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Database: PDB
Entry: 5O7N
LinkDB: 5O7N
Original site: 5O7N 
HEADER    HYDROLASE                               09-JUN-17   5O7N              
TITLE     BETA-LACTAMASE VIM-2 IN COMPLEX WITH (2R)-1-(2-BENZYL-3-              
TITLE    2 MERCAPTOPROPANOYL)PIPERIDINE-2-CARBOXYLIC ACID                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-LACTAMASE VIM-2;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE;                          
SOURCE   3 ORGANISM_TAXID: 573;                                                 
SOURCE   4 GENE: BLAVIM-2;                                                      
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST14                                   
KEYWDS    INHIBITOR, COMPLEX, MBL, BETA-LACTAMASE VIM-2, (2R)-1-(2-BENZYL-3-    
KEYWDS   2 MERCAPTOPROPANOYL)PIPERIDINE-2-CARBOXYLIC ACID, HYDROLASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.BUETTNER,J.S.KRAMER,D.POGORYELOV,E.PROSCHAK                         
REVDAT   2   03-JUL-19 5O7N    1       JRNL                                     
REVDAT   1   20-JUN-18 5O7N    0                                                
JRNL        AUTH   D.BUTTNER,J.S.KRAMER,F.M.KLINGLER,S.K.WITTMANN,M.R.HARTMANN, 
JRNL        AUTH 2 C.G.KURZ,D.KOHNHAUSER,L.WEIZEL,A.BRUGGERHOFF,D.FRANK,        
JRNL        AUTH 3 D.STEINHILBER,T.A.WICHELHAUS,D.POGORYELOV,E.PROSCHAK         
JRNL        TITL   CHALLENGES IN THE DEVELOPMENT OF A THIOL-BASED               
JRNL        TITL 2 BROAD-SPECTRUM INHIBITOR FOR METALLO-BETA-LACTAMASES.        
JRNL        REF    ACS INFECT DIS.               V.   4   360 2018              
JRNL        REFN                   ESSN 2373-8227                               
JRNL        PMID   29172434                                                     
JRNL        DOI    10.1021/ACSINFECDIS.7B00129                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.51                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 128064                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.790                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3573                            
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 51.4800 -  4.4430    0.99     4822   137  0.1752 0.1787        
REMARK   3     2  4.4430 -  3.5267    1.00     4819   140  0.1513 0.1873        
REMARK   3     3  3.5267 -  3.0810    1.00     4801   152  0.1659 0.1811        
REMARK   3     4  3.0810 -  2.7993    1.00     4832   146  0.0000 0.2400        
REMARK   3     5  2.7993 -  2.5987    1.00     4795   142  0.0000 0.1874        
REMARK   3     6  2.5987 -  2.4454    0.94     4618   125  0.0000 0.1753        
REMARK   3     7  2.4454 -  2.3230    0.94     4492   122  0.0000 0.2314        
REMARK   3     8  2.3230 -  2.2219    0.98     4771   135  0.1862 0.2350        
REMARK   3     9  2.2219 -  2.1363    0.99     4780   128  0.1788 0.2213        
REMARK   3    10  2.1363 -  2.0626    0.99     4805   131  0.1716 0.2016        
REMARK   3    11  2.0626 -  1.9981    0.99     4762   148  0.1711 0.1835        
REMARK   3    12  1.9981 -  1.9410    1.00     4820   120  0.1705 0.1807        
REMARK   3    13  1.9410 -  1.8899    1.00     4803   141  0.1803 0.2025        
REMARK   3    14  1.8899 -  1.8438    1.00     4810   147  0.1807 0.2209        
REMARK   3    15  1.8438 -  1.8019    1.00     4797   143  0.1988 0.2217        
REMARK   3    16  1.8019 -  1.7635    1.00     4800   126  0.2145 0.2771        
REMARK   3    17  1.7635 -  1.7282    1.00     4842   146  0.2237 0.2483        
REMARK   3    18  1.7282 -  1.6956    1.00     4850   142  0.2303 0.2280        
REMARK   3    19  1.6956 -  1.6653    1.00     4826   138  0.2304 0.2927        
REMARK   3    20  1.6653 -  1.6371    1.00     4807   134  0.2436 0.2714        
REMARK   3    21  1.6371 -  1.6107    1.00     4819   128  0.2432 0.2711        
REMARK   3    22  1.6107 -  1.5859    1.00     4816   152  0.2463 0.2772        
REMARK   3    23  1.5859 -  1.5626    1.00     4789   126  0.2538 0.2502        
REMARK   3    24  1.5626 -  1.5406    1.00     4796   145  0.2601 0.2837        
REMARK   3    25  1.5406 -  1.5197    1.00     4798   133  0.2749 0.2742        
REMARK   3    26  1.5197 -  1.5000    1.00     4821   146  0.2836 0.2915        
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)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.420           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.97                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.20                          
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      :  0.007           3730                                  
REMARK   3   ANGLE     :  0.936           5094                                  
REMARK   3   CHIRALITY :  0.065            574                                  
REMARK   3   PLANARITY :  0.006            674                                  
REMARK   3   DIHEDRAL  : 19.994           1304                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 5O7N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-JUN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200002178.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-SEP-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-3                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9677                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 4M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 128072                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.507                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.07561                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.7400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54090                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.170                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: AUTOSOL, PHASER                                       
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 32.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE VIM-2 IN CRYSTALLIZATION BUFFER      
REMARK 280  (50 MM TRIS/HCL PH 7.2, 100 UM ZNCL2 AND 150 MM NACL) WAS           
REMARK 280  CONCENTRATED TO 11,4 MG/ML, BEFORE 5 % GLYCEROL WAS ADDED AND       
REMARK 280  THE PROTEIN WAS FLASH FROZEN IN LIQUID NITROGEN. FOR                
REMARK 280  CRYSTALLISATION THE THRAWED PROTEIN SOLUTIONS WAS MIXED WITH        
REMARK 280  PRECIPITATION SOLUTION (34% PEG3350, 0,25 M MG FORMATE, 5 MM BME    
REMARK 280  + 2.5% OF A 1M DMSO INHIBITOR STOCK IN THE DROP) IN DIFFERANT       
REMARK 280  RATIOS. AS RESERVOIR PRECIPITATION SOLUTION WITHOUT INHIBITOR       
REMARK 280  WAS USED., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290.15K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       50.99450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.65400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       50.99450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       39.65400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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 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 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 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 435  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     MET A    13                                                      
REMARK 465     HIS A    14                                                      
REMARK 465     HIS A    15                                                      
REMARK 465     HIS A    16                                                      
REMARK 465     HIS A    17                                                      
REMARK 465     HIS A    18                                                      
REMARK 465     HIS A    19                                                      
REMARK 465     GLU A    20                                                      
REMARK 465     ASN A    21                                                      
REMARK 465     LEU A    22                                                      
REMARK 465     TYR A    23                                                      
REMARK 465     PHE A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     GLY A    26                                                      
REMARK 465     VAL A    27                                                      
REMARK 465     ASP A    28                                                      
REMARK 465     SER A    29                                                      
REMARK 465     SER A    30                                                      
REMARK 465     VAL A    36                                                      
REMARK 465     SER A    37                                                      
REMARK 465     VAL A   264                                                      
REMARK 465     VAL A   265                                                      
REMARK 465     GLU A   266                                                      
REMARK 465     MET B    13                                                      
REMARK 465     HIS B    14                                                      
REMARK 465     HIS B    15                                                      
REMARK 465     HIS B    16                                                      
REMARK 465     HIS B    17                                                      
REMARK 465     HIS B    18                                                      
REMARK 465     HIS B    19                                                      
REMARK 465     GLU B    20                                                      
REMARK 465     ASN B    21                                                      
REMARK 465     LEU B    22                                                      
REMARK 465     TYR B    23                                                      
REMARK 465     PHE B    24                                                      
REMARK 465     GLN B    25                                                      
REMARK 465     GLY B    26                                                      
REMARK 465     VAL B    27                                                      
REMARK 465     ASP B    28                                                      
REMARK 465     SER B    29                                                      
REMARK 465     SER B    30                                                      
REMARK 465     GLY B    31                                                      
REMARK 465     VAL B   264                                                      
REMARK 465     VAL B   265                                                      
REMARK 465     GLU B   266                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   539     O    HOH A   557              1.84            
REMARK 500   O    HOH A   414     O    HOH A   532              1.95            
REMARK 500   O    HOH A   519     O    HOH A   523              1.97            
REMARK 500   O    HOH A   533     O    HOH A   534              1.99            
REMARK 500   O    HOH A   506     O    HOH A   550              2.04            
REMARK 500   OE1  GLU A    43     NH2  ARG A    45              2.07            
REMARK 500   O    HOH B   497     O    HOH B   556              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   477     O    HOH B   534     3454     2.15            
REMARK 500   O    HOH A   444     O    HOH A   504     4747     2.18            
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    ASP A  84      145.46     72.09                                   
REMARK 500    TRP A  87       68.80     70.71                                   
REMARK 500    ALA A 178     -105.33   -150.38                                   
REMARK 500    ASP B  84      148.17     75.02                                   
REMARK 500    TRP B  87       72.06     69.51                                   
REMARK 500    ALA B 178     -106.63   -151.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 114   NE2                                                    
REMARK 620 2 HIS A 116   ND1  96.1                                              
REMARK 620 3 HIS A 179   NE2 102.1 106.3                                        
REMARK 620 4 9NK A 305   S01 132.0 104.1 112.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 118   OD2                                                    
REMARK 620 2 CYS A 198   SG  116.6                                              
REMARK 620 3 HIS A 240   NE2  95.1 109.3                                        
REMARK 620 4 9NK A 305   S01  97.9 116.6 119.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 304  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 153   NE2                                                    
REMARK 620 2 FMT A 308   O1   86.7                                              
REMARK 620 3 FMT A 308   O2  124.0  57.2                                        
REMARK 620 4 FMT A 309   O1  133.4 116.9  59.8                                  
REMARK 620 5 HIS A 251   ND1  49.6  73.8  78.0  96.7                            
REMARK 620 6 FMT A 307   O2  100.8 164.0 107.3  48.2 100.2                      
REMARK 620 7 FMT A 306   O1   80.3   6.5  62.5 122.3  70.4 166.9                
REMARK 620 8 FMT A 306   O2  122.3  52.3   5.1  64.7  78.2 112.3  57.7          
REMARK 620 9 FMT A 307   O1  134.5 109.6  52.4   7.5  93.3  55.3 114.9  57.3    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 251   ND1                                                    
REMARK 620 2 FMT A 306   O2  120.4                                              
REMARK 620 3 FMT A 307   O1  116.1  57.5                                        
REMARK 620 4 FMT A 306   O1  101.0  55.2 112.5                                  
REMARK 620 5 FMT A 307   O2   94.0 114.4  57.4 164.7                            
REMARK 620 6 HIS A 153   NE2  10.9 110.1 114.6  92.3 102.4                      
REMARK 620 7 FMT A 308   O2  122.6   4.8  52.8  59.7 109.6 112.6                
REMARK 620 8 FMT A 309   O1  112.0  65.0   7.6 120.1  50.1 112.0  60.4          
REMARK 620 9 FMT A 308   O1  100.5  50.1 107.5   6.2 162.9  91.2  54.7 115.1    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 114   NE2                                                    
REMARK 620 2 HIS B 116   ND1  97.8                                              
REMARK 620 3 HIS B 179   NE2 103.9 107.4                                        
REMARK 620 4 9NK B 305   S01 127.9 119.2  98.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 118   OD2                                                    
REMARK 620 2 CYS B 198   SG  111.6                                              
REMARK 620 3 HIS B 240   NE2  96.1 105.7                                        
REMARK 620 4 9NK B 305   S01 110.7 115.3 115.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 153   NE2                                                    
REMARK 620 2 FMT B 307   O1   84.4                                              
REMARK 620 3 FMT B 306   O1   91.1 174.0                                        
REMARK 620 4 FMT B 306   O2  134.8 118.0  62.9                                  
REMARK 620 5 FMT B 307   O2  138.9  61.0 121.5  59.7                            
REMARK 620 6 HIS B 251   ND1  45.3  75.0  99.0 100.0 101.0                      
REMARK 620 7 FMT B 308   O1   74.6  12.7 161.3 119.4  67.5  62.4                
REMARK 620 8 FMT B 308   O2  125.5  48.9 132.8  69.9  13.6  90.6  54.3          
REMARK 620 9 FMT B 309   O1   97.1 159.8  17.3  48.5 108.3  91.7 150.9 117.7    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 304  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 251   ND1                                                    
REMARK 620 2 FMT B 309   O2  108.8                                              
REMARK 620 3 FMT B 309   O1   98.1  63.1                                        
REMARK 620 4 FMT B 308   O2  108.5  58.6 120.9                                  
REMARK 620 5 FMT B 308   O1  113.4 106.8 148.4  52.6                            
REMARK 620 6 HIS B 153   NE2   9.6 110.5 107.4 101.0 104.2                      
REMARK 620 7 FMT B 306   O2  106.1  11.9  51.5  70.5 117.7 109.8                
REMARK 620 8 FMT B 307   O2  101.6  49.6 112.8  12.8  65.0  95.5  61.3          
REMARK 620 9 FMT B 306   O1   84.1  79.0  18.4 137.6 157.5  93.6  67.1 127.6    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9NK A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9NK B 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues FMT A 306 and FMT A      
REMARK 800  308                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues FMT A 306 and FMT A      
REMARK 800  308                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues FMT A 307 and FMT A      
REMARK 800  309                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues FMT B 307 and FMT B      
REMARK 800  308                                                                 
DBREF1 5O7N A   27   266  UNP                  A0A173FE28_KLEPN                 
DBREF2 5O7N A     A0A173FE28                          9         248             
DBREF1 5O7N B   27   266  UNP                  A0A173FE28_KLEPN                 
DBREF2 5O7N B     A0A173FE28                          9         248             
SEQADV 5O7N MET A   13  UNP  A0A173FE2           INITIATING METHIONINE          
SEQADV 5O7N HIS A   14  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N HIS A   15  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N HIS A   16  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N HIS A   17  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N HIS A   18  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N HIS A   19  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N GLU A   20  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N ASN A   21  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N LEU A   22  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N TYR A   23  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N PHE A   24  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N GLN A   25  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N GLY A   26  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N MET B   13  UNP  A0A173FE2           INITIATING METHIONINE          
SEQADV 5O7N HIS B   14  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N HIS B   15  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N HIS B   16  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N HIS B   17  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N HIS B   18  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N HIS B   19  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N GLU B   20  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N ASN B   21  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N LEU B   22  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N TYR B   23  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N PHE B   24  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N GLN B   25  UNP  A0A173FE2           EXPRESSION TAG                 
SEQADV 5O7N GLY B   26  UNP  A0A173FE2           EXPRESSION TAG                 
SEQRES   1 A  254  MET HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN          
SEQRES   2 A  254  GLY VAL ASP SER SER GLY GLU TYR PRO THR VAL SER GLU          
SEQRES   3 A  254  ILE PRO VAL GLY GLU VAL ARG LEU TYR GLN ILE ALA ASP          
SEQRES   4 A  254  GLY VAL TRP SER HIS ILE ALA THR GLN SER PHE ASP GLY          
SEQRES   5 A  254  ALA VAL TYR PRO SER ASN GLY LEU ILE VAL ARG ASP GLY          
SEQRES   6 A  254  ASP GLU LEU LEU LEU ILE ASP THR ALA TRP GLY ALA LYS          
SEQRES   7 A  254  ASN THR ALA ALA LEU LEU ALA GLU ILE GLU LYS GLN ILE          
SEQRES   8 A  254  GLY LEU PRO VAL THR ARG ALA VAL SER THR HIS PHE HIS          
SEQRES   9 A  254  ASP ASP ARG VAL GLY GLY VAL ASP VAL LEU ARG ALA ALA          
SEQRES  10 A  254  GLY VAL ALA THR TYR ALA SER PRO SER THR ARG ARG LEU          
SEQRES  11 A  254  ALA GLU VAL GLU GLY ASN GLU ILE PRO THR HIS SER LEU          
SEQRES  12 A  254  GLU GLY LEU SER SER SER GLY ASP ALA VAL ARG PHE GLY          
SEQRES  13 A  254  PRO VAL GLU LEU PHE TYR PRO GLY ALA ALA HIS SER THR          
SEQRES  14 A  254  ASP ASN LEU VAL VAL TYR VAL PRO SER ALA SER VAL LEU          
SEQRES  15 A  254  TYR GLY GLY CYS ALA ILE TYR GLU LEU SER ARG THR SER          
SEQRES  16 A  254  ALA GLY ASN VAL ALA ASP ALA ASP LEU ALA GLU TRP PRO          
SEQRES  17 A  254  THR SER ILE GLU ARG ILE GLN GLN HIS TYR PRO GLU ALA          
SEQRES  18 A  254  GLN PHE VAL ILE PRO GLY HIS GLY LEU PRO GLY GLY LEU          
SEQRES  19 A  254  ASP LEU LEU LYS HIS THR THR ASN VAL VAL LYS ALA HIS          
SEQRES  20 A  254  THR ASN ARG SER VAL VAL GLU                                  
SEQRES   1 B  254  MET HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN          
SEQRES   2 B  254  GLY VAL ASP SER SER GLY GLU TYR PRO THR VAL SER GLU          
SEQRES   3 B  254  ILE PRO VAL GLY GLU VAL ARG LEU TYR GLN ILE ALA ASP          
SEQRES   4 B  254  GLY VAL TRP SER HIS ILE ALA THR GLN SER PHE ASP GLY          
SEQRES   5 B  254  ALA VAL TYR PRO SER ASN GLY LEU ILE VAL ARG ASP GLY          
SEQRES   6 B  254  ASP GLU LEU LEU LEU ILE ASP THR ALA TRP GLY ALA LYS          
SEQRES   7 B  254  ASN THR ALA ALA LEU LEU ALA GLU ILE GLU LYS GLN ILE          
SEQRES   8 B  254  GLY LEU PRO VAL THR ARG ALA VAL SER THR HIS PHE HIS          
SEQRES   9 B  254  ASP ASP ARG VAL GLY GLY VAL ASP VAL LEU ARG ALA ALA          
SEQRES  10 B  254  GLY VAL ALA THR TYR ALA SER PRO SER THR ARG ARG LEU          
SEQRES  11 B  254  ALA GLU VAL GLU GLY ASN GLU ILE PRO THR HIS SER LEU          
SEQRES  12 B  254  GLU GLY LEU SER SER SER GLY ASP ALA VAL ARG PHE GLY          
SEQRES  13 B  254  PRO VAL GLU LEU PHE TYR PRO GLY ALA ALA HIS SER THR          
SEQRES  14 B  254  ASP ASN LEU VAL VAL TYR VAL PRO SER ALA SER VAL LEU          
SEQRES  15 B  254  TYR GLY GLY CYS ALA ILE TYR GLU LEU SER ARG THR SER          
SEQRES  16 B  254  ALA GLY ASN VAL ALA ASP ALA ASP LEU ALA GLU TRP PRO          
SEQRES  17 B  254  THR SER ILE GLU ARG ILE GLN GLN HIS TYR PRO GLU ALA          
SEQRES  18 B  254  GLN PHE VAL ILE PRO GLY HIS GLY LEU PRO GLY GLY LEU          
SEQRES  19 B  254  ASP LEU LEU LYS HIS THR THR ASN VAL VAL LYS ALA HIS          
SEQRES  20 B  254  THR ASN ARG SER VAL VAL GLU                                  
HET     ZN  A 301       1                                                       
HET     ZN  A 302       1                                                       
HET     ZN  A 303       1                                                       
HET     ZN  A 304       1                                                       
HET    9NK  A 305      21                                                       
HET    FMT  A 306       3                                                       
HET    FMT  A 307       3                                                       
HET    FMT  A 308       3                                                       
HET    FMT  A 309       3                                                       
HET    EDO  A 310       4                                                       
HET     ZN  B 301       1                                                       
HET     ZN  B 302       1                                                       
HET     ZN  B 303       1                                                       
HET     ZN  B 304       1                                                       
HET    9NK  B 305      21                                                       
HET    FMT  B 306       3                                                       
HET    FMT  B 307       3                                                       
HET    FMT  B 308       3                                                       
HET    FMT  B 309       3                                                       
HET    EDO  B 310       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     9NK (2~{R})-1-[(2~{S})-2-(PHENYLMETHYL)-3-SULFANYL-                  
HETNAM   2 9NK  PROPANOYL]PIPERIDINE-2-CARBOXYLIC ACID                          
HETNAM     FMT FORMIC ACID                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3   ZN    8(ZN 2+)                                                     
FORMUL   7  9NK    2(C16 H21 N O3 S)                                            
FORMUL   8  FMT    8(C H2 O2)                                                   
FORMUL  12  EDO    2(C2 H6 O2)                                                  
FORMUL  23  HOH   *338(H2 O)                                                    
HELIX    1 AA1 GLY A   88  ILE A  103  1                                  16    
HELIX    2 AA2 HIS A  116  GLY A  121  1                                   6    
HELIX    3 AA3 GLY A  122  ALA A  129  1                                   8    
HELIX    4 AA4 SER A  136  GLY A  147  1                                  12    
HELIX    5 AA5 CYS A  198  ILE A  200  5                                   3    
HELIX    6 AA6 GLU A  218  TYR A  230  1                                  13    
HELIX    7 AA7 LEU A  246  ASN A  261  1                                  16    
HELIX    8 AA8 GLY B   88  ILE B  103  1                                  16    
HELIX    9 AA9 HIS B  116  GLY B  121  1                                   6    
HELIX   10 AB1 GLY B  122  ALA B  129  1                                   8    
HELIX   11 AB2 SER B  136  GLY B  147  1                                  12    
HELIX   12 AB3 CYS B  198  ILE B  200  5                                   3    
HELIX   13 AB4 GLU B  218  TYR B  230  1                                  13    
HELIX   14 AB5 LEU B  246  ASN B  261  1                                  16    
SHEET    1 AA1 7 VAL A  44  ALA A  50  0                                        
SHEET    2 AA1 7 VAL A  53  PHE A  62 -1  O  ILE A  57   N  ARG A  45           
SHEET    3 AA1 7 ALA A  65  ASP A  76 -1  O  TYR A  67   N  GLN A  60           
SHEET    4 AA1 7 GLU A  79  ILE A  83 -1  O  ILE A  83   N  LEU A  72           
SHEET    5 AA1 7 VAL A 107  VAL A 111  1  O  ARG A 109   N  LEU A  82           
SHEET    6 AA1 7 ALA A 132  ALA A 135  1  O  ALA A 132   N  ALA A 110           
SHEET    7 AA1 7 HIS A 153  SER A 154  1  O  HIS A 153   N  THR A 133           
SHEET    1 AA2 5 ALA A 164  PHE A 167  0                                        
SHEET    2 AA2 5 VAL A 170  PHE A 173 -1  O  LEU A 172   N  VAL A 165           
SHEET    3 AA2 5 VAL A 185  VAL A 188 -1  O  VAL A 185   N  PHE A 173           
SHEET    4 AA2 5 VAL A 193  GLY A 197 -1  O  TYR A 195   N  VAL A 186           
SHEET    5 AA2 5 PHE A 235  PRO A 238  1  O  PHE A 235   N  LEU A 194           
SHEET    1 AA3 7 VAL B  44  ALA B  50  0                                        
SHEET    2 AA3 7 VAL B  53  PHE B  62 -1  O  ILE B  57   N  ARG B  45           
SHEET    3 AA3 7 ALA B  65  ASP B  76 -1  O  TYR B  67   N  GLN B  60           
SHEET    4 AA3 7 GLU B  79  ILE B  83 -1  O  ILE B  83   N  LEU B  72           
SHEET    5 AA3 7 VAL B 107  VAL B 111  1  O  ARG B 109   N  LEU B  82           
SHEET    6 AA3 7 ALA B 132  ALA B 135  1  O  ALA B 132   N  THR B 108           
SHEET    7 AA3 7 HIS B 153  SER B 154  1  O  HIS B 153   N  THR B 133           
SHEET    1 AA4 5 ASP B 163  PHE B 167  0                                        
SHEET    2 AA4 5 VAL B 170  TYR B 174 -1  O  LEU B 172   N  VAL B 165           
SHEET    3 AA4 5 VAL B 185  VAL B 188 -1  O  TYR B 187   N  GLU B 171           
SHEET    4 AA4 5 VAL B 193  GLY B 197 -1  O  TYR B 195   N  VAL B 186           
SHEET    5 AA4 5 PHE B 235  PRO B 238  1  O  PHE B 235   N  LEU B 194           
LINK         NE2 HIS A 114                ZN    ZN A 301     1555   1555  2.04  
LINK         ND1 HIS A 116                ZN    ZN A 301     1555   1555  1.80  
LINK         OD2 ASP A 118                ZN    ZN A 302     1555   1555  2.03  
LINK         NE2 HIS A 153                ZN    ZN A 304     1555   1555  1.93  
LINK         NE2 HIS A 179                ZN    ZN A 301     1555   1555  2.00  
LINK         SG ACYS A 198                ZN    ZN A 302     1555   1555  2.06  
LINK         NE2 HIS A 240                ZN    ZN A 302     1555   1555  2.08  
LINK         ND1 HIS A 251                ZN    ZN A 303     1555   1555  2.04  
LINK         NE2 HIS B 114                ZN    ZN B 301     1555   1555  2.04  
LINK         ND1 HIS B 116                ZN    ZN B 301     1555   1555  1.82  
LINK         OD2 ASP B 118                ZN    ZN B 302     1555   1555  2.01  
LINK         NE2 HIS B 153                ZN    ZN B 303     1555   1555  1.94  
LINK         NE2 HIS B 179                ZN    ZN B 301     1555   1555  2.03  
LINK         SG ACYS B 198                ZN    ZN B 302     1555   1555  2.28  
LINK         NE2 HIS B 240                ZN    ZN B 302     1555   1555  2.13  
LINK         ND1 HIS B 251                ZN    ZN B 304     1555   1555  1.99  
LINK        ZN    ZN A 301                 S01 9NK A 305     1555   1555  2.38  
LINK        ZN    ZN A 302                 S01 9NK A 305     1555   1555  2.78  
LINK        ZN    ZN A 303                 O2  FMT A 306     1555   1555  2.18  
LINK        ZN    ZN A 303                 O1  FMT A 307     1555   1555  2.29  
LINK        ZN    ZN A 303                 O1  FMT A 306     1555   1555  2.49  
LINK        ZN    ZN A 303                 O2  FMT A 307     1555   1555  2.25  
LINK        ZN    ZN A 304                 O1  FMT A 308     1555   1555  2.46  
LINK        ZN    ZN A 304                 O2  FMT A 308     1555   1555  2.02  
LINK        ZN    ZN A 304                 O1  FMT A 309     1555   1555  2.35  
LINK        ZN    ZN B 301                 S01 9NK B 305     1555   1555  2.32  
LINK        ZN    ZN B 302                 S01 9NK B 305     1555   1555  2.33  
LINK        ZN    ZN B 303                 O1  FMT B 307     1555   1555  2.10  
LINK        ZN    ZN B 303                 O1  FMT B 306     1555   1555  2.04  
LINK        ZN    ZN B 303                 O2  FMT B 306     1555   1555  2.14  
LINK        ZN    ZN B 303                 O2  FMT B 307     1555   1555  2.20  
LINK        ZN    ZN B 304                 O2  FMT B 309     1555   1555  2.13  
LINK        ZN    ZN B 304                 O1  FMT B 309     1555   1555  2.03  
LINK        ZN    ZN B 304                 O2  FMT B 308     1555   1555  2.65  
LINK        ZN    ZN B 304                 O1  FMT B 308     1555   1555  2.18  
LINK         NE2 HIS A 153                ZN    ZN A 303     1555   4757  2.00  
LINK         ND1 HIS A 251                ZN    ZN A 304     1555   4747  2.10  
LINK         NE2 HIS B 153                ZN    ZN B 304     1555   4748  2.04  
LINK         ND1 HIS B 251                ZN    ZN B 303     1555   4758  2.06  
LINK        ZN    ZN A 303                 O2  FMT A 308     1555   4747  2.07  
LINK        ZN    ZN A 303                 O1  FMT A 309     1555   4747  2.28  
LINK        ZN    ZN A 303                 O1  FMT A 308     1555   4747  2.57  
LINK        ZN    ZN A 303                 O2  FMT A 309     1555   4747  2.66  
LINK        ZN    ZN A 304                 O2  FMT A 307     1555   4757  2.36  
LINK        ZN    ZN A 304                 O1  FMT A 306     1555   4757  2.37  
LINK        ZN    ZN A 304                 O2  FMT A 306     1555   4757  2.13  
LINK        ZN    ZN A 304                 O1  FMT A 307     1555   4757  2.34  
LINK         C   FMT A 306                 O2  FMT A 308     1555   4747  1.45  
LINK         O1  FMT A 306                 C   FMT A 308     1555   4747  1.48  
LINK         C   FMT A 307                 O2  FMT A 309     1555   4747  1.34  
LINK        ZN    ZN B 303                 O1  FMT B 308     1555   4748  2.04  
LINK        ZN    ZN B 303                 O2  FMT B 308     1555   4748  2.61  
LINK        ZN    ZN B 303                 O1  FMT B 309     1555   4748  2.16  
LINK        ZN    ZN B 303                 O2  FMT B 309     1555   4748  2.22  
LINK        ZN    ZN B 304                 O2  FMT B 306     1555   4758  2.03  
LINK        ZN    ZN B 304                 O2  FMT B 307     1555   4758  2.20  
LINK        ZN    ZN B 304                 O1  FMT B 306     1555   4758  1.91  
LINK        ZN    ZN B 304                 O1  FMT B 307     1555   4758  2.23  
LINK         C   FMT B 307                 O1  FMT B 308     1555   4748  1.43  
SITE     1 AC1  4 HIS A 114  HIS A 116  HIS A 179  9NK A 305                    
SITE     1 AC2  5 ASP A 118  ARG A 119  CYS A 198  HIS A 240                    
SITE     2 AC2  5 9NK A 305                                                     
SITE     1 AC3  6 HIS A 153  HIS A 251  FMT A 306  FMT A 307                    
SITE     2 AC3  6 FMT A 308  FMT A 309                                          
SITE     1 AC4  6 HIS A 153  HIS A 251  FMT A 306  FMT A 307                    
SITE     2 AC4  6 FMT A 308  FMT A 309                                          
SITE     1 AC5 12 TRP A  87  HIS A 116  ASP A 118  HIS A 179                    
SITE     2 AC5 12 CYS A 198  ARG A 205  GLY A 209  ASN A 210                    
SITE     3 AC5 12 HIS A 240   ZN A 301   ZN A 302  HOH A 436                    
SITE     1 AC6  5 ASP A  76  LEU A  80  THR A 108  ARG A 109                    
SITE     2 AC6  5 PRO A 169                                                     
SITE     1 AC7  4 HIS B 114  HIS B 116  HIS B 179  9NK B 305                    
SITE     1 AC8  4 ASP B 118  CYS B 198  HIS B 240  9NK B 305                    
SITE     1 AC9  3 HIS B 153  FMT B 306  FMT B 307                               
SITE     1 AD1  3 HIS B 251  FMT B 308  FMT B 309                               
SITE     1 AD2 13 TYR B  67  HIS B 116  ASP B 118  HIS B 179                    
SITE     2 AD2 13 CYS B 198  GLY B 209  ASN B 210  HIS B 240                    
SITE     3 AD2 13  ZN B 301   ZN B 302  HOH B 423  HOH B 428                    
SITE     4 AD2 13 HOH B 429                                                     
SITE     1 AD3  4 ALA B 132  HIS B 153   ZN B 303  FMT B 307                    
SITE     1 AD4  5 THR B 206  HIS B 251  ASN B 254   ZN B 304                    
SITE     2 AD4  5 FMT B 308                                                     
SITE     1 AD5  6 ASP A  63  GLY A  64  TYR B  67  GLU B 202                    
SITE     2 AD5  6 ARG B 205  HOH B 455                                          
SITE     1 AD6  9 ALA A 132  THR A 152  HIS A 153  HIS A 251                    
SITE     2 AD6  9 ASN A 254   ZN A 303   ZN A 304  FMT A 307                    
SITE     3 AD6  9 FMT A 309                                                     
SITE     1 AD7  9 ALA A 132  THR A 152  HIS A 153  HIS A 251                    
SITE     2 AD7  9 ASN A 254   ZN A 303   ZN A 304  FMT A 307                    
SITE     3 AD7  9 FMT A 309                                                     
SITE     1 AD8 10 ALA A 132  HIS A 153  THR A 206  HIS A 251                    
SITE     2 AD8 10 ASN A 254   ZN A 303   ZN A 304  FMT A 306                    
SITE     3 AD8 10 FMT A 308  HOH A 405                                          
SITE     1 AD9  8 THR B 152  HIS B 153  HIS B 251  ASN B 254                    
SITE     2 AD9  8  ZN B 303   ZN B 304  FMT B 306  FMT B 309                    
CRYST1  101.989   79.308   67.645  90.00 130.45  90.00 C 1 2 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      0.009805  0.000000  0.008359        0.00000                         
SCALE2      0.000000  0.012609  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019427        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system