GenomeNet

Database: PDB
Entry: 6G9F
LinkDB: 6G9F
Original site: 6G9F 
HEADER    HYDROLASE/ANTIBIOTIC                    10-APR-18   6G9F              
TITLE     STRUCTURAL BASIS FOR THE INHIBITION OF E. COLI PBP2                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PENICILLIN-BINDING PROTEIN 2,PBP-2;                         
COMPND   5 EC: 3.4.16.4;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: THE SER 330 IN THE STRUCTURE IS MODIFIED COVALENTLY   
COMPND   8 AND IS NAMED (S31)                                                   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI O157:H7;                       
SOURCE   3 ORGANISM_TAXID: 83334;                                               
SOURCE   4 GENE: MRDA, PBPA, Z0781, ECS0673;                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693                                      
KEYWDS    PENICILLIN BINDING PROTEIN, HYDROLASE-ANTIBIOTIC COMPLEX              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.RUFF,N.LEVY                                                         
REVDAT   1   22-MAY-19 6G9F    0                                                
JRNL        AUTH   N.LEVY,J.M.BRUNEAU,E.LE ROUZIC,D.BONNARD,F.LE STRAT,         
JRNL        AUTH 2 A.CARAVANO,F.CHEVREUIL,J.BARBION,S.CHASSET,B.LEDOUSSAL,      
JRNL        AUTH 3 F.MOREAU,M.RUFF                                              
JRNL        TITL   STRUCTURAL BASIS FOR E. COLI PENICILLIN BINDING PROTEIN      
JRNL        TITL 2 (PBP) 2 INHIBITION, A PLATFORM FOR DRUG DESIGN.              
JRNL        REF    J.MED.CHEM.                   V.  62  4742 2019              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   30995398                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.9B00338                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.01                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 35639                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3754                            
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 39.0099 -  7.0360    0.97     2343   142  0.1533 0.1781        
REMARK   3     2  7.0360 -  5.5899    0.97     2331   143  0.1742 0.2271        
REMARK   3     3  5.5899 -  4.8848    0.96     2333   145  0.1508 0.1975        
REMARK   3     4  4.8848 -  4.4389    0.97     2292   139  0.1403 0.1616        
REMARK   3     5  4.4389 -  4.1211    0.97     2390   139  0.1519 0.1969        
REMARK   3     6  4.1211 -  3.8784    0.97     2324   134  0.1644 0.2564        
REMARK   3     7  3.8784 -  3.6843    0.97     2361   137  0.1769 0.2452        
REMARK   3     8  3.6843 -  3.5240    0.98     2360   140  0.1813 0.2468        
REMARK   3     9  3.5240 -  3.3884    0.98     2358   139  0.2012 0.2393        
REMARK   3    10  3.3884 -  3.2716    0.99     2405   139  0.2113 0.2964        
REMARK   3    11  3.2716 -  3.1693    0.99     2354   137  0.2200 0.3064        
REMARK   3    12  3.1693 -  3.0788    0.99     2424   144  0.2485 0.2938        
REMARK   3    13  3.0788 -  2.9977    0.99     2363   139  0.2394 0.3224        
REMARK   3    14  2.9977 -  2.9246    1.00     2427   146  0.2403 0.2881        
REMARK   3    15  2.9246 -  2.8582    0.99     2391   143  0.2468 0.3075        
REMARK   3    16  2.8582 -  2.7974    1.00     2449   145  0.2584 0.3032        
REMARK   3    17  2.7974 -  2.7414    0.99     2347   142  0.2733 0.2845        
REMARK   3    18  2.7414 -  2.6897    0.99     2384   142  0.2781 0.2805        
REMARK   3    19  2.6897 -  2.6417    1.00     2415   146  0.2998 0.3785        
REMARK   3    20  2.6417 -  2.5969    1.00     2413   140  0.3025 0.3335        
REMARK   3    21  2.5969 -  2.5550    0.99     2395   142  0.3044 0.3536        
REMARK   3    22  2.5550 -  2.5157    0.99     2368   140  0.3134 0.3395        
REMARK   3    23  2.5157 -  2.4787    0.99     2419   139  0.3072 0.3142        
REMARK   3    24  2.4787 -  2.4438    0.98     2394   144  0.3173 0.4203        
REMARK   3    25  2.4438 -  2.4108    0.94     2208   135  0.3243 0.3670        
REMARK   3    26  2.4108 -  2.3795    0.89     2203   129  0.3223 0.3192        
REMARK   3    27  2.3795 -  2.3498    0.77     1817   104  0.3194 0.3611        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.360            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.040           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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      :  0.008           4386                                  
REMARK   3   ANGLE     :  0.971           5965                                  
REMARK   3   CHIRALITY :  0.053            646                                  
REMARK   3   PLANARITY :  0.007            774                                  
REMARK   3   DIHEDRAL  :  6.285           2622                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  28.9950  55.2310  38.5428              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3710 T22:   0.3825                                     
REMARK   3      T33:   0.3007 T12:  -0.0529                                     
REMARK   3      T13:  -0.0141 T23:   0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5106 L22:   1.9455                                     
REMARK   3      L33:   0.0129 L12:   1.4841                                     
REMARK   3      L13:   0.2467 L23:   0.0109                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0350 S12:   0.0046 S13:   0.0023                       
REMARK   3      S21:  -0.0278 S22:  -0.0026 S23:   0.0460                       
REMARK   3      S31:   0.0582 S32:  -0.0198 S33:  -0.0001                       
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 6G9F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-APR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009607.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-FEB-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-X                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER R 4M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35810                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.005                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.14540                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.8700                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.54600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 6G9S                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRISBASE / BICINE PH 8,5 ; 0.1 M   
REMARK 280  [CARBOXYLIC ACIDS MIX (0.02 M SODIUM FORMATE ; 0.02 M AMMONIUM      
REMARK 280  ACETATE ; 0.02 M SODIUM CITRATE TRIBASIC DIHYDRATE ; 0.02 M         
REMARK 280  SODIUM POTASSIUM TARTRATE TETRAHYDRATE ; 0.02 M SODIUM OXAMATE) ;   
REMARK 280  24 % GLYCEROL ; 12 % PEG 4000] EQUILIBRATED AGAINST 2.0 M NACL,     
REMARK 280  PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.38350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.38350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       62.53900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       91.43750            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       62.53900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       91.43750            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       37.38350            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       62.53900            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       91.43750            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       37.38350            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       62.53900            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       91.43750            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 24270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 734  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 770  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 796  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 808  LIES ON A SPECIAL POSITION.                          
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     GLY A    55                                                      
REMARK 465     PRO A    56                                                      
REMARK 465     VAL A   550                                                      
REMARK 465     PHE A   551                                                      
REMARK 465     GLY A   552                                                      
REMARK 465     LEU A   553                                                      
REMARK 465     LYS A   554                                                      
REMARK 465     ALA A   555                                                      
REMARK 465     ASN A   556                                                      
REMARK 465     GLU A   557                                                      
REMARK 465     THR A   558                                                      
REMARK 465     TYR A   559                                                      
REMARK 465     ASN A   560                                                      
REMARK 465     ALA A   561                                                      
REMARK 465     HIS A   562                                                      
REMARK 465     LYS A   563                                                      
REMARK 465     ILE A   564                                                      
REMARK 465     ALA A   565                                                      
REMARK 465     GLU A   566                                                      
REMARK 465     ARG A   567                                                      
REMARK 465     GLY A   614                                                      
REMARK 465     ASP A   615                                                      
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    ARG A 125       31.45    -65.18                                   
REMARK 500    SER A 291     -160.05   -113.75                                   
REMARK 500    THR A 315       67.12     39.90                                   
REMARK 500    ALA A 329     -137.26     51.78                                   
REMARK 500    ASP A 420       55.41    -91.14                                   
REMARK 500    GLN A 455     -144.19   -122.71                                   
REMARK 500    GLU A 489      107.95     73.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 822        DISTANCE =  6.57 ANGSTROMS                       
REMARK 525    HOH A 823        DISTANCE =  6.84 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NXL A 1330                
DBREF  6G9F A   57   615  UNP    P0AD67   MRDA_ECO57      57    615             
SEQADV 6G9F GLY A   55  UNP  P0AD67              EXPRESSION TAG                 
SEQADV 6G9F PRO A   56  UNP  P0AD67              EXPRESSION TAG                 
SEQRES   1 A  561  GLY PRO ASN ARG ILE LYS LEU VAL PRO ILE ALA PRO SER          
SEQRES   2 A  561  ARG GLY ILE ILE TYR ASP ARG ASN GLY ILE PRO LEU ALA          
SEQRES   3 A  561  LEU ASN ARG THR ILE TYR GLN ILE GLU MET MET PRO GLU          
SEQRES   4 A  561  LYS VAL ASP ASN VAL GLN GLN THR LEU ASP ALA LEU ARG          
SEQRES   5 A  561  SER VAL VAL ASP LEU THR ASP ASP ASP ILE ALA ALA PHE          
SEQRES   6 A  561  ARG LYS GLU ARG ALA ARG SER HIS ARG PHE THR SER ILE          
SEQRES   7 A  561  PRO VAL LYS THR ASN LEU THR GLU VAL GLN VAL ALA ARG          
SEQRES   8 A  561  PHE ALA VAL ASN GLN TYR ARG PHE PRO GLY VAL GLU VAL          
SEQRES   9 A  561  LYS GLY TYR LYS ARG ARG TYR TYR PRO TYR GLY SER ALA          
SEQRES  10 A  561  LEU THR HIS VAL ILE GLY TYR VAL SER LYS ILE ASN ASP          
SEQRES  11 A  561  LYS ASP VAL GLU ARG LEU ASN ASN ASP GLY LYS LEU ALA          
SEQRES  12 A  561  ASN TYR ALA ALA THR HIS ASP ILE GLY LYS LEU GLY ILE          
SEQRES  13 A  561  GLU ARG TYR TYR GLU ASP VAL LEU HIS GLY GLN THR GLY          
SEQRES  14 A  561  TYR GLU GLU VAL GLU VAL ASN ASN ARG GLY ARG VAL ILE          
SEQRES  15 A  561  ARG GLN LEU LYS GLU VAL PRO PRO GLN ALA GLY HIS ASP          
SEQRES  16 A  561  ILE TYR LEU THR LEU ASP LEU LYS LEU GLN GLN TYR ILE          
SEQRES  17 A  561  GLU THR LEU LEU ALA GLY SER ARG ALA ALA VAL VAL VAL          
SEQRES  18 A  561  THR ASP PRO ARG THR GLY GLY VAL LEU ALA LEU VAL SER          
SEQRES  19 A  561  THR PRO SER TYR ASP PRO ASN LEU PHE VAL ASP GLY ILE          
SEQRES  20 A  561  SER SER LYS ASP TYR SER ALA LEU LEU ASN ASP PRO ASN          
SEQRES  21 A  561  THR PRO LEU VAL ASN ARG ALA THR GLN GLY VAL TYR PRO          
SEQRES  22 A  561  PRO ALA SER THR VAL LYS PRO TYR VAL ALA VAL SER ALA          
SEQRES  23 A  561  LEU SER ALA GLY VAL ILE THR ARG ASN THR THR LEU PHE          
SEQRES  24 A  561  ASP PRO GLY TRP TRP GLN LEU PRO GLY SER GLU LYS ARG          
SEQRES  25 A  561  TYR ARG ASP TRP LYS LYS TRP GLY HIS GLY ARG LEU ASN          
SEQRES  26 A  561  VAL THR ARG SER LEU GLU GLU SER ALA ASP THR PHE PHE          
SEQRES  27 A  561  TYR GLN VAL ALA TYR ASP MET GLY ILE ASP ARG LEU SER          
SEQRES  28 A  561  GLU TRP MET GLY LYS PHE GLY TYR GLY HIS TYR THR GLY          
SEQRES  29 A  561  ILE ASP LEU ALA GLU GLU ARG SER GLY ASN MET PRO THR          
SEQRES  30 A  561  ARG GLU TRP LYS GLN LYS ARG PHE LYS LYS PRO TRP TYR          
SEQRES  31 A  561  GLN GLY ASP THR ILE PRO VAL GLY ILE GLY GLN GLY TYR          
SEQRES  32 A  561  TRP THR ALA THR PRO ILE GLN MET SER LYS ALA LEU MET          
SEQRES  33 A  561  ILE LEU ILE ASN ASP GLY ILE VAL LYS VAL PRO HIS LEU          
SEQRES  34 A  561  LEU MET SER THR ALA GLU ASP GLY LYS GLN VAL PRO TRP          
SEQRES  35 A  561  VAL GLN PRO HIS GLU PRO PRO VAL GLY ASP ILE HIS SER          
SEQRES  36 A  561  GLY TYR TRP GLU LEU ALA LYS ASP GLY MET TYR GLY VAL          
SEQRES  37 A  561  ALA ASN ARG PRO ASN GLY THR ALA HIS LYS TYR PHE ALA          
SEQRES  38 A  561  SER ALA PRO TYR LYS ILE ALA ALA LYS SER GLY THR ALA          
SEQRES  39 A  561  GLN VAL PHE GLY LEU LYS ALA ASN GLU THR TYR ASN ALA          
SEQRES  40 A  561  HIS LYS ILE ALA GLU ARG LEU ARG ASP HIS LYS LEU MET          
SEQRES  41 A  561  THR ALA PHE ALA PRO TYR ASN ASN PRO GLN VAL ALA VAL          
SEQRES  42 A  561  ALA MET ILE LEU GLU ASN GLY GLY ALA GLY PRO ALA VAL          
SEQRES  43 A  561  GLY THR LEU MET ARG GLN ILE LEU ASP HIS ILE MET LEU          
SEQRES  44 A  561  GLY ASP                                                      
HET    NXL  A1330      17                                                       
HETNAM     NXL (2S,5R)-1-FORMYL-5-[(SULFOOXY)AMINO]PIPERIDINE-2-                
HETNAM   2 NXL  CARBOXAMIDE                                                     
HETSYN     NXL AVIBACTAM, BOUND FORM, NXL104, BOUND FORM                        
FORMUL   2  NXL    C7 H13 N3 O6 S                                               
FORMUL   3  HOH   *123(H2 O)                                                    
HELIX    1 AA1 PRO A   92  VAL A   95  5                                   4    
HELIX    2 AA2 ASN A   97  ASP A  110  1                                  14    
HELIX    3 AA3 THR A  112  ARG A  125  1                                  14    
HELIX    4 AA4 THR A  139  GLN A  150  1                                  12    
HELIX    5 AA5 TYR A  151  PHE A  153  5                                   3    
HELIX    6 AA6 TYR A  168  ALA A  171  5                                   4    
HELIX    7 AA7 LEU A  172  GLY A  177  1                                   6    
HELIX    8 AA8 ASN A  183  ASP A  193  1                                  11    
HELIX    9 AA9 LYS A  195  ALA A  200  5                                   6    
HELIX   10 AB1 LEU A  208  TYR A  214  1                                   7    
HELIX   11 AB2 TYR A  214  HIS A  219  1                                   6    
HELIX   12 AB3 ASP A  255  LEU A  266  1                                  12    
HELIX   13 AB4 PRO A  294  ASP A  299  1                                   6    
HELIX   14 AB5 SER A  302  ASN A  311  1                                  10    
HELIX   15 AB6 ASN A  319  GLY A  324  1                                   6    
HELIX   16 AB7 PRO A  328  THR A  331  5                                   4    
HELIX   17 AB8 VAL A  332  GLY A  344  1                                  13    
HELIX   18 AB9 ASN A  379  SER A  387  1                                   9    
HELIX   19 AC1 ASP A  389  PHE A  411  1                                  23    
HELIX   20 AC2 THR A  431  LYS A  440  1                                  10    
HELIX   21 AC3 TYR A  444  GLY A  452  1                                   9    
HELIX   22 AC4 THR A  461  ASN A  474  1                                  14    
HELIX   23 AC5 GLY A  510  ARG A  525  1                                  16    
HELIX   24 AC6 ALA A  530  ALA A  535  1                                   6    
HELIX   25 AC7 ASN A  593  GLY A  595  5                                   3    
HELIX   26 AC8 ALA A  599  LEU A  613  1                                  15    
SHEET    1 AA1 3 ARG A  58  ILE A  64  0                                        
SHEET    2 AA1 3 GLY A 223  VAL A 229 -1  O  VAL A 227   N  LYS A  60           
SHEET    3 AA1 3 VAL A 235  VAL A 242 -1  O  LEU A 239   N  GLU A 226           
SHEET    1 AA2 3 ILE A 132  LYS A 135  0                                        
SHEET    2 AA2 3 PRO A  78  MET A  90 -1  N  ILE A  88   O  VAL A 134           
SHEET    3 AA2 3 VAL A 156  TYR A 165 -1  O  ARG A 163   N  ARG A  83           
SHEET    1 AA3 6 ILE A 132  LYS A 135  0                                        
SHEET    2 AA3 6 PRO A  78  MET A  90 -1  N  ILE A  88   O  VAL A 134           
SHEET    3 AA3 6 ILE A  71  TYR A  72 -1  N  ILE A  71   O  LEU A  79           
SHEET    4 AA3 6 ILE A 250  LEU A 252  1  O  LEU A 252   N  TYR A  72           
SHEET    5 AA3 6 LEU A 484  THR A 487 -1  O  MET A 485   N  TYR A 251           
SHEET    6 AA3 6 VAL A 494  PRO A 495 -1  O  VAL A 494   N  THR A 487           
SHEET    1 AA4 2 VAL A 179  LYS A 181  0                                        
SHEET    2 AA4 2 ASP A 204  GLY A 206 -1  O  ILE A 205   N  SER A 180           
SHEET    1 AA5 2 GLY A 220  GLN A 221  0                                        
SHEET    2 AA5 2 GLN A 245  ALA A 246 -1  O  GLN A 245   N  GLN A 221           
SHEET    1 AA6 5 VAL A 283  THR A 289  0                                        
SHEET    2 AA6 5 ALA A 271  THR A 276 -1  N  VAL A 275   O  ALA A 285           
SHEET    3 AA6 5 VAL A 585  LEU A 591 -1  O  ALA A 586   N  THR A 276           
SHEET    4 AA6 5 HIS A 571  ALA A 578 -1  N  LYS A 572   O  LEU A 591           
SHEET    5 AA6 5 ALA A 542  ALA A 548 -1  N  GLY A 546   O  LEU A 573           
SHEET    1 AA7 2 LEU A 352  ASP A 354  0                                        
SHEET    2 AA7 2 GLY A 376  LEU A 378 -1  O  LEU A 378   N  LEU A 352           
SHEET    1 AA8 2 TRP A 357  GLN A 359  0                                        
SHEET    2 AA8 2 ARG A 366  ARG A 368 -1  O  TYR A 367   N  TRP A 358           
LINK         OG  SER A 330                 CAN NXL A1330     1555   1555  1.44  
CISPEP   1 THR A  289    PRO A  290          0        -1.09                     
CISPEP   2 GLU A  489    ASP A  490          0        23.89                     
CISPEP   3 ALA A  578    PRO A  579          0       -13.81                     
SITE     1 AC1 12 ALA A 329  SER A 330  LYS A 333  TRP A 370                    
SITE     2 AC1 12 SER A 387  ASP A 389  ILE A 453  SER A 545                    
SITE     3 AC1 12 GLY A 546  THR A 547  HOH A 709  HOH A 738                    
CRYST1  125.078  182.875   74.767  90.00  90.00  90.00 C 2 2 21      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      0.007995  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005468  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013375        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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