GenomeNet

Database: PDB
Entry: 1ZP5
LinkDB: 1ZP5
Original site: 1ZP5 
HEADER    HYDROLASE                               16-MAY-05   1ZP5              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN MMP-8 AND A N-HYDROXYUREA    
TITLE    2 INHIBITOR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUTROPHIL COLLAGENASE;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN (80-242);                                 
COMPND   5 SYNONYM: MATRIX METALLOPROTEINASE-8, MMP-8, PMNL COLLAGENASE, PMNL-  
COMPND   6 CL;                                                                  
COMPND   7 EC: 3.4.24.34;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MMP8, CLG1;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PSVB30                                    
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.CAMPESTRE,M.AGAMENNONE,P.TORTORELLA,S.PREZIUSO,A.BIASONE,E.GAVUZZO, 
AUTHOR   2 G.POCHETTI,F.MAZZA,H.TSCHESCHE,C.GALLINA                             
REVDAT   4   24-JAN-18 1ZP5    1       JRNL                                     
REVDAT   3   11-OCT-17 1ZP5    1       REMARK                                   
REVDAT   2   24-FEB-09 1ZP5    1       VERSN                                    
REVDAT   1   06-DEC-05 1ZP5    0                                                
JRNL        AUTH   C.CAMPESTRE,M.AGAMENNONE,P.TORTORELLA,S.PREZIUSO,A.BIASONE,  
JRNL        AUTH 2 E.GAVUZZO,G.POCHETTI,F.MAZZA,O.HILLER,H.TSCHESCHE,           
JRNL        AUTH 3 V.CONSALVI,C.GALLINA                                         
JRNL        TITL   N-HYDROXYUREA AS ZINC BINDING GROUP IN MATRIX                
JRNL        TITL 2 METALLOPROTEINASE INHIBITION: MODE OF BINDING IN A COMPLEX   
JRNL        TITL 3 WITH MMP-8.                                                  
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  16    20 2006              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   16242329                                                     
JRNL        DOI    10.1016/J.BMCL.2005.09.057                                   
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.M.MURI,M.J.NIETO,R.D.SINDELAR,J.S.WILLIAMSON               
REMARK   1  TITL   HYDROXAMIC ACIDS AS PHARMACOLOGICAL AGENTS.                  
REMARK   1  REF    CURR.MED.CHEM.                V.   9  1631 2002              
REMARK   1  REFN                   ISSN 0929-8673                               
REMARK   1  PMID   12171558                                                     
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   F.GRAMS,M.CRIMMIN,L.HINNES,P.HUXLEY,M.PIEPER,H.TSCHESCHE,    
REMARK   1  AUTH 2 W.BODE                                                       
REMARK   1  TITL   STRUCTURE DETERMINATION AND ANALYSIS OF HUMAN NEUTROPHIL     
REMARK   1  TITL 2 COLLAGENASE COMPLEXED WITH A HYDROXAMATE INHIBITOR.          
REMARK   1  REF    BIOCHEMISTRY                  V.  34 14012 1995              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   7577999                                                      
REMARK   1  DOI    10.1021/BI00043A007                                          
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   P.J.HAJDUCK,G.SHEPPARD,D.G.NETTESHEIM,E.T.OLEJNICZAK,        
REMARK   1  AUTH 2 S.B.SHUKER,R.P.MEADOWS,D.H.STEINMAN,G.M.CARRERA,             
REMARK   1  AUTH 3 P.A.MARCOTTE,J.SEVERIN,K.WALTER,H.SMITH,E.GUBBINS,R.SIMMER,  
REMARK   1  AUTH 4 T.F.HOLZMAN,D.W.MORGAN,S.K.DAVIDSEN,J.B.SUMMERS,S.W.FESIK    
REMARK   1  TITL   DISCOVERY OF POTENT NON PEPTIDE INHIBITORS OF STROMELYSIN    
REMARK   1  TITL 2 USING SAR BY NMR.                                            
REMARK   1  REF    J.AM.CHEM.SOC.                V. 119  5818 1997              
REMARK   1  REFN                   ISSN 0002-7863                               
REMARK   1  DOI    10.1021/JA9702778                                            
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   M.R.MICHAELIDES,J.F.DELLARIA,J.GONG,J.H.HOLMS,J.J.BOUSKA,    
REMARK   1  AUTH 2 J.STACEY,C.K.WADA,H.R.HEYMAN,M.L.CURTIN,Y.GUO,               
REMARK   1  AUTH 3 C.L.GOODFELLOW,I.B.ELMORE,D.H.ALBERT,T.J.MAGOC,P.A.MARCOTTE, 
REMARK   1  AUTH 4 D.W.MORGAN,S.K.DAVIDSEN                                      
REMARK   1  TITL   BIARYL ETHER RETROHYDROXAMATES AS POTENT, LONG-LIVED, ORALLY 
REMARK   1  TITL 2 BIOAVAILABLE MMP INHIBITORS.                                 
REMARK   1  REF    BIOORG.MED.CHEM.LETT.         V.  11  1553 2001              
REMARK   1  REFN                   ISSN 0960-894X                               
REMARK   1  PMID   11412979                                                     
REMARK   1  DOI    10.1016/S0960-894X(01)00031-2                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 9738                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 974                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1283                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 27                                      
REMARK   3   SOLVENT ATOMS            : 125                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ZP5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000032978.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-MAY-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10932                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.480                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1I76                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 20.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, MES/NAOH, NA PHOSPHATE, PH      
REMARK 280  6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
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       16.19350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       33.66550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.33750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       33.66550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.19350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.33750            
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 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 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   OD1  ASN A   150     OG1  THR A   185     3555     2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    SER A 151   N   -  CA  -  C   ANGL. DEV. = -18.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 145     -131.11     40.32                                   
REMARK 500    HIS A 147       41.35   -143.19                                   
REMARK 500    ASN A 157     -167.43     59.62                                   
REMARK 500    THR A 185     -161.72   -108.20                                   
REMARK 500    GLU A 223       94.42    -42.80                                   
REMARK 500    SER A 225      -81.62    -50.89                                   
REMARK 500    TYR A 227      109.00    -51.63                                   
REMARK 500    LEU A 229      125.89    -34.32                                   
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                              CA A 996  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 137   O                                                      
REMARK 620 2 GLY A 171   O    92.8                                              
REMARK 620 3 GLY A 169   O   160.9 105.5                                        
REMARK 620 4 ASP A 173   OD1  89.2 103.5  91.6                                  
REMARK 620 5 HOH A1093   O   117.2 149.8  44.3  81.5                            
REMARK 620 6 HOH A1098   O    81.7 150.4  79.7 105.5  43.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 997  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A 159   O                                                      
REMARK 620 2 ASP A 154   OD1  88.4                                              
REMARK 620 3 GLY A 155   O   175.8  89.6                                        
REMARK 620 4 ASN A 157   O   102.0  88.0  81.7                                  
REMARK 620 5 ASP A 177   OD2  88.2  90.7  88.0 169.6                            
REMARK 620 6 GLU A 180   OE2  82.5 169.9  99.7  89.7  93.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 998  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 162   NE2                                                    
REMARK 620 2 ASP A 149   OD2 112.6                                              
REMARK 620 3 HIS A 175   ND1 114.8  91.2                                        
REMARK 620 4 HIS A 147   NE2 110.6 115.4 111.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 999  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 197   NE2                                                    
REMARK 620 2 2NI A1000   O3  110.0                                              
REMARK 620 3 HIS A 201   NE2 105.3 119.6                                        
REMARK 620 4 HIS A 207   NE2 104.1 114.5 101.9                                  
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 CA A 996                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 997                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 998                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 999                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2NI A 1000                
DBREF  1ZP5 A   80   242  UNP    P22894   MMP8_HUMAN     100    262             
SEQRES   1 A  163  MET LEU THR PRO GLY ASN PRO LYS TRP GLU ARG THR ASN          
SEQRES   2 A  163  LEU THR TYR ARG ILE ARG ASN TYR THR PRO GLN LEU SER          
SEQRES   3 A  163  GLU ALA GLU VAL GLU ARG ALA ILE LYS ASP ALA PHE GLU          
SEQRES   4 A  163  LEU TRP SER VAL ALA SER PRO LEU ILE PHE THR ARG ILE          
SEQRES   5 A  163  SER GLN GLY GLU ALA ASP ILE ASN ILE ALA PHE TYR GLN          
SEQRES   6 A  163  ARG ASP HIS GLY ASP ASN SER PRO PHE ASP GLY PRO ASN          
SEQRES   7 A  163  GLY ILE LEU ALA HIS ALA PHE GLN PRO GLY GLN GLY ILE          
SEQRES   8 A  163  GLY GLY ASP ALA HIS PHE ASP ALA GLU GLU THR TRP THR          
SEQRES   9 A  163  ASN THR SER ALA ASN TYR ASN LEU PHE LEU VAL ALA ALA          
SEQRES  10 A  163  HIS GLU PHE GLY HIS SER LEU GLY LEU ALA HIS SER SER          
SEQRES  11 A  163  ASP PRO GLY ALA LEU MET TYR PRO ASN TYR ALA PHE ARG          
SEQRES  12 A  163  GLU THR SER ASN TYR SER LEU PRO GLN ASP ASP ILE ASP          
SEQRES  13 A  163  GLY ILE GLN ALA ILE TYR GLY                                  
HET     CA  A 996       1                                                       
HET     CA  A 997       1                                                       
HET     ZN  A 998       1                                                       
HET     ZN  A 999       1                                                       
HET    2NI  A1000      23                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     2NI N-{2-[(4'-CYANO-1,1'-BIPHENYL-4-YL)OXY]ETHYL}-N'-                
HETNAM   2 2NI  HYDROXY-N-METHYLUREA                                            
FORMUL   2   CA    2(CA 2+)                                                     
FORMUL   4   ZN    2(ZN 2+)                                                     
FORMUL   6  2NI    C17 H17 N3 O3                                                
FORMUL   7  HOH   *125(H2 O)                                                    
HELIX    1   1 SER A  105  VAL A  122  1                                  18    
HELIX    2   2 ASN A  190  LEU A  203  1                                  14    
HELIX    3   3 PRO A  230  GLY A  242  1                                  13    
SHEET    1   A 5 ILE A 127  ARG A 130  0                                        
SHEET    2   A 5 ASN A  92  ILE A  97  1  N  LEU A  93   O  THR A 129           
SHEET    3   A 5 ILE A 138  TYR A 143  1  O  ILE A 140   N  ARG A  96           
SHEET    4   A 5 ALA A 174  ASP A 177  1  O  PHE A 176   N  ALA A 141           
SHEET    5   A 5 ALA A 161  ALA A 163 -1  N  HIS A 162   O  HIS A 175           
LINK        CA    CA A 996                 O   ASP A 137     1555   1555  2.53  
LINK        CA    CA A 996                 O   GLY A 171     1555   1555  2.54  
LINK        CA    CA A 996                 O   GLY A 169     1555   1555  2.65  
LINK        CA    CA A 996                 OD1 ASP A 173     1555   1555  2.55  
LINK        CA    CA A 996                 O   HOH A1093     1555   1555  3.21  
LINK        CA    CA A 996                 O   HOH A1098     1555   1555  2.67  
LINK        CA    CA A 997                 O   ILE A 159     1555   1555  2.45  
LINK        CA    CA A 997                 OD1 ASP A 154     1555   1555  2.47  
LINK        CA    CA A 997                 O   GLY A 155     1555   1555  2.43  
LINK        CA    CA A 997                 O   ASN A 157     1555   1555  2.40  
LINK        CA    CA A 997                 OD2 ASP A 177     1555   1555  2.43  
LINK        CA    CA A 997                 OE2 GLU A 180     1555   1555  2.43  
LINK        ZN    ZN A 998                 NE2 HIS A 162     1555   1555  2.05  
LINK        ZN    ZN A 998                 OD2 ASP A 149     1555   1555  1.98  
LINK        ZN    ZN A 998                 ND1 HIS A 175     1555   1555  2.07  
LINK        ZN    ZN A 998                 NE2 HIS A 147     1555   1555  2.08  
LINK        ZN    ZN A 999                 NE2 HIS A 197     1555   1555  2.08  
LINK        ZN    ZN A 999                 O3  2NI A1000     1555   1555  2.26  
LINK        ZN    ZN A 999                 NE2 HIS A 201     1555   1555  2.06  
LINK        ZN    ZN A 999                 NE2 HIS A 207     1555   1555  2.11  
CISPEP   1 ASN A  188    TYR A  189          0        -0.35                     
SITE     1 AC1  5 ASP A 137  GLY A 169  GLY A 171  ASP A 173                    
SITE     2 AC1  5 HOH A1098                                                     
SITE     1 AC2  6 ASP A 154  GLY A 155  ASN A 157  ILE A 159                    
SITE     2 AC2  6 ASP A 177  GLU A 180                                          
SITE     1 AC3  4 HIS A 147  ASP A 149  HIS A 162  HIS A 175                    
SITE     1 AC4  4 HIS A 197  HIS A 201  HIS A 207  2NI A1000                    
SITE     1 AC5 16 ILE A 159  LEU A 160  ALA A 161  LEU A 193                    
SITE     2 AC5 16 HIS A 197  GLU A 198  HIS A 207  LEU A 214                    
SITE     3 AC5 16 TYR A 216  PRO A 217  ASN A 218  TYR A 219                    
SITE     4 AC5 16 ALA A 220   ZN A 999  HOH A1069  HOH A1105                    
CRYST1   32.387   52.675   67.331  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      0.030877  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018984  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014852        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system