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Database: PDB
Entry: 2OVZ
LinkDB: 2OVZ
Original site: 2OVZ 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           15-FEB-07   2OVZ              
TITLE     MMP-9 ACTIVE SITE MUTANT WITH PHOSPHINATE INHIBITOR                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MATRIX METALLOPROTEINASE-9 (EC 3.4.24.35) (MMP-9) (92 KDA  
COMPND   3 TYPE IV COLLAGENASE) (92 KDA GELATINASE) (GELATINASE B) (GELB);      
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: CATALYTIC DOMAIN RESIDUES: 110-215, 391-443;               
COMPND   6 EC: 3.4.24.35;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MMP9, CLG4B;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    MATRIX METALLOPROTEINASE, S1-PRIME POCKET, HYDROLASE-HYDROLASE        
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.TOCHOWICZ,W.BODE,K.MASKOS,P.GOETTIG                                 
REVDAT   5   16-AUG-17 2OVZ    1       SOURCE REMARK                            
REVDAT   4   13-JUL-11 2OVZ    1       VERSN                                    
REVDAT   3   24-FEB-09 2OVZ    1       VERSN                                    
REVDAT   2   14-AUG-07 2OVZ    1       JRNL                                     
REVDAT   1   19-JUN-07 2OVZ    0                                                
JRNL        AUTH   A.TOCHOWICZ,K.MASKOS,R.HUBER,R.OLTENFREITER,V.DIVE,          
JRNL        AUTH 2 A.YIOTAKIS,M.ZANDA,W.BODE,P.GOETTIG                          
JRNL        TITL   CRYSTAL STRUCTURES OF MMP-9 COMPLEXES WITH FIVE INHIBITORS:  
JRNL        TITL 2 CONTRIBUTION OF THE FLEXIBLE ARG424 SIDE-CHAIN TO            
JRNL        TITL 3 SELECTIVITY.                                                 
JRNL        REF    J.MOL.BIOL.                   V. 371   989 2007              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   17599356                                                     
JRNL        DOI    10.1016/J.JMB.2007.05.068                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1445661.330                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 26125                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1264                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4325                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2170                       
REMARK   3   BIN FREE R VALUE                    : 0.2650                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 234                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.017                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2510                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 98                                      
REMARK   3   SOLVENT ATOMS            : 181                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.43000                                              
REMARK   3    B22 (A**2) : 3.43000                                              
REMARK   3    B33 (A**2) : -6.87000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.07                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.28                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.15                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.100                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.770                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.770 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.420 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.450 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.460 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 59.02                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : INH_NEW.PAR                                    
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : INH_NEW.TOP                                    
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2OVZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000041652.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUL-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MPG/DESY, HAMBURG                  
REMARK 200  BEAMLINE                       : BW6                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0500                             
REMARK 200  MONOCHROMATOR                  : SI 111 DOUBLE CHANNEL              
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28175                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.04200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1GKD                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.0 M NACL, 0.1 M TRIS, VAPOR            
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K, PH 8.0, PH 8.00          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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      129.94500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       27.92500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       27.92500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       64.97250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       27.92500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       27.92500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      194.91750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       27.92500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       27.92500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       64.97250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       27.92500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       27.92500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      194.91750            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      129.94500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11830 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -463.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000       55.85000            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000       55.85000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      129.94500            
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     PHE B   110                                                      
REMARK 465     GLU B   111                                                      
REMARK 465     GLY B   112                                                      
REMARK 465     ASP B   113                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     GLU A   111                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ASP A  113   CB   CG   OD1  OD2                                  
REMARK 480     ARG A  162   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG A  424   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     LYS A  433   CG   CD   CE   NZ                                   
REMARK 480     LYS B  115   CD   CE   NZ                                        
REMARK 480     ARG B  162   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS B  184   CG   CD   CE   NZ                                   
REMARK 480     LEU B  187   CD1  CD2                                            
REMARK 480     ARG B  424   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS B  433   CG   CD   CE   NZ                                   
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    GLU A 111       35.40    -86.87                                   
REMARK 500    ALA A 173     -137.47     50.49                                   
REMARK 500    ASP A 185     -162.11     60.37                                   
REMARK 500    SER A 211     -157.64   -148.99                                   
REMARK 500    ALA B 173     -124.26     48.86                                   
REMARK 500    ASP B 185     -162.87     61.25                                   
REMARK 500    ALA B 189      171.99    175.43                                   
REMARK 500    SER B 211     -157.53   -147.61                                   
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 444  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 401   NE2                                                    
REMARK 620 2 HIS A 405   NE2 102.0                                              
REMARK 620 3 HIS A 411   NE2 116.2 103.9                                        
REMARK 620 4 5MR A 501   OAD 115.1 132.4  85.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 445  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 175   NE2                                                    
REMARK 620 2 ASP A 177   OD2 110.7                                              
REMARK 620 3 HIS A 203   ND1 116.3  97.0                                        
REMARK 620 4 HIS A 190   NE2 121.1  99.6 108.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 446  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 185   O                                                      
REMARK 620 2 ASP A 182   OD1  80.1                                              
REMARK 620 3 LEU A 187   O    99.2  89.0                                        
REMARK 620 4 ASP A 205   OD1 169.3  98.1  91.3                                  
REMARK 620 5 GLY A 183   O    87.0  92.1 173.8  82.5                            
REMARK 620 6 GLU A 208   OE1  81.6 161.4  90.6 100.5  90.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 447  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 502   O                                                      
REMARK 620 2 ASP A 165   O    85.5                                              
REMARK 620 3 GLY A 197   O    83.8 168.3                                        
REMARK 620 4 GLN A 199   O    80.1  99.7  83.0                                  
REMARK 620 5 ASP A 201   OD1 179.6  94.1  96.6  99.9                            
REMARK 620 6 HOH A 540   O    88.1  98.5  76.5 157.4  91.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 448  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 206   OD1                                                    
REMARK 620 2 GLU A 208   O   127.1                                              
REMARK 620 3 ASP A 131   OD2 105.7  82.3                                        
REMARK 620 4 HOH A 503   O   121.7 111.2  81.6                                  
REMARK 620 5 ASP A 206   O    75.4  96.7 178.9  98.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 449  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 213   O                                                      
REMARK 620 2 LEU A 212   O    72.9                                              
REMARK 620 3 LYS A 214   O    75.0 100.3                                        
REMARK 620 4 SER A 211   OG  138.1  77.4 140.1                                  
REMARK 620 5 HOH A 514   O    75.7 107.5 130.8  86.1                            
REMARK 620 6 HOH A 515   O   155.3 131.6  94.9  62.3  95.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 450  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 552   O                                                      
REMARK 620 2 SER A 149   O    92.7                                              
REMARK 620 3 HOH A 555   O    95.4  89.8                                        
REMARK 620 4 HOH A 548   O    87.3 173.9  96.3                                  
REMARK 620 5 HOH A 539   O   171.6  94.1  89.6  85.4                            
REMARK 620 6 THR A 152   O    92.1  79.1 166.9  94.8  84.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 444  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 5MR B 502   OAE                                                    
REMARK 620 2 HIS B 411   NE2  86.9                                              
REMARK 620 3 HIS B 405   NE2 120.1 107.1                                        
REMARK 620 4 HIS B 401   NE2 127.2 114.7  99.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 445  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 203   ND1                                                    
REMARK 620 2 HIS B 190   NE2 109.6                                              
REMARK 620 3 ASP B 177   OD2  94.9 117.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 446  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 185   O                                                      
REMARK 620 2 LEU B 187   O    97.8                                              
REMARK 620 3 GLU B 208   OE2  78.2  92.3                                        
REMARK 620 4 ASP B 182   OD2  88.1  88.0 166.2                                  
REMARK 620 5 GLY B 183   O    84.6 177.4  89.2  91.1                            
REMARK 620 6 ASP B 205   OD1 167.9  94.1 100.2  93.6  83.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 447  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 165   O                                                      
REMARK 620 2 HOH B 584   O    91.5                                              
REMARK 620 3 GLN B 199   O   102.2  81.3                                        
REMARK 620 4 HOH B 524   O   104.9  88.7 151.3                                  
REMARK 620 5 ASP B 201   OD1  94.7 173.7  98.7  88.4                            
REMARK 620 6 GLY B 197   O   168.1  78.1  82.2  69.4  95.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 448  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 503   O                                                      
REMARK 620 2 HOH B 564   O    51.6                                              
REMARK 620 3 GLU B 208   O   127.5  77.2                                        
REMARK 620 4 ASP B 131   OD2  86.4  95.7  88.3                                  
REMARK 620 5 ASP B 206   OD1 109.9 153.9 122.3 101.6                            
REMARK 620 6 ASP B 206   O    91.5  84.8  94.8 176.9  76.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 449  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 532   O                                                      
REMARK 620 2 GLY B 213   O    71.9                                              
REMARK 620 3 LYS B 214   O   121.4  70.9                                        
REMARK 620 4 LEU B 212   O   104.3  69.2 102.7                                  
REMARK 620 5 HOH B 525   O    90.5 148.9  99.1 141.5                            
REMARK 620 6 SER B 211   OG   81.4 134.8 152.8  83.6  63.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 450  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 542   O                                                      
REMARK 620 2 THR B 152   O    84.9                                              
REMARK 620 3 SER B 149   O   101.4  81.4                                        
REMARK 620 4 HOH B 522   O   163.0  85.6  91.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 444                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 445                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 444                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 445                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 446                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 447                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 448                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 449                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 450                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 446                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 447                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 448                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 449                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 450                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 451                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 452                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 451                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 453                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5MR A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5MR B 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1GKC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1GKD   RELATED DB: PDB                                   
DBREF  2OVZ A  110   215  UNP    P14780   MMP9_HUMAN     110    215             
DBREF  2OVZ A  391   443  UNP    P14780   MMP9_HUMAN     391    443             
DBREF  2OVZ B  110   215  UNP    P14780   MMP9_HUMAN     110    215             
DBREF  2OVZ B  391   443  UNP    P14780   MMP9_HUMAN     391    443             
SEQADV 2OVZ GLN A  402  UNP  P14780    GLU   402 ENGINEERED                     
SEQADV 2OVZ GLN B  402  UNP  P14780    GLU   402 ENGINEERED                     
SEQRES   1 A  159  PHE GLU GLY ASP LEU LYS TRP HIS HIS HIS ASN ILE THR          
SEQRES   2 A  159  TYR TRP ILE GLN ASN TYR SER GLU ASP LEU PRO ARG ALA          
SEQRES   3 A  159  VAL ILE ASP ASP ALA PHE ALA ARG ALA PHE ALA LEU TRP          
SEQRES   4 A  159  SER ALA VAL THR PRO LEU THR PHE THR ARG VAL TYR SER          
SEQRES   5 A  159  ARG ASP ALA ASP ILE VAL ILE GLN PHE GLY VAL ALA GLU          
SEQRES   6 A  159  HIS GLY ASP GLY TYR PRO PHE ASP GLY LYS ASP GLY LEU          
SEQRES   7 A  159  LEU ALA HIS ALA PHE PRO PRO GLY PRO GLY ILE GLN GLY          
SEQRES   8 A  159  ASP ALA HIS PHE ASP ASP ASP GLU LEU TRP SER LEU GLY          
SEQRES   9 A  159  LYS GLY GLN GLY TYR SER LEU PHE LEU VAL ALA ALA HIS          
SEQRES  10 A  159  GLN PHE GLY HIS ALA LEU GLY LEU ASP HIS SER SER VAL          
SEQRES  11 A  159  PRO GLU ALA LEU MET TYR PRO MET TYR ARG PHE THR GLU          
SEQRES  12 A  159  GLY PRO PRO LEU HIS LYS ASP ASP VAL ASN GLY ILE ARG          
SEQRES  13 A  159  HIS LEU TYR                                                  
SEQRES   1 B  159  PHE GLU GLY ASP LEU LYS TRP HIS HIS HIS ASN ILE THR          
SEQRES   2 B  159  TYR TRP ILE GLN ASN TYR SER GLU ASP LEU PRO ARG ALA          
SEQRES   3 B  159  VAL ILE ASP ASP ALA PHE ALA ARG ALA PHE ALA LEU TRP          
SEQRES   4 B  159  SER ALA VAL THR PRO LEU THR PHE THR ARG VAL TYR SER          
SEQRES   5 B  159  ARG ASP ALA ASP ILE VAL ILE GLN PHE GLY VAL ALA GLU          
SEQRES   6 B  159  HIS GLY ASP GLY TYR PRO PHE ASP GLY LYS ASP GLY LEU          
SEQRES   7 B  159  LEU ALA HIS ALA PHE PRO PRO GLY PRO GLY ILE GLN GLY          
SEQRES   8 B  159  ASP ALA HIS PHE ASP ASP ASP GLU LEU TRP SER LEU GLY          
SEQRES   9 B  159  LYS GLY GLN GLY TYR SER LEU PHE LEU VAL ALA ALA HIS          
SEQRES  10 B  159  GLN PHE GLY HIS ALA LEU GLY LEU ASP HIS SER SER VAL          
SEQRES  11 B  159  PRO GLU ALA LEU MET TYR PRO MET TYR ARG PHE THR GLU          
SEQRES  12 B  159  GLY PRO PRO LEU HIS LYS ASP ASP VAL ASN GLY ILE ARG          
SEQRES  13 B  159  HIS LEU TYR                                                  
HET     ZN  A 444       1                                                       
HET     ZN  A 445       1                                                       
HET     CA  A 446       1                                                       
HET     CA  A 447       1                                                       
HET     CA  A 448       1                                                       
HET     CA  A 449       1                                                       
HET     CA  A 450       1                                                       
HET     CL  A 451       1                                                       
HET     CL  A 452       1                                                       
HET     CL  A 453       1                                                       
HET    5MR  A 501      40                                                       
HET     ZN  B 444       1                                                       
HET     ZN  B 445       1                                                       
HET     CA  B 446       1                                                       
HET     CA  B 447       1                                                       
HET     CA  B 448       1                                                       
HET     CA  B 449       1                                                       
HET     CA  B 450       1                                                       
HET     CL  B 451       1                                                       
HET    5MR  B 502      40                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     5MR NALPHA-{(2S)-3-[(S)-HYDROXY(PHENYL)PHOSPHORYL]-2-[(3-            
HETNAM   2 5MR  PHENYLISOXAZOL-5-YL)METHYL]PROPANOYL}-L-                        
HETNAM   3 5MR  TRYPTOPHANAMIDE                                                 
FORMUL   3   ZN    4(ZN 2+)                                                     
FORMUL   5   CA    10(CA 2+)                                                    
FORMUL  10   CL    4(CL 1-)                                                     
FORMUL  13  5MR    2(C30 H29 N4 O5 P)                                           
FORMUL  23  HOH   *181(H2 O)                                                    
HELIX    1   1 PRO A  133  ALA A  150  1                                  18    
HELIX    2   2 LEU A  395  LEU A  407  1                                  13    
HELIX    3   3 HIS A  432  TYR A  443  1                                  12    
HELIX    4   4 PRO B  133  ALA B  150  1                                  18    
HELIX    5   5 LEU B  395  LEU B  407  1                                  13    
HELIX    6   6 HIS B  432  TYR B  443  1                                  12    
SHEET    1   A 5 THR A 155  ARG A 158  0                                        
SHEET    2   A 5 ASN A 120  ILE A 125  1  N  ILE A 121   O  THR A 157           
SHEET    3   A 5 ILE A 166  GLY A 171  1  O  ILE A 168   N  TRP A 124           
SHEET    4   A 5 ALA A 202  ASP A 205  1  O  PHE A 204   N  GLY A 171           
SHEET    5   A 5 ALA A 189  ALA A 191 -1  N  HIS A 190   O  HIS A 203           
SHEET    1   B 2 TRP A 210  SER A 211  0                                        
SHEET    2   B 2 TYR A 393  SER A 394  1  O  TYR A 393   N  SER A 211           
SHEET    1   C 5 THR B 155  ARG B 158  0                                        
SHEET    2   C 5 ASN B 120  ILE B 125  1  N  ILE B 121   O  THR B 157           
SHEET    3   C 5 ILE B 166  GLY B 171  1  O  ILE B 168   N  TRP B 124           
SHEET    4   C 5 ALA B 202  ASP B 205  1  O  PHE B 204   N  GLN B 169           
SHEET    5   C 5 ALA B 189  ALA B 191 -1  N  HIS B 190   O  HIS B 203           
SHEET    1   D 2 TRP B 210  SER B 211  0                                        
SHEET    2   D 2 TYR B 393  SER B 394  1  O  TYR B 393   N  SER B 211           
LINK        ZN    ZN A 444                 NE2 HIS A 401     1555   1555  2.08  
LINK        ZN    ZN A 444                 NE2 HIS A 405     1555   1555  2.04  
LINK        ZN    ZN A 444                 NE2 HIS A 411     1555   1555  2.09  
LINK        ZN    ZN A 444                 OAD 5MR A 501     1555   1555  1.79  
LINK        ZN    ZN A 445                 NE2 HIS A 175     1555   1555  2.06  
LINK        ZN    ZN A 445                 OD2 ASP A 177     1555   1555  1.98  
LINK        ZN    ZN A 445                 ND1 HIS A 203     1555   1555  2.05  
LINK        ZN    ZN A 445                 NE2 HIS A 190     1555   1555  2.17  
LINK        CA    CA A 446                 O   ASP A 185     1555   1555  2.24  
LINK        CA    CA A 446                 OD1 ASP A 182     1555   1555  2.43  
LINK        CA    CA A 446                 O   LEU A 187     1555   1555  2.35  
LINK        CA    CA A 446                 OD1 ASP A 205     1555   1555  2.34  
LINK        CA    CA A 446                 O   GLY A 183     1555   1555  2.18  
LINK        CA    CA A 446                 OE1 GLU A 208     1555   1555  2.11  
LINK        CA    CA A 447                 O   HOH A 502     1555   1555  2.57  
LINK        CA    CA A 447                 O   ASP A 165     1555   1555  2.34  
LINK        CA    CA A 447                 O   GLY A 197     1555   1555  2.64  
LINK        CA    CA A 447                 O   GLN A 199     1555   1555  2.40  
LINK        CA    CA A 447                 OD1 ASP A 201     1555   1555  2.51  
LINK        CA    CA A 447                 O   HOH A 540     1555   1555  2.30  
LINK        CA    CA A 448                 OD1 ASP A 206     1555   1555  2.55  
LINK        CA    CA A 448                 O   GLU A 208     1555   1555  2.27  
LINK        CA    CA A 448                 OD2 ASP A 131     1555   1555  2.31  
LINK        CA    CA A 448                 O   HOH A 503     1555   1555  2.31  
LINK        CA    CA A 448                 O   ASP A 206     1555   1555  2.24  
LINK        CA    CA A 449                 O   GLY A 213     1555   1555  2.72  
LINK        CA    CA A 449                 O   LEU A 212     1555   1555  2.28  
LINK        CA    CA A 449                 O   LYS A 214     1555   1555  2.45  
LINK        CA    CA A 449                 OG  SER A 211     1555   1555  3.23  
LINK        CA    CA A 449                 O   HOH A 514     1555   1555  2.18  
LINK        CA    CA A 449                 O   HOH A 515     1555   1555  2.46  
LINK        CA    CA A 450                 O   HOH A 552     1555   1555  2.40  
LINK        CA    CA A 450                 O   SER A 149     1555   1555  2.29  
LINK        CA    CA A 450                 O   HOH A 555     1555   1555  2.36  
LINK        CA    CA A 450                 O   HOH A 548     1555   1555  2.44  
LINK        CA    CA A 450                 O   HOH A 539     1555   1555  2.62  
LINK        CA    CA A 450                 O   THR A 152     1555   1555  2.27  
LINK        ZN    ZN B 444                 OAE 5MR B 502     1555   1555  1.81  
LINK        ZN    ZN B 444                 NE2 HIS B 411     1555   1555  2.05  
LINK        ZN    ZN B 444                 NE2 HIS B 405     1555   1555  2.07  
LINK        ZN    ZN B 444                 NE2 HIS B 401     1555   1555  2.04  
LINK        ZN    ZN B 445                 ND1 HIS B 203     1555   1555  2.07  
LINK        ZN    ZN B 445                 NE2 HIS B 190     1555   1555  2.03  
LINK        ZN    ZN B 445                 OD2 ASP B 177     1555   1555  2.02  
LINK        CA    CA B 446                 O   ASP B 185     1555   1555  2.31  
LINK        CA    CA B 446                 O   LEU B 187     1555   1555  2.25  
LINK        CA    CA B 446                 OE2 GLU B 208     1555   1555  2.13  
LINK        CA    CA B 446                 OD2 ASP B 182     1555   1555  2.34  
LINK        CA    CA B 446                 O   GLY B 183     1555   1555  2.19  
LINK        CA    CA B 446                 OD1 ASP B 205     1555   1555  2.37  
LINK        CA    CA B 447                 O   ASP B 165     1555   1555  2.28  
LINK        CA    CA B 447                 O   HOH B 584     1555   1555  2.49  
LINK        CA    CA B 447                 O   GLN B 199     1555   1555  2.30  
LINK        CA    CA B 447                 O   HOH B 524     1555   1555  2.60  
LINK        CA    CA B 447                 OD1 ASP B 201     1555   1555  2.45  
LINK        CA    CA B 447                 O   GLY B 197     1555   1555  2.84  
LINK        CA    CA B 448                 O   HOH B 503     1555   1555  2.56  
LINK        CA    CA B 448                 O   HOH B 564     1555   1555  3.09  
LINK        CA    CA B 448                 O   GLU B 208     1555   1555  2.28  
LINK        CA    CA B 448                 OD2 ASP B 131     1555   1555  2.29  
LINK        CA    CA B 448                 OD1 ASP B 206     1555   1555  2.44  
LINK        CA    CA B 448                 O   ASP B 206     1555   1555  2.43  
LINK        CA    CA B 449                 O   HOH B 532     1555   1555  2.33  
LINK        CA    CA B 449                 O   GLY B 213     1555   1555  3.01  
LINK        CA    CA B 449                 O   LYS B 214     1555   1555  2.39  
LINK        CA    CA B 449                 O   LEU B 212     1555   1555  2.24  
LINK        CA    CA B 449                 O   HOH B 525     1555   1555  2.50  
LINK        CA    CA B 449                 OG  SER B 211     1555   1555  3.04  
LINK        CA    CA B 450                 O   HOH B 542     1555   1555  2.50  
LINK        CA    CA B 450                 O   THR B 152     1555   1555  2.27  
LINK        CA    CA B 450                 O   SER B 149     1555   1555  2.25  
LINK        CA    CA B 450                 O   HOH B 522     1555   1555  2.30  
SITE     1 AC1  4 HIS A 401  HIS A 405  HIS A 411  5MR A 501                    
SITE     1 AC2  4 HIS A 175  ASP A 177  HIS A 190  HIS A 203                    
SITE     1 AC3  4 HIS B 401  HIS B 405  HIS B 411  5MR B 502                    
SITE     1 AC4  4 HIS B 175  ASP B 177  HIS B 190  HIS B 203                    
SITE     1 AC5  6 ASP A 182  GLY A 183  ASP A 185  LEU A 187                    
SITE     2 AC5  6 ASP A 205  GLU A 208                                          
SITE     1 AC6  6 ASP A 165  GLY A 197  GLN A 199  ASP A 201                    
SITE     2 AC6  6 HOH A 502  HOH A 540                                          
SITE     1 AC7  4 ASP A 131  ASP A 206  GLU A 208  HOH A 503                    
SITE     1 AC8  7 SER A 211  LEU A 212  GLY A 213  LYS A 214                    
SITE     2 AC8  7 GLY A 215  HOH A 514  HOH A 515                               
SITE     1 AC9  6 SER A 149  THR A 152  HOH A 539  HOH A 548                    
SITE     2 AC9  6 HOH A 552  HOH A 555                                          
SITE     1 BC1  6 ASP B 182  GLY B 183  ASP B 185  LEU B 187                    
SITE     2 BC1  6 ASP B 205  GLU B 208                                          
SITE     1 BC2  6 ASP B 165  GLY B 197  GLN B 199  ASP B 201                    
SITE     2 BC2  6 HOH B 524  HOH B 584                                          
SITE     1 BC3  5 ASP B 131  ASP B 206  GLU B 208  HOH B 503                    
SITE     2 BC3  5 HOH B 564                                                     
SITE     1 BC4  7 LEU A 212  SER B 211  LEU B 212  GLY B 213                    
SITE     2 BC4  7 LYS B 214  HOH B 525  HOH B 532                               
SITE     1 BC5  4 SER B 149  THR B 152  HOH B 522  HOH B 542                    
SITE     1 BC6  2 GLY A 213  SER A 394                                          
SITE     1 BC7  3 ARG A 143  PHE A 396  HOH B 531                               
SITE     1 BC8  2 GLY B 213  SER B 394                                          
SITE     1 BC9  4 ASN A 127  TYR A 128  HOH A 547  TYR B 128                    
SITE     1 CC1 18 PHE A 110  GLY A 186  LEU A 187  LEU A 188                    
SITE     2 CC1 18 ALA A 189  HIS A 190  VAL A 398  HIS A 401                    
SITE     3 CC1 18 GLN A 402  HIS A 405  HIS A 411  LEU A 418                    
SITE     4 CC1 18 TYR A 420  PRO A 421  MET A 422  TYR A 423                    
SITE     5 CC1 18  ZN A 444  HOH A 557                                          
SITE     1 CC2 19 MET A 422  GLY B 186  LEU B 187  LEU B 188                    
SITE     2 CC2 19 ALA B 189  HIS B 190  VAL B 398  HIS B 401                    
SITE     3 CC2 19 GLN B 402  HIS B 405  HIS B 411  LEU B 418                    
SITE     4 CC2 19 TYR B 420  PRO B 421  MET B 422  TYR B 423                    
SITE     5 CC2 19  ZN B 444  HOH B 562  HOH B 582                               
CRYST1   55.850   55.850  259.890  90.00  90.00  90.00 P 41 21 2    16          
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      0.017905  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017905  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003848        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system