GenomeNet

Database: PDB
Entry: 1XUD
LinkDB: 1XUD
Original site: 1XUD 
HEADER    HYDROLASE                               26-OCT-04   1XUD              
TITLE     MATRIX METALLOPROTEINASE-13 COMPLEXED WITH NON-ZINC BINDING           
TITLE    2 INHIBITOR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COLLAGENASE 3;                                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN;                                          
COMPND   5 SYNONYM: MATRIX METALLOPROTEINASE-13, MMP-13;                        
COMPND   6 EC: 3.4.24.-;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    MATRIX METALLOPROTEINASE, NON-ZINC BINDING INHIBITOR,                 
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.K.ENGEL,K.U.WENDT                                                   
REVDAT   2   24-FEB-09 1XUD    1       VERSN                                    
REVDAT   1   26-OCT-05 1XUD    0                                                
JRNL        AUTH   C.K.ENGEL,B.PIRARD,S.SCHIMANSKI,R.KIRSCH,                    
JRNL        AUTH 2 J.HABERMANN,O.KLINGLER,V.SCHLOTTE,K.U.WEITHMANN,             
JRNL        AUTH 3 K.U.WENDT                                                    
JRNL        TITL   STRUCTURAL BASIS FOR THE HIGHLY SELECTIVE                    
JRNL        TITL 2 INHIBITION OF MMP-13.                                        
JRNL        REF    CHEM.BIOL.                    V.  12   181 2005              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   15734640                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2004.11.014                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000.000                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 30796                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2783                            
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            : 2667                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 473                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01300                                              
REMARK   3    B22 (A**2) : -0.03400                                             
REMARK   3    B33 (A**2) : 0.02100                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.02200                                             
REMARK   3    B23 (A**2) : 0.00000                                              
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) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
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 1XUD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-OCT-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030781.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30796                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.7100                            
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) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 60.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.10100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.570                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       67.01100            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       18.23750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       67.01100            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       18.23750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 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     PRO A   273                                                      
REMARK 465     ASN A   274                                                      
REMARK 465     ASP B   270                                                      
REMARK 465     GLU B   271                                                      
REMARK 465     ASP B   272                                                      
REMARK 465     PRO B   273                                                      
REMARK 465     ASN B   274                                                      
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    PRO A 108      154.98    -48.82                                   
REMARK 500    LYS A 170     -130.85     40.40                                   
REMARK 500    SER A 182      172.84     74.56                                   
REMARK 500    ASN A 194     -110.99     50.21                                   
REMARK 500    SER A 210     -152.03   -122.40                                   
REMARK 500    ASP A 231     -163.68   -101.11                                   
REMARK 500    LYS B 170     -133.90     42.69                                   
REMARK 500    SER B 182      167.78     68.96                                   
REMARK 500    ALA B 186      167.82    178.91                                   
REMARK 500    ASN B 194     -119.20     56.09                                   
REMARK 500    SER B 211     -144.76   -129.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2173        DISTANCE =  6.92 ANGSTROMS                       
REMARK 525    HOH A2188        DISTANCE =  8.66 ANGSTROMS                       
REMARK 525    HOH A2189        DISTANCE =  9.16 ANGSTROMS                       
REMARK 525    HOH A2200        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH A2224        DISTANCE = 10.33 ANGSTROMS                       
REMARK 525    HOH A2237        DISTANCE =  7.44 ANGSTROMS                       
REMARK 525    HOH A2240        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH A2242        DISTANCE =  7.40 ANGSTROMS                       
REMARK 525    HOH A2248        DISTANCE =  8.19 ANGSTROMS                       
REMARK 525    HOH A2254        DISTANCE =  8.17 ANGSTROMS                       
REMARK 525    HOH A2255        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH A2259        DISTANCE =  8.23 ANGSTROMS                       
REMARK 525    HOH A2263        DISTANCE =  5.98 ANGSTROMS                       
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 A1261  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 222   NE2                                                    
REMARK 620 2 HIS A 226   NE2 100.9                                              
REMARK 620 3 HIS A 232   NE2 110.4  99.3                                        
REMARK 620 4 HOH A2019   O   106.1 101.2 133.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1262  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 172   NE2                                                    
REMARK 620 2 ASP A 174   OD2 108.2                                              
REMARK 620 3 HIS A 187   NE2 114.6 119.1                                        
REMARK 620 4 HIS A 200   ND1 109.0  94.2 109.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1264  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 179   OD1                                                    
REMARK 620 2 GLY A 180   O    86.7                                              
REMARK 620 3 GLU A 205   OE2 158.9  79.9                                        
REMARK 620 4 SER A 182   O    78.6  80.1  83.0                                  
REMARK 620 5 LEU A 184   O    95.3 175.6  97.0  96.5                            
REMARK 620 6 ASP A 202   OD2  93.9  92.9 103.0 170.0  90.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1265  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 194   O                                                      
REMARK 620 2 GLY A 196   O    99.0                                              
REMARK 620 3 ASP A 198   OD1 109.5  98.8                                        
REMARK 620 4 HOH A2110   O    72.9  74.3 173.0                                  
REMARK 620 5 HOH A2098   O    75.7 166.2  95.0  92.0                            
REMARK 620 6 ASP A 162   O   158.2  83.4  91.3  87.1  96.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1261  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 222   NE2                                                    
REMARK 620 2 HIS B 226   NE2 107.5                                              
REMARK 620 3 HIS B 232   NE2 112.6 100.6                                        
REMARK 620 4 HOH B3013   O   108.2 112.7 114.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1262  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 172   NE2                                                    
REMARK 620 2 ASP B 174   OD2 117.5                                              
REMARK 620 3 HIS B 187   NE2 113.6 112.9                                        
REMARK 620 4 HIS B 200   ND1 107.8  90.7 111.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1264  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 179   OD1                                                    
REMARK 620 2 GLY B 180   O    88.8                                              
REMARK 620 3 SER B 182   O    78.0  78.8                                        
REMARK 620 4 ASP B 202   OD2  93.0  87.4 163.6                                  
REMARK 620 5 LEU B 184   O    93.8 177.4 101.9  92.2                            
REMARK 620 6 GLU B 205   OE1 153.1  97.0  77.4 113.4  80.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1265  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 194   O                                                      
REMARK 620 2 GLY B 196   O    98.8                                              
REMARK 620 3 ASP B 198   OD1 102.3 100.2                                        
REMARK 620 4 ASP B 162   O   167.5  82.9  89.5                                  
REMARK 620 5 HOH B3074   O    84.3  73.2 171.5  84.4                            
REMARK 620 6 HOH B3128   O    74.2 163.0  96.4 100.6  90.5                      
REMARK 620 N                    1     2     3     4     5                       
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 1261                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1262                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1264                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1265                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1261                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1262                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1264                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1265                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB4 A 2001                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB4 B 3001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1XUC   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH PB3                                            
REMARK 900 RELATED ID: 1XUR   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH PB5                                            
DBREF  1XUD A  104   274  UNP    P45452   MMP13_HUMAN    104    274             
DBREF  1XUD B  104   274  UNP    P45452   MMP13_HUMAN    104    274             
SEQRES   1 A  171  TYR ASN VAL PHE PRO ARG THR LEU LYS TRP SER LYS MET          
SEQRES   2 A  171  ASN LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP MET          
SEQRES   3 A  171  THR HIS SER GLU VAL GLU LYS ALA PHE LYS LYS ALA PHE          
SEQRES   4 A  171  LYS VAL TRP SER ASP VAL THR PRO LEU ASN PHE THR ARG          
SEQRES   5 A  171  LEU HIS ASP GLY ILE ALA ASP ILE MET ILE SER PHE GLY          
SEQRES   6 A  171  ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO          
SEQRES   7 A  171  SER GLY LEU LEU ALA HIS ALA PHE PRO PRO GLY PRO ASN          
SEQRES   8 A  171  TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP GLU THR TRP          
SEQRES   9 A  171  THR SER SER SER LYS GLY TYR ASN LEU PHE LEU VAL ALA          
SEQRES  10 A  171  ALA HIS GLU PHE GLY HIS SER LEU GLY LEU ASP HIS SER          
SEQRES  11 A  171  LYS ASP PRO GLY ALA LEU MET PHE PRO ILE TYR THR TYR          
SEQRES  12 A  171  THR GLY LYS SER HIS PHE MET LEU PRO ASP ASP ASP VAL          
SEQRES  13 A  171  GLN GLY ILE GLN SER LEU TYR GLY PRO GLY ASP GLU ASP          
SEQRES  14 A  171  PRO ASN                                                      
SEQRES   1 B  171  TYR ASN VAL PHE PRO ARG THR LEU LYS TRP SER LYS MET          
SEQRES   2 B  171  ASN LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP MET          
SEQRES   3 B  171  THR HIS SER GLU VAL GLU LYS ALA PHE LYS LYS ALA PHE          
SEQRES   4 B  171  LYS VAL TRP SER ASP VAL THR PRO LEU ASN PHE THR ARG          
SEQRES   5 B  171  LEU HIS ASP GLY ILE ALA ASP ILE MET ILE SER PHE GLY          
SEQRES   6 B  171  ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO          
SEQRES   7 B  171  SER GLY LEU LEU ALA HIS ALA PHE PRO PRO GLY PRO ASN          
SEQRES   8 B  171  TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP GLU THR TRP          
SEQRES   9 B  171  THR SER SER SER LYS GLY TYR ASN LEU PHE LEU VAL ALA          
SEQRES  10 B  171  ALA HIS GLU PHE GLY HIS SER LEU GLY LEU ASP HIS SER          
SEQRES  11 B  171  LYS ASP PRO GLY ALA LEU MET PHE PRO ILE TYR THR TYR          
SEQRES  12 B  171  THR GLY LYS SER HIS PHE MET LEU PRO ASP ASP ASP VAL          
SEQRES  13 B  171  GLN GLY ILE GLN SER LEU TYR GLY PRO GLY ASP GLU ASP          
SEQRES  14 B  171  PRO ASN                                                      
HET     ZN  A1261       1                                                       
HET     ZN  A1262       1                                                       
HET     CA  A1264       1                                                       
HET     CA  A1265       1                                                       
HET     ZN  B1261       1                                                       
HET     ZN  B1262       1                                                       
HET     CA  B1264       1                                                       
HET     CA  B1265       1                                                       
HET    PB4  A2001      30                                                       
HET    PB4  B3001      30                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     PB4 N,N'-BIS(4-FLUORO-3-METHYLBENZYL)PYRIMIDINE-4,6-                 
HETNAM   2 PB4  DICARBOXAMIDE                                                   
HETSYN     PB4 PYRIMIDINE-4,6-DICARBOXYLIC ACID BIS-(4-FLUORO-3-                
HETSYN   2 PB4  METHYL-BENZYLAMIDE)                                             
FORMUL   3   ZN    4(ZN 2+)                                                     
FORMUL   5   CA    4(CA 2+)                                                     
FORMUL  11  PB4    2(C22 H20 F2 N4 O2)                                          
FORMUL  13  HOH   *473(H2 O)                                                    
HELIX    1   1 THR A  130  ASP A  147  1                                  18    
HELIX    2   2 LEU A  216  GLY A  229  1                                  14    
HELIX    3   3 PRO A  255  GLY A  267  1                                  13    
HELIX    4   4 THR B  130  ASP B  147  1                                  18    
HELIX    5   5 LEU B  216  GLY B  229  1                                  14    
HELIX    6   6 PRO B  255  GLY B  267  1                                  13    
SHEET    1   A 5 ASN A 152  LEU A 156  0                                        
SHEET    2   A 5 ASN A 117  ILE A 122  1  N  TYR A 120   O  LEU A 156           
SHEET    3   A 5 ILE A 163  GLY A 168  1  O  ILE A 165   N  ARG A 121           
SHEET    4   A 5 ALA A 199  ASP A 202  1  O  PHE A 201   N  SER A 166           
SHEET    5   A 5 ALA A 186  ALA A 188 -1  N  HIS A 187   O  HIS A 200           
SHEET    1   B 2 TRP A 207  THR A 208  0                                        
SHEET    2   B 2 TYR A 214  ASN A 215  1  O  TYR A 214   N  THR A 208           
SHEET    1   C 5 ASN B 152  ARG B 155  0                                        
SHEET    2   C 5 ASN B 117  ILE B 122  1  N  LEU B 118   O  ASN B 152           
SHEET    3   C 5 ILE B 163  GLY B 168  1  O  ILE B 165   N  ARG B 121           
SHEET    4   C 5 ALA B 199  ASP B 202  1  O  PHE B 201   N  SER B 166           
SHEET    5   C 5 ALA B 186  ALA B 188 -1  N  HIS B 187   O  HIS B 200           
SHEET    1   D 2 TRP B 207  THR B 208  0                                        
SHEET    2   D 2 TYR B 214  ASN B 215  1  O  TYR B 214   N  THR B 208           
LINK        ZN    ZN A1261                 NE2 HIS A 222     1555   1555  2.17  
LINK        ZN    ZN A1261                 NE2 HIS A 226     1555   1555  2.14  
LINK        ZN    ZN A1261                 NE2 HIS A 232     1555   1555  2.10  
LINK        ZN    ZN A1262                 NE2 HIS A 172     1555   1555  2.09  
LINK        ZN    ZN A1262                 OD2 ASP A 174     1555   1555  2.01  
LINK        ZN    ZN A1262                 NE2 HIS A 187     1555   1555  2.14  
LINK        ZN    ZN A1262                 ND1 HIS A 200     1555   1555  2.15  
LINK        CA    CA A1264                 OD1 ASP A 179     1555   1555  2.51  
LINK        CA    CA A1264                 O   GLY A 180     1555   1555  2.43  
LINK        CA    CA A1264                 OE2 GLU A 205     1555   1555  2.58  
LINK        CA    CA A1265                 O   ASN A 194     1555   1555  2.50  
LINK        CA    CA A1265                 O   GLY A 196     1555   1555  2.52  
LINK        CA    CA A1265                 OD1 ASP A 198     1555   1555  2.60  
LINK        ZN    ZN B1261                 NE2 HIS B 222     1555   1555  2.16  
LINK        ZN    ZN B1261                 NE2 HIS B 226     1555   1555  2.18  
LINK        ZN    ZN B1261                 NE2 HIS B 232     1555   1555  2.17  
LINK        ZN    ZN B1262                 NE2 HIS B 172     1555   1555  2.11  
LINK        ZN    ZN B1262                 OD2 ASP B 174     1555   1555  2.07  
LINK        ZN    ZN B1262                 NE2 HIS B 187     1555   1555  2.13  
LINK        ZN    ZN B1262                 ND1 HIS B 200     1555   1555  2.19  
LINK        CA    CA B1264                 OD1 ASP B 179     1555   1555  2.58  
LINK        CA    CA B1264                 O   GLY B 180     1555   1555  2.46  
LINK        CA    CA B1265                 O   ASN B 194     1555   1555  2.58  
LINK        CA    CA B1265                 O   GLY B 196     1555   1555  2.55  
LINK        CA    CA B1265                 OD1 ASP B 198     1555   1555  2.57  
LINK        ZN    ZN A1261                 O   HOH A2019     1555   1555  2.41  
LINK        CA    CA A1264                 O   SER A 182     1555   1555  2.56  
LINK        CA    CA A1264                 O   LEU A 184     1555   1555  2.39  
LINK        CA    CA A1264                 OD2 ASP A 202     1555   1555  2.43  
LINK        CA    CA A1265                 O   HOH A2110     1555   1555  2.86  
LINK        CA    CA A1265                 O   HOH A2098     1555   1555  2.66  
LINK        CA    CA A1265                 O   ASP A 162     1555   1555  2.53  
LINK        ZN    ZN B1261                 O   HOH B3013     1555   1555  2.41  
LINK        CA    CA B1264                 O   SER B 182     1555   1555  2.65  
LINK        CA    CA B1264                 OD2 ASP B 202     1555   1555  2.48  
LINK        CA    CA B1264                 O   LEU B 184     1555   1555  2.42  
LINK        CA    CA B1264                 OE1 GLU B 205     1555   1555  2.59  
LINK        CA    CA B1265                 O   ASP B 162     1555   1555  2.54  
LINK        CA    CA B1265                 O   HOH B3074     1555   1555  2.71  
LINK        CA    CA B1265                 O   HOH B3128     1555   1555  2.80  
SITE     1 AC1  4 HIS A 222  HIS A 226  HIS A 232  HOH A2019                    
SITE     1 AC2  4 HIS A 172  ASP A 174  HIS A 187  HIS A 200                    
SITE     1 AC3  6 ASP A 179  GLY A 180  SER A 182  LEU A 184                    
SITE     2 AC3  6 ASP A 202  GLU A 205                                          
SITE     1 AC4  6 ASP A 162  ASN A 194  GLY A 196  ASP A 198                    
SITE     2 AC4  6 HOH A2098  HOH A2110                                          
SITE     1 AC5  4 HIS B 222  HIS B 226  HIS B 232  HOH B3013                    
SITE     1 AC6  4 HIS B 172  ASP B 174  HIS B 187  HIS B 200                    
SITE     1 AC7  6 ASP B 179  GLY B 180  SER B 182  LEU B 184                    
SITE     2 AC7  6 ASP B 202  GLU B 205                                          
SITE     1 AC8  6 ASP B 162  ASN B 194  GLY B 196  ASP B 198                    
SITE     2 AC8  6 HOH B3074  HOH B3128                                          
SITE     1 AC9 19 LEU A 185  PHE A 217  LEU A 218  VAL A 219                    
SITE     2 AC9 19 HIS A 222  ALA A 238  LEU A 239  PHE A 241                    
SITE     3 AC9 19 PRO A 242  ILE A 243  TYR A 244  THR A 245                    
SITE     4 AC9 19 TYR A 246  THR A 247  LYS A 249  SER A 250                    
SITE     5 AC9 19 PHE A 252  HOH A2007  HOH A2008                               
SITE     1 BC1 19 ASN B 215  PHE B 217  LEU B 218  VAL B 219                    
SITE     2 BC1 19 HIS B 222  ALA B 238  LEU B 239  PHE B 241                    
SITE     3 BC1 19 PRO B 242  ILE B 243  TYR B 244  THR B 245                    
SITE     4 BC1 19 TYR B 246  THR B 247  LYS B 249  SER B 250                    
SITE     5 BC1 19 HIS B 251  PHE B 252  HOH B3006                               
CRYST1  134.022   36.475   95.060  90.00 130.41  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007461  0.000000  0.006353        0.00000                         
SCALE2      0.000000  0.027416  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013816        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system