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Database: PDB
Entry: 4PKU
LinkDB: 4PKU
Original site: 4PKU 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           15-MAY-14   4PKU              
TITLE     ANTHRAX TOXIN LETHAL FACTOR WITH BOUND SMALL MOLECULE INHIBITOR 15    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LETHAL FACTOR;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 298-809;                                      
COMPND   5 SYNONYM: LF,ANTHRAX LETHAL TOXIN ENDOPEPTIDASE COMPONENT;            
COMPND   6 EC: 3.4.24.83;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;                             
SOURCE   3 ORGANISM_TAXID: 1392;                                                
SOURCE   4 GENE: LEF, PXO1-107, BXA0172, GBAA_PXO1_0172;                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 PLYSS;                           
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PMCSG10                                   
KEYWDS    ANTHRAX TOXIN, LETHAL FACTOR, METALLOPROTEINASE, METALLOPROTEASE,     
KEYWDS   2 STRUCTURAL DYNAMICS, LIGAND-INDUCED CONFORMATIONAL CHANGE,           
KEYWDS   3 HYDROLASE-HYDROLASE INHIBITOR COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.M.MAIZE,T.DE LA MORA,B.C.FINZEL                                     
REVDAT   5   27-DEC-23 4PKU    1       REMARK                                   
REVDAT   4   11-DEC-19 4PKU    1       REMARK                                   
REVDAT   3   27-SEP-17 4PKU    1       SOURCE KEYWDS REMARK                     
REVDAT   2   26-NOV-14 4PKU    1       JRNL                                     
REVDAT   1   12-NOV-14 4PKU    0                                                
JRNL        AUTH   K.M.MAIZE,E.K.KURBANOV,T.DE LA MORA-REY,T.W.GEDERS,          
JRNL        AUTH 2 D.J.HWANG,M.A.WALTERS,R.L.JOHNSON,E.A.AMIN,B.C.FINZEL        
JRNL        TITL   ANTHRAX TOXIN LETHAL FACTOR DOMAIN 3 IS HIGHLY MOBILE AND    
JRNL        TITL 2 RESPONSIVE TO LIGAND BINDING.                                
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  70  2813 2014              
JRNL        REFN                   ESSN 1399-0047                               
JRNL        PMID   25372673                                                     
JRNL        DOI    10.1107/S1399004714018161                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.4_1496                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.51                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 24080                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1223                            
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 45.5224 -  4.9903    1.00     2698   148  0.1734 0.2102        
REMARK   3     2  4.9903 -  3.9616    1.00     2565   139  0.1628 0.2331        
REMARK   3     3  3.9616 -  3.4611    1.00     2547   140  0.1839 0.2413        
REMARK   3     4  3.4611 -  3.1447    1.00     2527   146  0.2256 0.2793        
REMARK   3     5  3.1447 -  2.9193    1.00     2520   113  0.2364 0.2866        
REMARK   3     6  2.9193 -  2.7473    1.00     2540   121  0.2292 0.2867        
REMARK   3     7  2.7473 -  2.6097    1.00     2484   138  0.2319 0.2877        
REMARK   3     8  2.6097 -  2.4961    1.00     2492   151  0.2286 0.2784        
REMARK   3     9  2.4961 -  2.4000    1.00     2484   127  0.2318 0.2955        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.470           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.67                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.23                          
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      :  0.003           4037                                  
REMARK   3   ANGLE     :  0.752           5452                                  
REMARK   3   CHIRALITY :  0.028            603                                  
REMARK   3   PLANARITY :  0.003            702                                  
REMARK   3   DIHEDRAL  : 15.545           1519                                  
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 4PKU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000201583.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS 2.5.1                          
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24160                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 143.360                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 11-16% PEG 8K, 50 MM BIS-TRIS, 100 MM    
REMARK 280  MAGNESIUM ACETATE, PH 6.8, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 286K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       30.66850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.67900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.94750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.67900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.66850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.94750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A   262                                                      
REMARK 465     ASN A   263                                                      
REMARK 465     ALA A   264                                                      
REMARK 465     LEU A   265                                                      
REMARK 465     ILE A   345                                                      
REMARK 465     ARG A   346                                                      
REMARK 465     ASP A   347                                                      
REMARK 465     SER A   348                                                      
REMARK 465     LEU A   349                                                      
REMARK 465     SER A   350                                                      
REMARK 465     GLU A   351                                                      
REMARK 465     GLU A   352                                                      
REMARK 465     GLU A   353                                                      
REMARK 465     LYS A   354                                                      
REMARK 465     GLU A   355                                                      
REMARK 465     LEU A   356                                                      
REMARK 465     LEU A   357                                                      
REMARK 465     ASN A   358                                                      
REMARK 465     ARG A   359                                                      
REMARK 465     ILE A   360                                                      
REMARK 465     GLN A   361                                                      
REMARK 465     VAL A   362                                                      
REMARK 465     ASP A   363                                                      
REMARK 465     SER A   364                                                      
REMARK 465     SER A   365                                                      
REMARK 465     ASN A   366                                                      
REMARK 465     LEU A   777                                                      
REMARK 465     VAL A   778                                                      
REMARK 465     PRO A   779                                                      
REMARK 465     ARG A   780                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 272    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 304    CG   CD   CE   NZ                                   
REMARK 470     HIS A 309    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 317    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 318    CG   CD1  CD2                                       
REMARK 470     LYS A 320    CG   CD   CE   NZ                                   
REMARK 470     ARG A 321    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 322    CG1  CG2  CD1                                       
REMARK 470     GLN A 323    CG   CD   OE1  NE2                                  
REMARK 470     ILE A 324    CG1  CG2  CD1                                       
REMARK 470     ASP A 325    CG   OD1  OD2                                       
REMARK 470     SER A 326    OG                                                  
REMARK 470     GLU A 333    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 335    CG   CD   CE   NZ                                   
REMARK 470     GLU A 336    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 340    CG   CD   CE   NZ                                   
REMARK 470     ASP A 344    CG   OD1  OD2                                       
REMARK 470     GLU A 372    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 495    CG   OD1  OD2                                       
REMARK 470     ASN A 496    CG   OD1  ND2                                       
REMARK 470     SER A 538    OG                                                  
REMARK 470     GLU A 539    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 578    CG   CD   CE   NZ                                   
REMARK 470     ASP A 701    CG   OD1  OD2                                       
REMARK 470     ASN A 703    CG   OD1  ND2                                       
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   OE2  GLU A   269     OG   SER A   312     4455     2.19            
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    ASN A 586       77.48   -110.00                                   
REMARK 500    LEU A 725     -127.19   -117.79                                   
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 802  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 686   NE2                                                    
REMARK 620 2 HIS A 690   NE2  83.4                                              
REMARK 620 3 GLU A 735   OE1  91.2 105.2                                        
REMARK 620 4 30P A 801   O5   91.7  92.0 162.8                                  
REMARK 620 5 30P A 801   O3   93.5 169.6  84.8  78.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 30P A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 802                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JKY   RELATED DB: PDB                                   
REMARK 900 THE FULL-LENGTH PROTEIN IN A I4132 SPACEGROUP                        
REMARK 900 RELATED ID: 1J7N   RELATED DB: PDB                                   
REMARK 900 THE FULL-LENGTH PROTEIN WITH BOUND ZINC IN A P21 SPACEGROUP          
REMARK 900 RELATED ID: 1PWP   RELATED DB: PDB                                   
REMARK 900 THE FULL-LENGTH PROTEIN COMPLEXED WITH SMALL MOLECULE INHIBITOR NSC  
REMARK 900 12155 IN A P21 SPACEGROUP                                            
REMARK 900 RELATED ID: 1PWQ   RELATED DB: PDB                                   
REMARK 900 THE FULL-LENGTH PROTEIN COMPLEXED WITH A METAL-CHELATING PEPTIDYL    
REMARK 900 SMALL MOLECULE INHIBITOR IN A P21 SPACEGROUP                         
REMARK 900 RELATED ID: 1PWU   RELATED DB: PDB                                   
REMARK 900 THE FULL-LENGTH PROTEIN COMPLEXED WITH GM6001 IN A P21 SPACEGROUP    
REMARK 900 RELATED ID: 1PWV   RELATED DB: PDB                                   
REMARK 900 THE FULL-LENGTH PROTEIN COMPLEXED WITH AN OPTIMIZED PEPTIDE          
REMARK 900 SUBSTRATE IN A P21 SPACEGROUP                                        
REMARK 900 RELATED ID: 1PWW   RELATED DB: PDB                                   
REMARK 900 THE FULL-LENGTH INACTIVE MUTANT PROTEIN COMPLEXED WITH AN OPTIMIZED  
REMARK 900 PEPTIDE SUBSTRATE AND ZINC IN A P21 SPACEGROUP.                      
REMARK 900 RELATED ID: 1ZXV   RELATED DB: PDB                                   
REMARK 900 THE FULL-LENGTH PROTEIN COMPLEXED WITH A SMALL MOLECULE INHIBITOR    
REMARK 900 IN A P21 SPACEGROUP                                                  
REMARK 900 RELATED ID: 1YQY   RELATED DB: PDB                                   
REMARK 900 THE N-TERMINALLY TRUNCATED PROTEIN COMPLEXED WITH A SMALL MOLECULE   
REMARK 900 INHIBITOR IN A P212121 SPACEGROUP                                    
REMARK 900 RELATED ID: 4PKQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4PKR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4PKS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4PKT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4PKV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4PKW   RELATED DB: PDB                                   
DBREF  4PKU A  265   776  UNP    P15917   LEF_BACAN      298    809             
SEQADV 4PKU SER A  262  UNP  P15917              EXPRESSION TAG                 
SEQADV 4PKU ASN A  263  UNP  P15917              EXPRESSION TAG                 
SEQADV 4PKU ALA A  264  UNP  P15917              EXPRESSION TAG                 
SEQADV 4PKU SER A  266  UNP  P15917    ALA   299 ENGINEERED MUTATION            
SEQADV 4PKU LEU A  777  UNP  P15917              EXPRESSION TAG                 
SEQADV 4PKU VAL A  778  UNP  P15917              EXPRESSION TAG                 
SEQADV 4PKU PRO A  779  UNP  P15917              EXPRESSION TAG                 
SEQADV 4PKU ARG A  780  UNP  P15917              EXPRESSION TAG                 
SEQRES   1 A  519  SER ASN ALA LEU SER ARG TYR GLU LYS TRP GLU LYS ILE          
SEQRES   2 A  519  LYS GLN HIS TYR GLN HIS TRP SER ASP SER LEU SER GLU          
SEQRES   3 A  519  GLU GLY ARG GLY LEU LEU LYS LYS LEU GLN ILE PRO ILE          
SEQRES   4 A  519  GLU PRO LYS LYS ASP ASP ILE ILE HIS SER LEU SER GLN          
SEQRES   5 A  519  GLU GLU LYS GLU LEU LEU LYS ARG ILE GLN ILE ASP SER          
SEQRES   6 A  519  SER ASP PHE LEU SER THR GLU GLU LYS GLU PHE LEU LYS          
SEQRES   7 A  519  LYS LEU GLN ILE ASP ILE ARG ASP SER LEU SER GLU GLU          
SEQRES   8 A  519  GLU LYS GLU LEU LEU ASN ARG ILE GLN VAL ASP SER SER          
SEQRES   9 A  519  ASN PRO LEU SER GLU LYS GLU LYS GLU PHE LEU LYS LYS          
SEQRES  10 A  519  LEU LYS LEU ASP ILE GLN PRO TYR ASP ILE ASN GLN ARG          
SEQRES  11 A  519  LEU GLN ASP THR GLY GLY LEU ILE ASP SER PRO SER ILE          
SEQRES  12 A  519  ASN LEU ASP VAL ARG LYS GLN TYR LYS ARG ASP ILE GLN          
SEQRES  13 A  519  ASN ILE ASP ALA LEU LEU HIS GLN SER ILE GLY SER THR          
SEQRES  14 A  519  LEU TYR ASN LYS ILE TYR LEU TYR GLU ASN MET ASN ILE          
SEQRES  15 A  519  ASN ASN LEU THR ALA THR LEU GLY ALA ASP LEU VAL ASP          
SEQRES  16 A  519  SER THR ASP ASN THR LYS ILE ASN ARG GLY ILE PHE ASN          
SEQRES  17 A  519  GLU PHE LYS LYS ASN PHE LYS TYR SER ILE SER SER ASN          
SEQRES  18 A  519  TYR MET ILE VAL ASP ILE ASN GLU ARG PRO ALA LEU ASP          
SEQRES  19 A  519  ASN GLU ARG LEU LYS TRP ARG ILE GLN LEU SER PRO ASP          
SEQRES  20 A  519  THR ARG ALA GLY TYR LEU GLU ASN GLY LYS LEU ILE LEU          
SEQRES  21 A  519  GLN ARG ASN ILE GLY LEU GLU ILE LYS ASP VAL GLN ILE          
SEQRES  22 A  519  ILE LYS GLN SER GLU LYS GLU TYR ILE ARG ILE ASP ALA          
SEQRES  23 A  519  LYS VAL VAL PRO LYS SER LYS ILE ASP THR LYS ILE GLN          
SEQRES  24 A  519  GLU ALA GLN LEU ASN ILE ASN GLN GLU TRP ASN LYS ALA          
SEQRES  25 A  519  LEU GLY LEU PRO LYS TYR THR LYS LEU ILE THR PHE ASN          
SEQRES  26 A  519  VAL HIS ASN ARG TYR ALA SER ASN ILE VAL GLU SER ALA          
SEQRES  27 A  519  TYR LEU ILE LEU ASN GLU TRP LYS ASN ASN ILE GLN SER          
SEQRES  28 A  519  ASP LEU ILE LYS LYS VAL THR ASN TYR LEU VAL ASP GLY          
SEQRES  29 A  519  ASN GLY ARG PHE VAL PHE THR ASP ILE THR LEU PRO ASN          
SEQRES  30 A  519  ILE ALA GLU GLN TYR THR HIS GLN ASP GLU ILE TYR GLU          
SEQRES  31 A  519  GLN VAL HIS SER LYS GLY LEU TYR VAL PRO GLU SER ARG          
SEQRES  32 A  519  SER ILE LEU LEU HIS GLY PRO SER LYS GLY VAL GLU LEU          
SEQRES  33 A  519  ARG ASN ASP SER GLU GLY PHE ILE HIS GLU PHE GLY HIS          
SEQRES  34 A  519  ALA VAL ASP ASP TYR ALA GLY TYR LEU LEU ASP LYS ASN          
SEQRES  35 A  519  GLN SER ASP LEU VAL THR ASN SER LYS LYS PHE ILE ASP          
SEQRES  36 A  519  ILE PHE LYS GLU GLU GLY SER ASN LEU THR SER TYR GLY          
SEQRES  37 A  519  ARG THR ASN GLU ALA GLU PHE PHE ALA GLU ALA PHE ARG          
SEQRES  38 A  519  LEU MET HIS SER THR ASP HIS ALA GLU ARG LEU LYS VAL          
SEQRES  39 A  519  GLN LYS ASN ALA PRO LYS THR PHE GLN PHE ILE ASN ASP          
SEQRES  40 A  519  GLN ILE LYS PHE ILE ILE ASN SER LEU VAL PRO ARG              
HET    30P  A 801      26                                                       
HET     ZN  A 802       1                                                       
HETNAM     30P N~2~-(3-AMINOBENZYL)-N~2~-[(4-FLUORO-3-METHYLPHENYL)             
HETNAM   2 30P  SULFONYL]-N-HYDROXY-D-ALANINAMIDE                               
HETNAM      ZN ZINC ION                                                         
FORMUL   2  30P    C17 H20 F N3 O4 S                                            
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4  HOH   *81(H2 O)                                                     
HELIX    1 AA1 SER A  266  TYR A  278  1                                  13    
HELIX    2 AA2 TYR A  278  SER A  284  1                                   7    
HELIX    3 AA3 SER A  286  ILE A  298  1                                  13    
HELIX    4 AA4 LYS A  303  LEU A  311  1                                   9    
HELIX    5 AA5 SER A  312  ILE A  322  1                                  11    
HELIX    6 AA6 GLN A  323  SER A  327  5                                   5    
HELIX    7 AA7 SER A  331  ILE A  343  1                                  13    
HELIX    8 AA8 SER A  369  ILE A  383  1                                  15    
HELIX    9 AA9 ASP A  387  GLY A  396  1                                  10    
HELIX   10 AB1 ASN A  405  LEU A  423  1                                  19    
HELIX   11 AB2 ASN A  442  LEU A  446  5                                   5    
HELIX   12 AB3 THR A  447  ALA A  452  1                                   6    
HELIX   13 AB4 ASN A  464  ASN A  474  1                                  11    
HELIX   14 AB5 PRO A  551  GLY A  575  1                                  25    
HELIX   15 AB6 TYR A  591  ILE A  610  1                                  20    
HELIX   16 AB7 GLN A  611  GLY A  625  1                                  15    
HELIX   17 AB8 THR A  635  ASN A  638  5                                   4    
HELIX   18 AB9 ILE A  639  THR A  644  1                                   6    
HELIX   19 AC1 GLU A  648  GLN A  652  5                                   5    
HELIX   20 AC2 ASN A  679  ASP A  701  1                                  23    
HELIX   21 AC3 LEU A  707  ASN A  710  5                                   4    
HELIX   22 AC4 SER A  711  GLY A  722  1                                  12    
HELIX   23 AC5 SER A  727  THR A  731  5                                   5    
HELIX   24 AC6 ASN A  732  HIS A  745  1                                  14    
HELIX   25 AC7 ASP A  748  ALA A  759  1                                  12    
HELIX   26 AC8 ALA A  759  SER A  776  1                                  18    
SHEET    1 AA1 5 TYR A 436  MET A 441  0                                        
SHEET    2 AA1 5 LEU A 499  GLN A 504 -1  O  ILE A 503   N  LEU A 437           
SHEET    3 AA1 5 GLU A 541  VAL A 550  1  O  ILE A 543   N  LYS A 500           
SHEET    4 AA1 5 ILE A 525  LYS A 536 -1  N  ILE A 535   O  TYR A 542           
SHEET    5 AA1 5 TYR A 477  SER A 480 -1  N  SER A 478   O  LEU A 527           
SHEET    1 AA2 3 ILE A 485  ASP A 487  0                                        
SHEET    2 AA2 3 LYS A 518  LEU A 521 -1  O  LEU A 519   N  VAL A 486           
SHEET    3 AA2 3 ALA A 511  LEU A 514 -1  N  LEU A 514   O  LYS A 518           
SHEET    1 AA3 4 ILE A 583  ASN A 586  0                                        
SHEET    2 AA3 4 PHE A 629  THR A 632  1  O  PHE A 629   N  THR A 584           
SHEET    3 AA3 4 SER A 665  HIS A 669  1  O  ILE A 666   N  VAL A 630           
SHEET    4 AA3 4 GLY A 657  VAL A 660 -1  N  LEU A 658   O  LEU A 667           
LINK         NE2 HIS A 686                ZN    ZN A 802     1555   1555  2.48  
LINK         NE2 HIS A 690                ZN    ZN A 802     1555   1555  2.47  
LINK         OE1 GLU A 735                ZN    ZN A 802     1555   1555  2.44  
LINK         O5  30P A 801                ZN    ZN A 802     1555   1555  2.08  
LINK         O3  30P A 801                ZN    ZN A 802     1555   1555  2.08  
SITE     1 AC1 17 ASP A 328  HIS A 654  SER A 655  LYS A 656                    
SITE     2 AC1 17 GLY A 657  VAL A 675  LEU A 677  HIS A 686                    
SITE     3 AC1 17 GLU A 687  HIS A 690  TYR A 728  GLU A 735                    
SITE     4 AC1 17 GLU A 739  ARG A 742   ZN A 802  HOH A 924                    
SITE     5 AC1 17 HOH A 968                                                     
SITE     1 AC2  5 HIS A 686  HIS A 690  GLU A 735  30P A 801                    
SITE     2 AC2  5 HOH A 968                                                     
CRYST1   61.337   67.895  143.358  90.00  90.00  90.00 P 21 21 21    4          
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      0.016303  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014729  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006976        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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