1701 0.2188        
REMARK   3     5  4.2209 -  3.9185    1.00     2731   136  0.1811 0.2307        
REMARK   3     6  3.9185 -  3.6876    1.00     2714   131  0.1997 0.2468        
REMARK   3     7  3.6876 -  3.5030    1.00     2722   137  0.2071 0.2250        
REMARK   3     8  3.5030 -  3.3505    0.99     2704   138  0.2229 0.2734        
REMARK   3     9  3.3505 -  3.2216    0.99     2678   145  0.2533 0.2770        
REMARK   3    10  3.2216 -  3.1104    0.99     2681   134  0.2735 0.3413        
REMARK   3    11  3.1104 -  3.0132    0.98     2668   129  0.2925 0.3015        
REMARK   3    12  3.0132 -  2.9271    0.98     2635   137  0.3156 0.3782        
REMARK   3    13  2.9271 -  2.8500    0.97     2640   139  0.3469 0.3790        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.86                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 33.46                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.610           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 60.49                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.04800                                              
REMARK   3    B22 (A**2) : -2.37450                                             
REMARK   3    B33 (A**2) : 0.32640                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -7.28930                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.017           8015                                  
REMARK   3   ANGLE     :  1.662          10973                                  
REMARK   3   CHIRALITY :  0.093           1283                                  
REMARK   3   PLANARITY :  0.012           1441                                  
REMARK   3   DIHEDRAL  : 17.795           2813                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 29:57)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  27.3076  -1.4391  -5.7599              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2242 T22:   0.3496                                     
REMARK   3      T33:   0.4192 T12:  -0.0363                                     
REMARK   3      T13:  -0.0920 T23:  -0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4762 L22:   0.3534                                     
REMARK   3      L33:   0.9173 L12:   0.2992                                     
REMARK   3      L13:  -0.2938 L23:   0.2038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0893 S12:   0.5168 S13:  -0.3346                       
REMARK   3      S21:  -0.4857 S22:   0.0144 S23:   0.0303                       
REMARK   3      S31:   0.2004 S32:   0.0196 S33:   0.0024                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 58:144)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  31.4178  17.8957  15.9672              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1302 T22:   0.3115                                     
REMARK   3      T33:   0.1418 T12:  -0.0227                                     
REMARK   3      T13:   0.0818 T23:  -0.0461                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0299 L22:   0.7564                                     
REMARK   3      L33:   1.0531 L12:   0.5788                                     
REMARK   3      L13:   0.8972 L23:  -0.0692                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3966 S12:  -0.0052 S13:   0.6770                       
REMARK   3      S21:   0.3557 S22:   0.0226 S23:  -0.3841                       
REMARK   3      S31:  -0.4708 S32:   0.2386 S33:  -0.0162                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 145:179)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  34.8507  20.8380   2.9663              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3539 T22:   0.5236                                     
REMARK   3      T33:   0.5257 T12:  -0.0505                                     
REMARK   3      T13:  -0.0261 T23:   0.0190                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1032 L22:   0.1447                                     
REMARK   3      L33:   0.2194 L12:   0.1297                                     
REMARK   3      L13:   0.0877 L23:   0.1367                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2825 S12:   0.0400 S13:   0.3749                       
REMARK   3      S21:  -0.2709 S22:   0.2599 S23:   0.0594                       
REMARK   3      S31:  -0.2904 S32:  -0.1978 S33:   0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 180:293)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  29.4879   3.5915   7.4452              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1709 T22:   0.2158                                     
REMARK   3      T33:   0.2772 T12:  -0.0116                                     
REMARK   3      T13:   0.0283 T23:  -0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0830 L22:   1.0739                                     
REMARK   3      L33:   1.4999 L12:   0.7965                                     
REMARK   3      L13:   0.0016 L23:   0.6682                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0258 S12:  -0.0483 S13:  -0.0041                       
REMARK   3      S21:   0.0195 S22:   0.0319 S23:  -0.0634                       
REMARK   3      S31:  -0.0498 S32:  -0.1146 S33:  -0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 29:144)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   6.9568   7.9516  28.0649              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3962 T22:   0.3705                                     
REMARK   3      T33:   0.3948 T12:   0.0065                                     
REMARK   3      T13:   0.0248 T23:   0.0168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8920 L22:   1.4309                                     
REMARK   3      L33:   0.7563 L12:  -0.1105                                     
REMARK   3      L13:   0.5957 L23:  -0.2485                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0010 S12:  -0.0246 S13:   0.1449                       
REMARK   3      S21:   0.0500 S22:   0.0430 S23:   0.0687                       
REMARK   3      S31:  -0.1571 S32:  -0.0811 S33:   0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 145:164)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.1133  16.4380  32.5286              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7268 T22:   0.6043                                     
REMARK   3      T33:   0.7113 T12:   0.0861                                     
REMARK   3      T13:   0.1614 T23:  -0.0595                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7101 L22:   0.0983                                     
REMARK   3      L33:   0.7722 L12:   0.0700                                     
REMARK   3      L13:   0.4396 L23:  -0.1015                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1696 S12:  -0.9403 S13:   0.0459                       
REMARK   3      S21:  -0.1625 S22:   0.2935 S23:   0.1806                       
REMARK   3      S31:  -0.4452 S32:  -0.8313 S33:   0.4148                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 165:179)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  11.5368  19.4181  35.7513              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3369 T22:   1.2203                                     
REMARK   3      T33:   0.6906 T12:   0.0412                                     
REMARK   3      T13:   0.0642 T23:   0.1713                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7977 L22:   0.0720                                     
REMARK   3      L33:   0.5975 L12:   0.2168                                     
REMARK   3      L13:   0.6831 L23:   0.1921                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0965 S12:   0.9769 S13:   0.3119                       
REMARK   3      S21:   0.1414 S22:   0.5578 S23:  -0.5350                       
REMARK   3      S31:   0.9522 S32:   0.3755 S33:   0.0470                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 180:293)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   7.1983  -0.4088  33.5395              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3485 T22:   0.3118                                     
REMARK   3      T33:   0.3074 T12:  -0.0120                                     
REMARK   3      T13:   0.0382 T23:  -0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8043 L22:   0.6397                                     
REMARK   3      L33:   1.2181 L12:  -0.2427                                     
REMARK   3      L13:   0.3547 L23:  -0.9892                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0995 S12:   0.0587 S13:  -0.0328                       
REMARK   3      S21:   0.0845 S22:   0.0918 S23:   0.1786                       
REMARK   3      S31:   0.0777 S32:   0.0342 S33:   0.0196                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN C AND (RESSEQ 29:154)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  12.2848 -32.5759   9.3381              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3148 T22:   0.2266                                     
REMARK   3      T33:   0.2788 T12:  -0.0247                                     
REMARK   3      T13:  -0.0452 T23:  -0.0233                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9240 L22:   1.5205                                     
REMARK   3      L33:   1.5161 L12:  -0.3431                                     
REMARK   3      L13:   0.7813 L23:  -0.2994                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1081 S12:  -0.0935 S13:  -0.1247                       
REMARK   3      S21:  -0.0126 S22:   0.0439 S23:   0.0496                       
REMARK   3      S31:   0.1798 S32:  -0.1971 S33:   0.0001                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN C AND (RESSEQ 155:179)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  17.2456 -41.6902   3.2723              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7077 T22:   0.9981                                     
REMARK   3      T33:   0.7088 T12:  -0.0149                                     
REMARK   3      T13:  -0.0886 T23:   0.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6649 L22:   0.0930                                     
REMARK   3      L33:   0.1497 L12:   0.1445                                     
REMARK   3      L13:  -0.2150 L23:  -0.1364                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4023 S12:  -1.2399 S13:  -0.0166                       
REMARK   3      S21:  -0.3739 S22:  -0.1474 S23:  -0.0803                       
REMARK   3      S31:   0.1294 S32:   0.3411 S33:   0.0316                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN C AND (RESSEQ 180:293)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  16.1694 -23.3949   6.1250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2469 T22:   0.2204                                     
REMARK   3      T33:   0.1966 T12:   0.0154                                     
REMARK   3      T13:  -0.0023 T23:  -0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4448 L22:   0.9703                                     
REMARK   3      L33:   0.8439 L12:   0.8402                                     
REMARK   3      L13:  -0.4999 L23:  -0.2173                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0130 S12:  -0.0843 S13:  -0.0534                       
REMARK   3      S21:   0.0723 S22:   0.0510 S23:   0.0824                       
REMARK   3      S31:   0.1837 S32:   0.0445 S33:   0.0000                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN D AND (RESSEQ 29:68)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  11.3829 -24.7916  50.6537              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4381 T22:   0.4010                                     
REMARK   3      T33:   0.4004 T12:   0.0025                                     
REMARK   3      T13:   0.0290 T23:   0.0496                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4871 L22:   0.8318                                     
REMARK   3      L33:   0.6618 L12:   0.4593                                     
REMARK   3      L13:   0.1807 L23:  -0.2161                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1538 S12:  -0.1086 S13:   0.2747                       
REMARK   3      S21:   0.7087 S22:  -0.1446 S23:   0.0861                       
REMARK   3      S31:  -0.0279 S32:   0.1894 S33:   0.0426                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN D AND (RESSEQ 69:229)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  25.8046 -38.2373  37.8212              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4440 T22:   0.3101                                     
REMARK   3      T33:   0.2919 T12:   0.0289                                     
REMARK   3      T13:  -0.0021 T23:  -0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2230 L22:   0.9498                                     
REMARK   3      L33:   1.2400 L12:  -0.4108                                     
REMARK   3      L13:   0.5498 L23:   0.0415                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0327 S12:   0.0833 S13:  -0.0362                       
REMARK   3      S21:  -0.1368 S22:   0.0120 S23:  -0.0204                       
REMARK   3      S31:   0.1546 S32:   0.1797 S33:   0.0004                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN D AND (RESSEQ 230:293)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  14.0892 -26.6455  41.2907              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3299 T22:   0.2771                                     
REMARK   3      T33:   0.3589 T12:   0.0183                                     
REMARK   3      T13:  -0.0241 T23:   0.0151                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5754 L22:   0.8796                                     
REMARK   3      L33:   0.9756 L12:  -0.7460                                     
REMARK   3      L13:   0.4783 L23:  -0.2329                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0816 S12:   0.0781 S13:  -0.2278                       
REMARK   3      S21:  -0.0928 S22:  -0.0135 S23:   0.1426                       
REMARK   3      S31:   0.1324 S32:  -0.2461 S33:  -0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4EBN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000071415.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 120                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37239                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 12.040                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.0400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 2GDN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.5, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 291K                                                    
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       48.33600            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ARG A 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 114    CG   CD   OE1  NE2                                  
REMARK 470     ARG B  33    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 114    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 163    CG   OD1  OD2                                       
REMARK 470     GLU B 165    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 168    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 169    CG   CD1  CD2                                       
REMARK 470     ARG B 171    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 172    CG   OD1  OD2                                       
REMARK 470     GLU B 177    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 178    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 230    CG   CD   CE   NZ                                   
REMARK 470     TYR B 272    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B 275    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 114    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 165    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 168    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 171    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 172    CG   OD1  OD2                                       
REMARK 470     GLU C 177    CG   CD   OE1  OE2                                  
REMARK 470     ASN C 197    CG   OD1  ND2                                       
REMARK 470     ASP C 228    CG   OD1  OD2                                       
REMARK 470     GLU C 275    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  36    CG   CD   OE1  OE2                                  
REMARK 470     GLN D  83    CG   CD   OE1  NE2                                  
REMARK 470     LYS D  93    CG   CD   CE   NZ                                   
REMARK 470     ARG D 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN D 110    CG   CD   OE1  NE2                                  
REMARK 470     GLN D 114    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 219    CG   CD   CE   NZ                                   
REMARK 470     ASP D 273    CG   OD1  OD2                                       
REMARK 470     GLU D 275    CG   CD   OE1  OE2                                  
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    THR C  71   N   -  CA  -  CB  ANGL. DEV. =  12.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS A  69     -134.65     56.74                                   
REMARK 500    GLN A  83       27.74    166.91                                   
REMARK 500    ASN A  86      112.99   -171.01                                   
REMARK 500    PRO A  87      143.41    -25.21                                   
REMARK 500    SER A 104     -120.65   -126.23                                   
REMARK 500    ARG A 220     -114.57   -102.43                                   
REMARK 500    CYS B  69     -133.35     55.65                                   
REMARK 500    LEU B 162     -159.61    -96.38                                   
REMARK 500    ASP B 163      -36.44    145.92                                   
REMARK 500    GLU B 165     -127.26    -62.72                                   
REMARK 500    PRO B 167       27.85    -57.66                                   
REMARK 500    LEU B 169      -20.87     97.62                                   
REMARK 500    ARG B 220     -109.49   -109.16                                   
REMARK 500    ASP B 246      106.74   -164.31                                   
REMARK 500    CYS C  69     -172.70     49.05                                   
REMARK 500    SER C  70        2.73    -45.65                                   
REMARK 500    ASP C 172      139.55    -33.26                                   
REMARK 500    ARG C 220     -113.92   -101.45                                   
REMARK 500    GLU D  36     -108.88    -62.01                                   
REMARK 500    LEU D  37      -54.44     20.33                                   
REMARK 500    CYS D  69     -139.20     57.35                                   
REMARK 500    SER D  99      -12.19    -40.18                                   
REMARK 500    ILE D 105       97.18    -44.92                                   
REMARK 500    VAL D 108      -39.94   -134.73                                   
REMARK 500    ARG D 220     -112.67   -101.62                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AXL B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AXL C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3VFF   RELATED DB: PDB                                   
REMARK 900 BLAC E166A CDC-OME ACYL-INTERMEDIATE COMPLEX                         
REMARK 900 RELATED ID: 3VFH   RELATED DB: PDB                                   
REMARK 900 BLAC E166A CDC-1 ACYL-INTERMEDIATE COMPLEX                           
REMARK 900 RELATED ID: 4EBI   RELATED DB: PDB                                   
REMARK 900 BLAC TEBIPENEM ACYL-INTERMEDIATE COMPLEX                             
REMARK 900 RELATED ID: 4EBL   RELATED DB: PDB                                   
REMARK 900 BLAC E166A FAROPENEM ACYL-INTERMEDIATE COMPLEX                       
REMARK 900 RELATED ID: 4EBM   RELATED DB: PDB                                   
REMARK 900 BLAC BIAPENEM ACYL-INTERMEDIATE COMPLEX                              
REMARK 900 RELATED ID: 4EBO   RELATED DB: PDB                                   
REMARK 900 BLAC E166A CEFOPERAZONE ACYL-INTERMEDIATE COMPLEX                    
REMARK 900 RELATED ID: 4EBP   RELATED DB: PDB                                   
REMARK 900 BLAC E166A CEFOTAXIME ACYL-INTERMEDIATE COMPLEX                      
DBREF  4EBN A   29   293  UNP    P0C5C1   BLAC_MYCTU      43    307             
DBREF  4EBN B   29   293  UNP    P0C5C1   BLAC_MYCTU      43    307             
DBREF  4EBN C   29   293  UNP    P0C5C1   BLAC_MYCTU      43    307             
DBREF  4EBN D   29   293  UNP    P0C5C1   BLAC_MYCTU      43    307             
SEQADV 4EBN ALA A  166  UNP  P0C5C1    GLU   182 ENGINEERED MUTATION            
SEQADV 4EBN ALA B  166  UNP  P0C5C1    GLU   182 ENGINEERED MUTATION            
SEQADV 4EBN ALA C  166  UNP  P0C5C1    GLU   182 ENGINEERED MUTATION            
SEQADV 4EBN ALA D  166  UNP  P0C5C1    GLU   182 ENGINEERED MUTATION            
SEQRES   1 A  265  ASP LEU ALA ASP ARG PHE ALA GLU LEU GLU ARG ARG TYR          
SEQRES   2 A  265  ASP ALA ARG LEU GLY VAL TYR VAL PRO ALA THR GLY THR          
SEQRES   3 A  265  THR ALA ALA ILE GLU TYR ARG ALA ASP GLU ARG PHE ALA          
SEQRES   4 A  265  PHE CYS SER THR PHE LYS ALA PRO LEU VAL ALA ALA VAL          
SEQRES   5 A  265  LEU HIS GLN ASN PRO LEU THR HIS LEU ASP LYS LEU ILE          
SEQRES   6 A  265  THR TYR THR SER ASP ASP ILE ARG SER ILE SER PRO VAL          
SEQRES   7 A  265  ALA GLN GLN HIS VAL GLN THR GLY MET THR ILE GLY GLN          
SEQRES   8 A  265  LEU CYS ASP ALA ALA ILE ARG TYR SER ASP GLY THR ALA          
SEQRES   9 A  265  ALA ASN LEU LEU LEU ALA ASP LEU GLY GLY PRO GLY GLY          
SEQRES  10 A  265  GLY THR ALA ALA PHE THR GLY TYR LEU ARG SER LEU GLY          
SEQRES  11 A  265  ASP THR VAL SER ARG LEU ASP ALA GLU ALA PRO GLU LEU          
SEQRES  12 A  265  ASN ARG ASP PRO PRO GLY ASP GLU ARG ASP THR THR THR          
SEQRES  13 A  265  PRO HIS ALA ILE ALA LEU VAL LEU GLN GLN LEU VAL LEU          
SEQRES  14 A  265  GLY ASN ALA LEU PRO PRO ASP LYS ARG ALA LEU LEU THR          
SEQRES  15 A  265  ASP TRP MET ALA ARG ASN THR THR GLY ALA LYS ARG ILE          
SEQRES  16 A  265  ARG ALA GLY PHE PRO ALA ASP TRP LYS VAL ILE ASP LYS          
SEQRES  17 A  265  THR GLY THR GLY ASP TYR GLY ARG ALA ASN ASP ILE ALA          
SEQRES  18 A  265  VAL VAL TRP SER PRO THR GLY VAL PRO TYR VAL VAL ALA          
SEQRES  19 A  265  VAL MET SER ASP ARG ALA GLY GLY GLY TYR ASP ALA GLU          
SEQRES  20 A  265  PRO ARG GLU ALA LEU LEU ALA GLU ALA ALA THR CYS VAL          
SEQRES  21 A  265  ALA GLY VAL LEU ALA                                          
SEQRES   1 B  265  ASP LEU ALA ASP ARG PHE ALA GLU LEU GLU ARG ARG TYR          
SEQRES   2 B  265  ASP ALA ARG LEU GLY VAL TYR VAL PRO ALA THR GLY THR          
SEQRES   3 B  265  THR ALA ALA ILE GLU TYR ARG ALA ASP GLU ARG PHE ALA          
SEQRES   4 B  265  PHE CYS SER THR PHE LYS ALA PRO LEU VAL ALA ALA VAL          
SEQRES   5 B  265  LEU HIS GLN ASN PRO LEU THR HIS LEU ASP LYS LEU ILE          
SEQRES   6 B  265  THR TYR THR SER ASP ASP ILE ARG SER ILE SER PRO VAL          
SEQRES   7 B  265  ALA GLN GLN HIS VAL GLN THR GLY MET THR ILE GLY GLN          
SEQRES   8 B  265  LEU CYS ASP ALA ALA ILE ARG TYR SER ASP GLY THR ALA          
SEQRES   9 B  265  ALA ASN LEU LEU LEU ALA ASP LEU GLY GLY PRO GLY GLY          
SEQRES  10 B  265  GLY THR ALA ALA PHE THR GLY TYR LEU ARG SER LEU GLY          
SEQRES  11 B  265  ASP THR VAL SER ARG LEU ASP ALA GLU ALA PRO GLU LEU          
SEQRES  12 B  265  ASN ARG ASP PRO PRO GLY ASP GLU ARG ASP THR THR THR          
SEQRES  13 B  265  PRO HIS ALA ILE ALA LEU VAL LEU GLN GLN LEU VAL LEU          
SEQRES  14 B  265  GLY ASN ALA LEU PRO PRO ASP LYS ARG ALA LEU LEU THR          
SEQRES  15 B  265  ASP TRP MET ALA ARG ASN THR THR GLY ALA LYS ARG ILE          
SEQRES  16 B  265  ARG ALA GLY PHE PRO ALA ASP TRP LYS VAL ILE ASP LYS          
SEQRES  17 B  265  THR GLY THR GLY ASP TYR GLY ARG ALA ASN ASP ILE ALA          
SEQRES  18 B  265  VAL VAL TRP SER PRO THR GLY VAL PRO TYR VAL VAL ALA          
SEQRES  19 B  265  VAL MET SER ASP ARG ALA GLY GLY GLY TYR ASP ALA GLU          
SEQRES  20 B  265  PRO ARG GLU ALA LEU LEU ALA GLU ALA ALA THR CYS VAL          
SEQRES  21 B  265  ALA GLY VAL LEU ALA                                          
SEQRES   1 C  265  ASP LEU ALA ASP ARG PHE ALA GLU LEU GLU ARG ARG TYR          
SEQRES   2 C  265  ASP ALA ARG LEU GLY VAL TYR VAL PRO ALA THR GLY THR          
SEQRES   3 C  265  THR ALA ALA ILE GLU TYR ARG ALA ASP GLU ARG PHE ALA          
SEQRES   4 C  265  PHE CYS SER THR PHE LYS ALA PRO LEU VAL ALA ALA VAL          
SEQRES   5 C  265  LEU HIS GLN ASN PRO LEU THR HIS LEU ASP LYS LEU ILE          
SEQRES   6 C  265  THR TYR THR SER ASP ASP ILE ARG SER ILE SER PRO VAL          
SEQRES   7 C  265  ALA GLN GLN HIS VAL GLN THR GLY MET THR ILE GLY GLN          
SEQRES   8 C  265  LEU CYS ASP ALA ALA ILE ARG TYR SER ASP GLY THR ALA          
SEQRES   9 C  265  ALA ASN LEU LEU LEU ALA ASP LEU GLY GLY PRO GLY GLY          
SEQRES  10 C  265  GLY THR ALA ALA PHE THR GLY TYR LEU ARG SER LEU GLY          
SEQRES  11 C  265  ASP THR VAL SER ARG LEU ASP ALA GLU ALA PRO GLU LEU          
SEQRES  12 C  265  ASN ARG ASP PRO PRO GLY ASP GLU ARG ASP THR THR THR          
SEQRES  13 C  265  PRO HIS ALA ILE ALA LEU VAL LEU GLN GLN LEU VAL LEU          
SEQRES  14 C  265  GLY ASN ALA LEU PRO PRO ASP LYS ARG ALA LEU LEU THR          
SEQRES  15 C  265  ASP TRP MET ALA ARG ASN THR THR GLY ALA LYS ARG ILE          
SEQRES  16 C  265  ARG ALA GLY PHE PRO ALA ASP TRP LYS VAL ILE ASP LYS          
SEQRES  17 C  265  THR GLY THR GLY ASP TYR GLY ARG ALA ASN ASP ILE ALA          
SEQRES  18 C  265  VAL VAL TRP SER PRO THR GLY VAL PRO TYR VAL VAL ALA          
SEQRES  19 C  265  VAL MET SER ASP ARG ALA GLY GLY GLY TYR ASP ALA GLU          
SEQRES  20 C  265  PRO ARG GLU ALA LEU LEU ALA GLU ALA ALA THR CYS VAL          
SEQRES  21 C  265  ALA GLY VAL LEU ALA                                          
SEQRES   1 D  265  ASP LEU ALA ASP ARG PHE ALA GLU LEU GLU ARG ARG TYR          
SEQRES   2 D  265  ASP ALA ARG LEU GLY VAL TYR VAL PRO ALA THR GLY THR          
SEQRES   3 D  265  THR ALA ALA ILE GLU TYR ARG ALA ASP GLU ARG PHE ALA          
SEQRES   4 D  265  PHE CYS SER THR PHE LYS ALA PRO LEU VAL ALA ALA VAL          
SEQRES   5 D  265  LEU HIS GLN ASN PRO LEU THR HIS LEU ASP LYS LEU ILE          
SEQRES   6 D  265  THR TYR THR SER ASP ASP ILE ARG SER ILE SER PRO VAL          
SEQRES   7 D  265  ALA GLN GLN HIS VAL GLN THR GLY MET THR ILE GLY GLN          
SEQRES   8 D  265  LEU CYS ASP ALA ALA ILE ARG TYR SER ASP GLY THR ALA          
SEQRES   9 D  265  ALA ASN LEU LEU LEU ALA ASP LEU GLY GLY PRO GLY GLY          
SEQRES  10 D  265  GLY THR ALA ALA PHE THR GLY TYR LEU ARG SER LEU GLY          
SEQRES  11 D  265  ASP THR VAL SER ARG LEU ASP ALA GLU ALA PRO GLU LEU          
SEQRES  12 D  265  ASN ARG ASP PRO PRO GLY ASP GLU ARG ASP THR THR THR          
SEQRES  13 D  265  PRO HIS ALA ILE ALA LEU VAL LEU GLN GLN LEU VAL LEU          
SEQRES  14 D  265  GLY ASN ALA LEU PRO PRO ASP LYS ARG ALA LEU LEU THR          
SEQRES  15 D  265  ASP TRP MET ALA ARG ASN THR THR GLY ALA LYS ARG ILE          
SEQRES  16 D  265  ARG ALA GLY PHE PRO ALA ASP TRP LYS VAL ILE ASP LYS          
SEQRES  17 D  265  THR GLY THR GLY ASP TYR GLY ARG ALA ASN ASP ILE ALA          
SEQRES  18 D  265  VAL VAL TRP SER PRO THR GLY VAL PRO TYR VAL VAL ALA          
SEQRES  19 D  265  VAL MET SER ASP ARG ALA GLY GLY GLY TYR ASP ALA GLU          
SEQRES  20 D  265  PRO ARG GLU ALA LEU LEU ALA GLU ALA ALA THR CYS VAL          
SEQRES  21 D  265  ALA GLY VAL LEU ALA                                          
HET    PO4  A 301       5                                                       
HET    PO4  A 302       5                                                       
HET    PO4  A 303       5                                                       
HET    AXL  B 301      25                                                       
HET    AXL  C 301      25                                                       
HET    PO4  C 302       5                                                       
HET    PO4  D 301       5                                                       
HET    PO4  D 302       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     AXL 2-{1-[2-AMINO-2-(4-HYDROXY-PHENYL)-ACETYLAMINO]-2-OXO-           
HETNAM   2 AXL  ETHYL}-5,5-DIMETHYL-THIAZOLIDINE-4-CARBOXYLIC ACID              
HETSYN     AXL AMOXICILLIN, BOUND FORM                                          
FORMUL   5  PO4    6(O4 P 3-)                                                   
FORMUL   8  AXL    2(C16 H21 N3 O5 S)                                           
HELIX    1   1 ASP A   29  ASP A   42  1                                  14    
HELIX    2   2 PHE A   72  HIS A   82  1                                  11    
HELIX    3   3 THR A   89  ASP A   92  5                                   4    
HELIX    4   4 ILE A  119  TYR A  129  1                                  11    
HELIX    5   5 ASP A  131  ASP A  141  1                                  11    
HELIX    6   6 PRO A  145  GLY A  145B 5                                   3    
HELIX    7   7 GLY A  145C LEU A  155  1                                  12    
HELIX    8   8 PRO A  167  ARG A  171  5                                   5    
HELIX    9   9 THR A  182  LEU A  195  1                                  14    
HELIX   10  10 PRO A  200  ARG A  213  1                                  14    
HELIX   11  11 ARG A  220  PHE A  225  1                                   6    
HELIX   12  12 ARG A  267  ALA A  274  5                                   8    
HELIX   13  13 ARG A  277  ALA A  293  1                                  17    
HELIX   14  14 LEU B   30  ASP B   42  1                                  13    
HELIX   15  15 PHE B   72  GLN B   83  1                                  12    
HELIX   16  16 PRO B   87  ASP B   92  5                                   6    
HELIX   17  17 VAL B  108  HIS B  112  5                                   5    
HELIX   18  18 ILE B  119  TYR B  129  1                                  11    
HELIX   19  19 ASP B  131  ASP B  141  1                                  11    
HELIX   20  20 LEU B  142  GLY B  143  5                                   2    
HELIX   21  21 GLY B  144  GLY B  145B 5                                   4    
HELIX   22  22 GLY B  145C LEU B  155  1                                  12    
HELIX   23  23 THR B  182  LEU B  195  1                                  14    
HELIX   24  24 PRO B  200  ARG B  213  1                                  14    
HELIX   25  25 ARG B  220  PHE B  225  1                                   6    
HELIX   26  26 ARG B  267  GLY B  271  5                                   5    
HELIX   27  27 ARG B  277  ALA B  293  1                                  17    
HELIX   28  28 LEU C   30  ASP C   42  1                                  13    
HELIX   29  29 CYS C   69  THR C   71  5                                   3    
HELIX   30  30 PHE C   72  ASN C   86  1                                  13    
HELIX   31  31 PRO C   87  ASP C   92  5                                   6    
HELIX   32  32 THR C   98  ILE C  102  5                                   5    
HELIX   33  33 ALA C  109  VAL C  113  5                                   5    
HELIX   34  34 ILE C  119  TYR C  129  1                                  11    
HELIX   35  35 GLY C  132  ASP C  141  1                                  10    
HELIX   36  36 GLY C  144  LEU C  155  1                                  16    
HELIX   37  37 PRO C  167  ASP C  172  1                                   6    
HELIX   38  38 THR C  182  LEU C  195  1                                  14    
HELIX   39  39 PRO C  200  ARG C  213  1                                  14    
HELIX   40  40 ARG C  220  PHE C  225  1                                   6    
HELIX   41  41 ARG C  277  ALA C  293  1                                  17    
HELIX   42  42 LEU D   30  ASP D   42  1                                  13    
HELIX   43  43 CYS D   69  THR D   71  5                                   3    
HELIX   44  44 PHE D   72  GLN D   83  1                                  12    
HELIX   45  45 PRO D   87  ASP D   92  5                                   6    
HELIX   46  46 VAL D  108  VAL D  113  1                                   6    
HELIX   47  47 ILE D  119  TYR D  129  1                                  11    
HELIX   48  48 ASP D  131  GLY D  143  1                                  13    
HELIX   49  49 PRO D  145  GLY D  145B 5                                   3    
HELIX   50  50 GLY D  145C SER D  154  1                                  11    
HELIX   51  51 PRO D  167  ARG D  171  5                                   5    
HELIX   52  52 THR D  182  LEU D  195  1                                  14    
HELIX   53  53 PRO D  200  ARG D  213  1                                  14    
HELIX   54  54 ARG D  220  PHE D  225  1                                   6    
HELIX   55  55 ARG D  277  ALA D  293  1                                  17    
SHEET    1   A 5 ILE A  58  TYR A  60  0                                        
SHEET    2   A 5 ARG A  44  VAL A  49 -1  N  VAL A  47   O  TYR A  60           
SHEET    3   A 5 PRO A 258  ASP A 266 -1  O  MET A 264   N  GLY A  46           
SHEET    4   A 5 ALA A 244  TRP A 251 -1  N  ALA A 248   O  VAL A 261           
SHEET    5   A 5 LYS A 230  THR A 237 -1  N  GLY A 236   O  ASN A 245           
SHEET    1   B 2 PHE A  66  ALA A  67  0                                        
SHEET    2   B 2 THR A 180  THR A 181 -1  O  THR A 181   N  PHE A  66           
SHEET    1   C 2 LEU A  94  ILE A  95  0                                        
SHEET    2   C 2 MET A 117  THR A 118 -1  O  MET A 117   N  ILE A  95           
SHEET    1   D 5 ILE B  58  TYR B  60  0                                        
SHEET    2   D 5 ARG B  44  VAL B  49 -1  N  VAL B  47   O  TYR B  60           
SHEET    3   D 5 PRO B 258  ASP B 266 -1  O  MET B 264   N  GLY B  46           
SHEET    4   D 5 ARG B 243  TRP B 251 -1  N  ALA B 248   O  VAL B 261           
SHEET    5   D 5 LYS B 230  GLY B 238 -1  N  LYS B 234   O  ILE B 247           
SHEET    1   E 2 PHE B  66  ALA B  67  0                                        
SHEET    2   E 2 THR B 180  THR B 181 -1  O  THR B 181   N  PHE B  66           
SHEET    1   F 2 LEU B  94  ILE B  95  0                                        
SHEET    2   F 2 MET B 117  THR B 118 -1  O  MET B 117   N  ILE B  95           
SHEET    1   G 5 ILE C  58  TYR C  60  0                                        
SHEET    2   G 5 ARG C  44  VAL C  49 -1  N  VAL C  47   O  TYR C  60           
SHEET    3   G 5 PRO C 258  ASP C 266 -1  O  MET C 264   N  GLY C  46           
SHEET    4   G 5 ARG C 243  TRP C 251 -1  N  ALA C 248   O  VAL C 261           
SHEET    5   G 5 LYS C 230  GLY C 238 -1  N  GLY C 236   O  ASN C 245           
SHEET    1   H 2 PHE C  66  ALA C  67  0                                        
SHEET    2   H 2 THR C 180  THR C 181 -1  O  THR C 181   N  PHE C  66           
SHEET    1   I 2 LEU C  94  ILE C  95  0                                        
SHEET    2   I 2 MET C 117  THR C 118 -1  O  MET C 117   N  ILE C  95           
SHEET    1   J 5 ILE D  58  TYR D  60  0                                        
SHEET    2   J 5 ARG D  44  VAL D  49 -1  N  VAL D  47   O  TYR D  60           
SHEET    3   J 5 PRO D 258  ASP D 266 -1  O  MET D 264   N  GLY D  46           
SHEET    4   J 5 ALA D 244  TRP D 251 -1  N  ASP D 246   O  VAL D 263           
SHEET    5   J 5 LYS D 230  THR D 237 -1  N  ILE D 232   O  VAL D 249           
SHEET    1   K 2 PHE D  66  ALA D  67  0                                        
SHEET    2   K 2 THR D 180  THR D 181 -1  O  THR D 181   N  PHE D  66           
SHEET    1   L 2 LEU D  94  ILE D  95  0                                        
SHEET    2   L 2 MET D 117  THR D 118 -1  O  MET D 117   N  ILE D  95           
LINK         OG  SER B  70                 C1  AXL B 301     1555   1555  1.35  
LINK         OG  SER C  70                 C1  AXL C 301     1555   1555  1.35  
CISPEP   1 ALA A  166    PRO A  167          0         1.54                     
CISPEP   2 ALA C  166    PRO C  167          0         5.08                     
CISPEP   3 ALA D  166    PRO D  167          0         8.76                     
SITE     1 AC1  7 SER A  70  SER A 130  THR A 216  THR A 235                    
SITE     2 AC1  7 THR A 237  GLN B 110  GLN B 111                               
SITE     1 AC2  2 ASP A 124  ARG A 213                                          
SITE     1 AC3  3 LEU A  88  ASP A 202  LYS A 203                               
SITE     1 AC4  7 CYS B  69  SER B  70  SER B 130  ASN B 170                    
SITE     2 AC4  7 THR B 235  GLY B 236  THR B 237                               
SITE     1 AC5  5 SER C  70  SER C 130  ASN C 170  THR C 235                    
SITE     2 AC5  5 THR C 237                                                     
SITE     1 AC6  3 ASP C 124  ARG C 128  ARG C 213                               
SITE     1 AC7  6 GLN C 111  SER D 130  THR D 216  THR D 235                    
SITE     2 AC7  6 GLY D 236  THR D 237                                          
SITE     1 AC8  3 ASP D 124  ARG D 128  ARG D 213                               
CRYST1   79.567   96.672  109.808  90.00 107.52  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      0.012568  0.000000  0.003968        0.00000                         
SCALE2      0.000000  0.010344  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009550        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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