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Database: PDB
Entry: 5UWM
LinkDB: 5UWM
Original site: 5UWM 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           21-FEB-17   5UWM              
TITLE     MATRIX METALLOPROTEINASE-13 COMPLEXED WITH SELECTIVE INHIBITOR        
TITLE    2 COMPOUND (R)-17A                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COLLAGENASE 3;                                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MATRIX METALLOPROTEINASE-13,MMP-13;                         
COMPND   5 EC: 3.4.24.-;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: CATALYTIC DOMAIN (UNP RESIDUES 104-274);              
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: COLLAGENASE 3;                                             
COMPND  10 CHAIN: C, D;                                                         
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 OTHER_DETAILS: PROTEOLYTIC FRAGMENT                                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MMP13;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PKA8H;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PKA8H                                     
KEYWDS    METALLOPROTEINASE, COLLAGENASE, MMP-13, HYDROLASE, HYDROLASE-         
KEYWDS   2 HYDROLASE INHIBITOR COMPLEX                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.B.TAYLOR,X.CAO,P.J.HART                                             
REVDAT   2   26-JUL-17 5UWM    1       JRNL                                     
REVDAT   1   12-JUL-17 5UWM    0                                                
JRNL        AUTH   J.Y.CHOI,R.FUERST,A.M.KNAPINSKA,A.B.TAYLOR,L.SMITH,X.CAO,    
JRNL        AUTH 2 P.J.HART,G.B.FIELDS,W.R.ROUSH                                
JRNL        TITL   STRUCTURE-BASED DESIGN AND SYNTHESIS OF POTENT AND SELECTIVE 
JRNL        TITL 2 MATRIX METALLOPROTEINASE 13 INHIBITORS.                      
JRNL        REF    J. MED. CHEM.                 V.  60  5816 2017              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   28653849                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.7B00514                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.62 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.77                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.970                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 43436                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.131                           
REMARK   3   R VALUE            (WORKING SET) : 0.129                           
REMARK   3   FREE R VALUE                     : 0.178                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.610                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2002                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 32.7787 -  3.9030    0.98     2913   140  0.1213 0.1380        
REMARK   3     2  3.9030 -  3.0987    1.00     2965   140  0.1292 0.1636        
REMARK   3     3  3.0987 -  2.7072    1.00     2953   145  0.1423 0.2144        
REMARK   3     4  2.7072 -  2.4598    1.00     2974   139  0.1354 0.1961        
REMARK   3     5  2.4598 -  2.2835    1.00     2952   146  0.1201 0.1720        
REMARK   3     6  2.2835 -  2.1489    1.00     2978   145  0.1132 0.1614        
REMARK   3     7  2.1489 -  2.0413    1.00     2939   140  0.1100 0.1636        
REMARK   3     8  2.0413 -  1.9525    1.00     2973   145  0.1116 0.1701        
REMARK   3     9  1.9525 -  1.8773    1.00     2957   142  0.1179 0.1849        
REMARK   3    10  1.8773 -  1.8125    1.00     2966   145  0.1249 0.1869        
REMARK   3    11  1.8125 -  1.7559    1.00     2955   144  0.1348 0.2146        
REMARK   3    12  1.7559 -  1.7057    1.00     2978   145  0.1571 0.2338        
REMARK   3    13  1.7057 -  1.6608    1.00     2977   145  0.1712 0.2499        
REMARK   3    14  1.6608 -  1.6203    1.00     2954   141  0.1998 0.2678        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.150            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.400           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.10                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           2752                                  
REMARK   3   ANGLE     :  0.987           3755                                  
REMARK   3   CHIRALITY :  0.053            379                                  
REMARK   3   PLANARITY :  0.007            486                                  
REMARK   3   DIHEDRAL  : 14.391            976                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5UWM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000226516.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-NOV-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43442                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.620                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.770                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.64600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4L19                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE 0.1 M TRIS:HCL     
REMARK 280  PH 8.5, 30% POLYETHYLENE GLYCOL 4000, VAPOR DIFFUSION, SITTING      
REMARK 280  DROP, TEMPERATURE 295K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       70.03650            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       40.43559            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       15.62000            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       70.03650            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       40.43559            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       15.62000            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       70.03650            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       40.43559            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       15.62000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       80.87118            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       31.24000            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       80.87118            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       31.24000            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       80.87118            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       31.24000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8270 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8100 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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     MET A   103                                                      
REMARK 465     TYR A   104                                                      
REMARK 465     ASN A   105                                                      
REMARK 465     VAL A   106                                                      
REMARK 465     PHE A   107                                                      
REMARK 465     PRO A   108                                                      
REMARK 465     ARG A   109                                                      
REMARK 465     THR A   110                                                      
REMARK 465     GLY A   248                                                      
REMARK 465     LYS A   249                                                      
REMARK 465     SER A   250                                                      
REMARK 465     GLY A   269                                                      
REMARK 465     ASP A   270                                                      
REMARK 465     GLU A   271                                                      
REMARK 465     ASP A   272                                                      
REMARK 465     PRO A   273                                                      
REMARK 465     ASN A   274                                                      
REMARK 465     MET B   103                                                      
REMARK 465     TYR B   104                                                      
REMARK 465     ASN B   105                                                      
REMARK 465     VAL B   106                                                      
REMARK 465     PHE B   107                                                      
REMARK 465     PRO B   108                                                      
REMARK 465     ARG B   109                                                      
REMARK 465     THR B   110                                                      
REMARK 465     THR B   247                                                      
REMARK 465     GLY B   248                                                      
REMARK 465     LYS B   249                                                      
REMARK 465     SER B   250                                                      
REMARK 465     HIS B   251                                                      
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 465     VAL D   211                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   413     O    HOH A   530              2.01            
REMARK 500   O    HOH B   489     O    HOH B   552              2.02            
REMARK 500   O    HOH B   403     O    HOH B   491              2.06            
REMARK 500   O    HOH B   485     O    HOH B   549              2.08            
REMARK 500   O    HOH B   532     O    HOH B   549              2.12            
REMARK 500   O    HOH A   506     O    HOH A   538              2.16            
REMARK 500   O    HOH A   514     O    HOH A   524              2.16            
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    LYS A 170     -132.69     46.13                                   
REMARK 500    SER A 182     -175.67     74.88                                   
REMARK 500    ASN A 194     -120.80     59.92                                   
REMARK 500    LYS B 170     -131.59     48.02                                   
REMARK 500    SER B 182     -163.42     66.20                                   
REMARK 500    ASN B 194     -118.22     56.91                                   
REMARK 500    SER B 210     -163.42   -123.50                                   
REMARK 500    ASP B 231     -141.27    -96.21                                   
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 304  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 128   OD1                                                    
REMARK 620 2 ASP A 128   OD2  50.0                                              
REMARK 620 3 ASP A 203   O   152.7 154.1                                        
REMARK 620 4 ASP A 203   OD1  94.8  88.5  78.9                                  
REMARK 620 5 GLU A 205   O   126.5  81.8  80.5 107.2                            
REMARK 620 6 HOH A 498   O    81.9  92.8 101.9 174.3  78.5                      
REMARK 620 7 HOH A 525   O    75.7 125.7  78.4  95.3 145.4  79.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 305  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 162   O                                                      
REMARK 620 2 ASN A 194   O   169.7                                              
REMARK 620 3 GLY A 196   O    91.7  97.1                                        
REMARK 620 4 ASP A 198   OD1  85.5  99.5  91.0                                  
REMARK 620 5 HOH A 418   O    88.1  88.4  79.1 168.0                            
REMARK 620 6 HOH A 434   O    87.2  83.2 169.1  99.7  90.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 172   NE2                                                    
REMARK 620 2 ASP A 174   OD2 111.4                                              
REMARK 620 3 HIS A 187   NE2 118.0 112.7                                        
REMARK 620 4 HIS A 200   ND1 103.5  95.6 113.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 303  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 179   OD1                                                    
REMARK 620 2 GLY A 180   O    86.2                                              
REMARK 620 3 SER A 182   O    85.4  86.0                                        
REMARK 620 4 LEU A 184   O    94.3 179.5  93.9                                  
REMARK 620 5 ASP A 202   OD2  94.4  89.7 175.7  90.4                            
REMARK 620 6 GLU A 205   OE2 170.7  92.9  85.4  86.5  94.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 222   NE2                                                    
REMARK 620 2 HIS A 226   NE2  99.2                                              
REMARK 620 3 HIS A 232   NE2 116.9 103.9                                        
REMARK 620 4 ASN C 215   O    93.4  89.5 143.5                                  
REMARK 620 5 ASN C 215   OXT 125.6 117.8  92.5  51.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 304  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 128   OD1                                                    
REMARK 620 2 ASP B 128   OD2  50.7                                              
REMARK 620 3 ASP B 203   O   154.1 151.3                                        
REMARK 620 4 ASP B 203   OD1  93.2  87.4  79.1                                  
REMARK 620 5 GLU B 205   O   125.2  79.7  80.6 108.1                            
REMARK 620 6 HOH B 492   O    76.4 126.9  79.1  91.8 148.2                      
REMARK 620 7 HOH B 496   O    84.6  95.9 100.3 173.5  78.1  81.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 305  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 162   O                                                      
REMARK 620 2 ASN B 194   O   173.3                                              
REMARK 620 3 GLY B 196   O    91.3  94.9                                        
REMARK 620 4 ASP B 198   OD1  87.3  95.2  90.8                                  
REMARK 620 5 HOH B 431   O    91.0  82.5 170.5  98.5                            
REMARK 620 6 HOH B 418   O    88.3  90.1  81.2 170.7  89.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 172   NE2                                                    
REMARK 620 2 ASP B 174   OD2 111.0                                              
REMARK 620 3 HIS B 187   NE2 113.7 115.4                                        
REMARK 620 4 HIS B 200   ND1 106.1  97.6 111.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 303  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 179   OD1                                                    
REMARK 620 2 GLY B 180   O    87.1                                              
REMARK 620 3 SER B 182   O    86.4  87.1                                        
REMARK 620 4 LEU B 184   O    91.0 178.1  92.9                                  
REMARK 620 5 ASP B 202   OD2  90.8  87.3 173.8  92.7                            
REMARK 620 6 GLU B 205   OE2 173.7  92.1  87.3  89.8  95.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 222   NE2                                                    
REMARK 620 2 HIS B 226   NE2 103.4                                              
REMARK 620 3 HIS B 232   NE2 115.4 100.9                                        
REMARK 620 4 ASN D 215   O   125.8 114.9  94.1                                  
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 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8OA A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8OA B 306                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5UWK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UWL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UWN   RELATED DB: PDB                                   
DBREF  5UWM A  104   274  UNP    P45452   MMP13_HUMAN    104    274             
DBREF  5UWM B  104   274  UNP    P45452   MMP13_HUMAN    104    274             
DBREF  5UWM C  211   215  PDB    5UWM     5UWM           211    215             
DBREF  5UWM D  211   215  PDB    5UWM     5UWM           211    215             
SEQADV 5UWM MET A  103  UNP  P45452              INITIATING METHIONINE          
SEQADV 5UWM MET B  103  UNP  P45452              INITIATING METHIONINE          
SEQRES   1 A  172  MET TYR ASN VAL PHE PRO ARG THR LEU LYS TRP SER LYS          
SEQRES   2 A  172  MET ASN LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP          
SEQRES   3 A  172  MET THR HIS SER GLU VAL GLU LYS ALA PHE LYS LYS ALA          
SEQRES   4 A  172  PHE LYS VAL TRP SER ASP VAL THR PRO LEU ASN PHE THR          
SEQRES   5 A  172  ARG LEU HIS ASP GLY ILE ALA ASP ILE MET ILE SER PHE          
SEQRES   6 A  172  GLY ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY          
SEQRES   7 A  172  PRO SER GLY LEU LEU ALA HIS ALA PHE PRO PRO GLY PRO          
SEQRES   8 A  172  ASN TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP GLU THR          
SEQRES   9 A  172  TRP THR SER SER SER LYS GLY TYR ASN LEU PHE LEU VAL          
SEQRES  10 A  172  ALA ALA HIS GLU PHE GLY HIS SER LEU GLY LEU ASP HIS          
SEQRES  11 A  172  SER LYS ASP PRO GLY ALA LEU MET PHE PRO ILE TYR THR          
SEQRES  12 A  172  TYR THR GLY LYS SER HIS PHE MET LEU PRO ASP ASP ASP          
SEQRES  13 A  172  VAL GLN GLY ILE GLN SER LEU TYR GLY PRO GLY ASP GLU          
SEQRES  14 A  172  ASP PRO ASN                                                  
SEQRES   1 B  172  MET TYR ASN VAL PHE PRO ARG THR LEU LYS TRP SER LYS          
SEQRES   2 B  172  MET ASN LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP          
SEQRES   3 B  172  MET THR HIS SER GLU VAL GLU LYS ALA PHE LYS LYS ALA          
SEQRES   4 B  172  PHE LYS VAL TRP SER ASP VAL THR PRO LEU ASN PHE THR          
SEQRES   5 B  172  ARG LEU HIS ASP GLY ILE ALA ASP ILE MET ILE SER PHE          
SEQRES   6 B  172  GLY ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY          
SEQRES   7 B  172  PRO SER GLY LEU LEU ALA HIS ALA PHE PRO PRO GLY PRO          
SEQRES   8 B  172  ASN TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP GLU THR          
SEQRES   9 B  172  TRP THR SER SER SER LYS GLY TYR ASN LEU PHE LEU VAL          
SEQRES  10 B  172  ALA ALA HIS GLU PHE GLY HIS SER LEU GLY LEU ASP HIS          
SEQRES  11 B  172  SER LYS ASP PRO GLY ALA LEU MET PHE PRO ILE TYR THR          
SEQRES  12 B  172  TYR THR GLY LYS SER HIS PHE MET LEU PRO ASP ASP ASP          
SEQRES  13 B  172  VAL GLN GLY ILE GLN SER LEU TYR GLY PRO GLY ASP GLU          
SEQRES  14 B  172  ASP PRO ASN                                                  
SEQRES   1 C    5  VAL THR PRO LEU ASN                                          
SEQRES   1 D    5  VAL THR PRO LEU ASN                                          
HET     ZN  A 301       1                                                       
HET     ZN  A 302       1                                                       
HET     CA  A 303       1                                                       
HET     CA  A 304       1                                                       
HET     CA  A 305       1                                                       
HET    8OA  A 306      38                                                       
HET     ZN  B 301       1                                                       
HET     ZN  B 302       1                                                       
HET     CA  B 303       1                                                       
HET     CA  B 304       1                                                       
HET     CA  B 305       1                                                       
HET    8OA  B 306      34                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     8OA (R)-N-(3-METHYL-1-(METHYLAMINO)-1-OXOBUTAN-2-YL)-5-(4-           
HETNAM   2 8OA  (((4-OXO-4,5,6,7-TETRAHYDRO-3H-CYCLOPENTA[D]PYRIMIDIN-          
HETNAM   3 8OA  2-YL)THIO)METHYL)PHENYL)FURAN-2-CARBOXAMIDE                     
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   7   CA    6(CA 2+)                                                     
FORMUL  10  8OA    2(C25 H28 N4 O4 S)                                           
FORMUL  17  HOH   *353(H2 O)                                                    
HELIX    1 AA1 THR A  130  ASP A  147  1                                  18    
HELIX    2 AA2 LEU A  216  LEU A  228  1                                  13    
HELIX    3 AA3 PRO A  255  GLY A  267  1                                  13    
HELIX    4 AA4 THR B  130  ASP B  147  1                                  18    
HELIX    5 AA5 LEU B  216  LEU B  228  1                                  13    
HELIX    6 AA6 PRO B  255  GLY B  267  1                                  13    
SHEET    1 AA1 5 ASN A 152  LEU A 156  0                                        
SHEET    2 AA1 5 ASN A 117  ILE A 122  1  N  TYR A 120   O  LEU A 156           
SHEET    3 AA1 5 ILE A 163  GLY A 168  1  O  ILE A 165   N  ARG A 121           
SHEET    4 AA1 5 ALA A 199  ASP A 202  1  O  PHE A 201   N  GLY A 168           
SHEET    5 AA1 5 ALA A 186  ALA A 188 -1  N  HIS A 187   O  HIS A 200           
SHEET    1 AA2 2 TRP A 207  THR A 208  0                                        
SHEET    2 AA2 2 TYR A 214  ASN A 215  1  O  TYR A 214   N  THR A 208           
SHEET    1 AA3 5 ASN B 152  ARG B 155  0                                        
SHEET    2 AA3 5 ASN B 117  ILE B 122  1  N  LEU B 118   O  ASN B 152           
SHEET    3 AA3 5 ILE B 163  GLY B 168  1  O  ILE B 165   N  ARG B 121           
SHEET    4 AA3 5 ALA B 199  ASP B 202  1  O  PHE B 201   N  GLY B 168           
SHEET    5 AA3 5 ALA B 186  ALA B 188 -1  N  HIS B 187   O  HIS B 200           
SHEET    1 AA4 2 TRP B 207  THR B 208  0                                        
SHEET    2 AA4 2 TYR B 214  ASN B 215  1  O  TYR B 214   N  THR B 208           
LINK         OD1 ASP A 128                CA    CA A 304     1555   1555  2.69  
LINK         OD2 ASP A 128                CA    CA A 304     1555   1555  2.40  
LINK         O   ASP A 162                CA    CA A 305     1555   1555  2.40  
LINK         NE2 HIS A 172                ZN    ZN A 302     1555   1555  2.02  
LINK         OD2 ASP A 174                ZN    ZN A 302     1555   1555  2.02  
LINK         OD1 ASP A 179                CA    CA A 303     1555   1555  2.36  
LINK         O   GLY A 180                CA    CA A 303     1555   1555  2.26  
LINK         O   SER A 182                CA    CA A 303     1555   1555  2.37  
LINK         O   LEU A 184                CA    CA A 303     1555   1555  2.32  
LINK         NE2 HIS A 187                ZN    ZN A 302     1555   1555  2.02  
LINK         O   ASN A 194                CA    CA A 305     1555   1555  2.35  
LINK         O   GLY A 196                CA    CA A 305     1555   1555  2.28  
LINK         OD1 ASP A 198                CA    CA A 305     1555   1555  2.45  
LINK         ND1 HIS A 200                ZN    ZN A 302     1555   1555  2.03  
LINK         OD2 ASP A 202                CA    CA A 303     1555   1555  2.32  
LINK         O   ASP A 203                CA    CA A 304     1555   1555  2.48  
LINK         OD1 ASP A 203                CA    CA A 304     1555   1555  2.40  
LINK         O   GLU A 205                CA    CA A 304     1555   1555  2.36  
LINK         OE2 GLU A 205                CA    CA A 303     1555   1555  2.22  
LINK         NE2 HIS A 222                ZN    ZN A 301     1555   1555  2.03  
LINK         NE2 HIS A 226                ZN    ZN A 301     1555   1555  1.98  
LINK         NE2 HIS A 232                ZN    ZN A 301     1555   1555  2.06  
LINK         OD1 ASP B 128                CA    CA B 304     1555   1555  2.68  
LINK         OD2 ASP B 128                CA    CA B 304     1555   1555  2.43  
LINK         O   ASP B 162                CA    CA B 305     1555   1555  2.35  
LINK         NE2 HIS B 172                ZN    ZN B 302     1555   1555  2.02  
LINK         OD2 ASP B 174                ZN    ZN B 302     1555   1555  2.02  
LINK         OD1 ASP B 179                CA    CA B 303     1555   1555  2.32  
LINK         O   GLY B 180                CA    CA B 303     1555   1555  2.33  
LINK         O   SER B 182                CA    CA B 303     1555   1555  2.34  
LINK         O   LEU B 184                CA    CA B 303     1555   1555  2.29  
LINK         NE2 HIS B 187                ZN    ZN B 302     1555   1555  2.07  
LINK         O   ASN B 194                CA    CA B 305     1555   1555  2.31  
LINK         O   GLY B 196                CA    CA B 305     1555   1555  2.30  
LINK         OD1 ASP B 198                CA    CA B 305     1555   1555  2.48  
LINK         ND1 HIS B 200                ZN    ZN B 302     1555   1555  2.06  
LINK         OD2 ASP B 202                CA    CA B 303     1555   1555  2.33  
LINK         O   ASP B 203                CA    CA B 304     1555   1555  2.36  
LINK         OD1 ASP B 203                CA    CA B 304     1555   1555  2.46  
LINK         O   GLU B 205                CA    CA B 304     1555   1555  2.35  
LINK         OE2 GLU B 205                CA    CA B 303     1555   1555  2.25  
LINK         NE2 HIS B 222                ZN    ZN B 301     1555   1555  2.02  
LINK         NE2 HIS B 226                ZN    ZN B 301     1555   1555  2.12  
LINK         NE2 HIS B 232                ZN    ZN B 301     1555   1555  2.06  
LINK         O   ASN C 215                ZN    ZN A 301     1555   1555  2.65  
LINK         OXT ASN C 215                ZN    ZN A 301     1555   1555  1.98  
LINK         O   ASN D 215                ZN    ZN B 301     1555   1555  1.96  
LINK        CA    CA A 304                 O   HOH A 498     1555   1555  2.51  
LINK        CA    CA A 304                 O   HOH A 525     1555   1555  2.34  
LINK        CA    CA A 305                 O   HOH A 418     1555   1555  2.45  
LINK        CA    CA A 305                 O   HOH A 434     1555   1555  2.37  
LINK        CA    CA B 304                 O   HOH B 492     1555   1555  2.30  
LINK        CA    CA B 304                 O   HOH B 496     1555   1555  2.48  
LINK        CA    CA B 305                 O   HOH B 431     1555   1555  2.45  
LINK        CA    CA B 305                 O   HOH B 418     1555   1555  2.50  
SITE     1 AC1  4 HIS A 222  HIS A 226  HIS A 232  ASN C 215                    
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  5 ASP A 128  ASP A 203  GLU A 205  HOH A 498                    
SITE     2 AC4  5 HOH A 525                                                     
SITE     1 AC5  6 ASP A 162  ASN A 194  GLY A 196  ASP A 198                    
SITE     2 AC5  6 HOH A 418  HOH A 434                                          
SITE     1 AC6 19 GLY A 183  LEU A 184  LEU A 185  HIS A 222                    
SITE     2 AC6 19 GLU A 223  LEU A 239  PHE A 241  PRO A 242                    
SITE     3 AC6 19 ILE A 243  TYR A 244  THR A 245  THR A 247                    
SITE     4 AC6 19 PRO A 255  HOH A 474  PHE B 241  PRO B 242                    
SITE     5 AC6 19 ILE B 243  8OA B 306  ASN C 215                               
SITE     1 AC7  4 HIS B 222  HIS B 226  HIS B 232  ASN D 215                    
SITE     1 AC8  4 HIS B 172  ASP B 174  HIS B 187  HIS B 200                    
SITE     1 AC9  6 ASP B 179  GLY B 180  SER B 182  LEU B 184                    
SITE     2 AC9  6 ASP B 202  GLU B 205                                          
SITE     1 AD1  5 ASP B 128  ASP B 203  GLU B 205  HOH B 492                    
SITE     2 AD1  5 HOH B 496                                                     
SITE     1 AD2  6 ASP B 162  ASN B 194  GLY B 196  ASP B 198                    
SITE     2 AD2  6 HOH B 418  HOH B 431                                          
SITE     1 AD3 17 8OA A 306  LEU B 184  LEU B 185  LEU B 218                    
SITE     2 AD3 17 HIS B 222  GLU B 223  GLY B 237  LEU B 239                    
SITE     3 AD3 17 PHE B 241  PRO B 242  ILE B 243  TYR B 244                    
SITE     4 AD3 17 THR B 245  HOH B 454  HOH B 465  HOH C 305                    
SITE     5 AD3 17 ASN D 215                                                     
CRYST1  140.073  140.073   46.860  90.00  90.00 120.00 H 3          18          
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      0.007139  0.004122  0.000000        0.00000                         
SCALE2      0.000000  0.008244  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021340        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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