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Database: PDB
Entry: 1YOU
LinkDB: 1YOU
Original site: 1YOU 
HEADER    HYDROLASE                               28-JAN-05   1YOU              
TITLE     CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF MMP-13 COMPLEXED WITH A  
TITLE    2 POTENT PYRIMIDINETRIONE INHIBITOR                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COLLAGENASE 3;                                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: MMP-13 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 GENE: MMP13;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE, METALLOPROTEASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.PANDIT                                                              
REVDAT   3   13-JUL-11 1YOU    1       VERSN                                    
REVDAT   2   24-FEB-09 1YOU    1       VERSN                                    
REVDAT   1   15-MAR-05 1YOU    0                                                
JRNL        AUTH   J.A.BLAGG,M.C.NOE,L.A.WOLF-GOUVEIA,L.A.REITER,E.R.LAIRD,     
JRNL        AUTH 2 S.P.CHANG,D.E.DANLEY,J.T.DOWNS,N.C.ELLIOTT,J.D.ESKRA,        
JRNL        AUTH 3 R.J.GRIFFITHS,J.R.HARDINK,A.I.HAUGETO,C.S.JONES,J.L.LIRAS,   
JRNL        AUTH 4 L.L.LOPRESTI-MORROW,P.G.MITCHELL,J.PANDIT,R.P.ROBINSON,      
JRNL        AUTH 5 C.SUBRAMANYAM,M.L.VAUGHN-BOWSER,S.A.YOCUM                    
JRNL        TITL   POTENT PYRIMIDINETRIONE-BASED INHIBITORS OF MMP-13 WITH      
JRNL        TITL 2 ENHANCED SELECTIVITY OVER MMP-14.                            
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  15  1807 2005              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   15780611                                                     
JRNL        DOI    10.1016/J.BMCL.2005.02.038                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 12847                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.295                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1080                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 664                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 67.95                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 59                           
REMARK   3   BIN FREE R VALUE                    : 0.3290                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2637                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 79                                      
REMARK   3   SOLVENT ATOMS            : 17                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.24000                                             
REMARK   3    B22 (A**2) : 1.07000                                              
REMARK   3    B33 (A**2) : -0.83000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.600         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.327         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.220         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.881         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.923                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.847                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2806 ; 0.022 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3822 ; 2.064 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   331 ; 7.984 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   131 ;38.600 ;23.969       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   394 ;19.781 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;14.044 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   376 ; 0.157 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2224 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1222 ; 0.233 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1811 ; 0.321 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    89 ; 0.177 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    18 ; 0.140 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    68 ; 0.317 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.219 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1702 ; 1.042 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2659 ; 1.726 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1308 ; 2.696 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1163 ; 3.485 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 3                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    112       A     173      4                      
REMARK   3           1     B    112       B     173      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    510 ;  0.35 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    510 ;  1.36 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    176       A     247      4                      
REMARK   3           1     B    176       B     247      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    556 ;  0.31 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    556 ;  1.50 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    252       A     268      4                      
REMARK   3           1     B    252       B     268      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    A    (A):    129 ;  0.36 ;  0.50           
REMARK   3   MEDIUM THERMAL     3    A (A**2):    129 ;  1.68 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1YOU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB031762.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15989                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.060                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 830C                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       40.54450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.11150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.54450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.11150            
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, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 12180 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 29030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -298.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       81.08900            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      108.22300            
REMARK 350   BIOMT3   2  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     GLY B   269                                                      
REMARK 465     ASP B   270                                                      
REMARK 465     GLU B   271                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 250    OG                                                  
REMARK 470     MET A 253    CG   SD   CE                                        
REMARK 470     LYS B 249    CB   CG   CD   CE   NZ                              
REMARK 470     SER B 250    OG                                                  
REMARK 470     HIS B 251    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 470     MET B 253    CG   SD   CE                                        
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    PHE A   175     OH   TYR B   195              2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 193   C   -  N   -  CA  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    PRO B 108   C   -  N   -  CA  ANGL. DEV. =  10.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 109      157.56     77.96                                   
REMARK 500    THR A 110       86.52   -162.23                                   
REMARK 500    LYS A 170     -141.35     49.20                                   
REMARK 500    PHE A 175       19.80     57.72                                   
REMARK 500    SER A 182     -164.06     63.79                                   
REMARK 500    ASN A 194     -112.35     57.91                                   
REMARK 500    ASP A 202      101.54    -57.76                                   
REMARK 500    SER A 210     -154.97   -129.18                                   
REMARK 500    PRO A 242       39.14    -75.16                                   
REMARK 500    LYS A 249      -65.37    -20.65                                   
REMARK 500    ASN B 105      117.53     88.41                                   
REMARK 500    ARG B 109      -46.86      6.85                                   
REMARK 500    THR B 110      150.28    178.18                                   
REMARK 500    VAL B 144      -48.83    -28.85                                   
REMARK 500    LYS B 170     -134.49     59.08                                   
REMARK 500    TYR B 176       64.63   -115.03                                   
REMARK 500    SER B 182     -164.87     54.97                                   
REMARK 500    ASN B 194     -109.29     72.69                                   
REMARK 500    SER B 210     -110.68   -122.64                                   
REMARK 500    PRO B 242       20.54    -77.49                                   
REMARK 500    THR B 247      -43.70   -147.90                                   
REMARK 500    SER B 250      -89.03      3.68                                   
REMARK 500    HIS B 251       55.40   -104.07                                   
REMARK 500    LEU B 254      113.46    -36.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO B  108     ARG B  109                  137.62                    
REMARK 500 LYS B  249     SER B  250                  147.57                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN A 105        24.5      L          L   OUTSIDE RANGE           
REMARK 500    THR A 247        23.4      L          L   OUTSIDE RANGE           
REMARK 500    LYS A 249        25.0      L          L   OUTSIDE RANGE           
REMARK 500    ASN B 105        23.8      L          L   OUTSIDE RANGE           
REMARK 500    PHE B 252        16.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 232   NE2                                                    
REMARK 620 2 HIS A 222   NE2 112.1                                              
REMARK 620 3 HIS A 226   NE2  82.4 102.7                                        
REMARK 620 4 PFD A 998   N9  124.5 107.8 124.1                                  
REMARK 620 N                    1     2     3                                   
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 HIS A 200   ND1 104.3                                              
REMARK 620 3 HIS A 187   NE2 113.3 113.9                                        
REMARK 620 4 ASP A 174   OD2 114.8  97.9 111.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 180   O                                                      
REMARK 620 2 GLU A 205   OE2  96.6                                              
REMARK 620 3 ASP A 202   OD2  91.0  89.9                                        
REMARK 620 4 LEU A 184   O   174.1  87.7  93.0                                  
REMARK 620 5 ASP A 179   OD1  79.3 175.7  91.5  96.3                            
REMARK 620 6 SER A 182   O    86.5  92.5 176.7  89.3  85.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 232   NE2                                                    
REMARK 620 2 HIS B 226   NE2  95.1                                              
REMARK 620 3 HIS B 222   NE2 109.6 101.4                                        
REMARK 620 4 PFD B 999   N9  109.2 134.6 105.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 304  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 172   NE2                                                    
REMARK 620 2 HIS B 200   ND1  90.8                                              
REMARK 620 3 HIS B 187   NE2 123.0 113.5                                        
REMARK 620 4 ASP B 174   OD2 112.2 106.3 108.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 403  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B 180   O                                                      
REMARK 620 2 LEU B 184   O   173.1                                              
REMARK 620 3 ASP B 202   OD2  85.5  96.6                                        
REMARK 620 4 GLU B 205   OE2  99.7  87.0  88.0                                  
REMARK 620 5 SER B 182   O    89.6  89.3 169.9  84.1                            
REMARK 620 6 ASP B 179   OD1  96.7  76.5 101.0 161.9  88.4                      
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 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 ZN B 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PFD A 998                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PFD B 999                 
DBREF  1YOU A  104   271  UNP    P45452   MMP13_HUMAN    104    271             
DBREF  1YOU B  104   271  UNP    P45452   MMP13_HUMAN    104    271             
SEQRES   1 A  168  TYR ASN VAL PHE PRO ARG THR LEU LYS TRP SER LYS MET          
SEQRES   2 A  168  ASN LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP MET          
SEQRES   3 A  168  THR HIS SER GLU VAL GLU LYS ALA PHE LYS LYS ALA PHE          
SEQRES   4 A  168  LYS VAL TRP SER ASP VAL THR PRO LEU ASN PHE THR ARG          
SEQRES   5 A  168  LEU HIS ASP GLY ILE ALA ASP ILE MET ILE SER PHE GLY          
SEQRES   6 A  168  ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO          
SEQRES   7 A  168  SER GLY LEU LEU ALA HIS ALA PHE PRO PRO GLY PRO ASN          
SEQRES   8 A  168  TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP GLU THR TRP          
SEQRES   9 A  168  THR SER SER SER LYS GLY TYR ASN LEU PHE LEU VAL ALA          
SEQRES  10 A  168  ALA HIS GLU PHE GLY HIS SER LEU GLY LEU ASP HIS SER          
SEQRES  11 A  168  LYS ASP PRO GLY ALA LEU MET PHE PRO ILE TYR THR TYR          
SEQRES  12 A  168  THR GLY LYS SER HIS PHE MET LEU PRO ASP ASP ASP VAL          
SEQRES  13 A  168  GLN GLY ILE GLN SER LEU TYR GLY PRO GLY ASP GLU              
SEQRES   1 B  168  TYR ASN VAL PHE PRO ARG THR LEU LYS TRP SER LYS MET          
SEQRES   2 B  168  ASN LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP MET          
SEQRES   3 B  168  THR HIS SER GLU VAL GLU LYS ALA PHE LYS LYS ALA PHE          
SEQRES   4 B  168  LYS VAL TRP SER ASP VAL THR PRO LEU ASN PHE THR ARG          
SEQRES   5 B  168  LEU HIS ASP GLY ILE ALA ASP ILE MET ILE SER PHE GLY          
SEQRES   6 B  168  ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO          
SEQRES   7 B  168  SER GLY LEU LEU ALA HIS ALA PHE PRO PRO GLY PRO ASN          
SEQRES   8 B  168  TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP GLU THR TRP          
SEQRES   9 B  168  THR SER SER SER LYS GLY TYR ASN LEU PHE LEU VAL ALA          
SEQRES  10 B  168  ALA HIS GLU PHE GLY HIS SER LEU GLY LEU ASP HIS SER          
SEQRES  11 B  168  LYS ASP PRO GLY ALA LEU MET PHE PRO ILE TYR THR TYR          
SEQRES  12 B  168  THR GLY LYS SER HIS PHE MET LEU PRO ASP ASP ASP VAL          
SEQRES  13 B  168  GLN GLY ILE GLN SER LEU TYR GLY PRO GLY ASP GLU              
HET     ZN  A 301       1                                                       
HET     ZN  A 302       1                                                       
HET     ZN  B 303       1                                                       
HET     ZN  B 304       1                                                       
HET     CA  A 401       1                                                       
HET     CA  B 403       1                                                       
HET    SO4  A 501       5                                                       
HET    SO4  A 502       5                                                       
HET    SO4  B 503       5                                                       
HET    PFD  A 998      29                                                       
HET    PFD  B 999      29                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PFD 5-(2-ETHOXYETHYL)-5-[4-(4-FLUOROPHENOXY)                         
HETNAM   2 PFD  PHENOXY]PYRIMIDINE-2,4,6(1H,3H,5H)-TRIONE                       
FORMUL   3   ZN    4(ZN 2+)                                                     
FORMUL   7   CA    2(CA 2+)                                                     
FORMUL   9  SO4    3(O4 S 2-)                                                   
FORMUL  12  PFD    2(C20 H19 F N2 O6)                                           
FORMUL  14  HOH   *17(H2 O)                                                     
HELIX    1   1 THR A  130  ASP A  147  1                                  18    
HELIX    2   2 LEU A  216  LEU A  228  1                                  13    
HELIX    3   3 GLY A  248  PHE A  252  5                                   5    
HELIX    4   4 PRO A  255  GLY A  267  1                                  13    
HELIX    5   5 THR B  130  ASP B  147  1                                  18    
HELIX    6   6 LEU B  216  LEU B  228  1                                  13    
HELIX    7   7 GLY B  248  PHE B  252  5                                   5    
HELIX    8   8 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  THR A 154           
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  LEU B 156  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  GLY B 168           
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 A 301                 NE2 HIS A 232     1555   1555  2.09  
LINK        ZN    ZN A 302                 NE2 HIS A 172     1555   1555  2.06  
LINK        CA    CA A 401                 O   GLY A 180     1555   1555  2.29  
LINK        ZN    ZN B 303                 NE2 HIS B 232     1555   1555  2.02  
LINK        ZN    ZN B 304                 NE2 HIS B 172     1555   1555  1.89  
LINK        CA    CA B 403                 O   GLY B 180     1555   1555  2.23  
LINK        ZN    ZN A 301                 NE2 HIS A 222     1555   1555  2.11  
LINK        ZN    ZN A 301                 NE2 HIS A 226     1555   1555  2.41  
LINK        ZN    ZN A 301                 N9  PFD A 998     1555   1555  2.11  
LINK        ZN    ZN A 302                 ND1 HIS A 200     1555   1555  1.90  
LINK        ZN    ZN A 302                 NE2 HIS A 187     1555   1555  2.06  
LINK        ZN    ZN A 302                 OD2 ASP A 174     1555   1555  1.99  
LINK        CA    CA A 401                 OE2 GLU A 205     1555   1555  2.21  
LINK        CA    CA A 401                 OD2 ASP A 202     1555   1555  2.39  
LINK        CA    CA A 401                 O   LEU A 184     1555   1555  2.19  
LINK        CA    CA A 401                 OD1 ASP A 179     1555   1555  2.33  
LINK        CA    CA A 401                 O   SER A 182     1555   1555  2.31  
LINK        ZN    ZN B 303                 NE2 HIS B 226     1555   1555  2.03  
LINK        ZN    ZN B 303                 NE2 HIS B 222     1555   1555  2.28  
LINK        ZN    ZN B 303                 N9  PFD B 999     1555   1555  2.10  
LINK        ZN    ZN B 304                 ND1 HIS B 200     1555   1555  2.05  
LINK        ZN    ZN B 304                 NE2 HIS B 187     1555   1555  2.12  
LINK        ZN    ZN B 304                 OD2 ASP B 174     1555   1555  1.93  
LINK        CA    CA B 403                 O   LEU B 184     1555   1555  2.45  
LINK        CA    CA B 403                 OD2 ASP B 202     1555   1555  2.21  
LINK        CA    CA B 403                 OE2 GLU B 205     1555   1555  2.20  
LINK        CA    CA B 403                 O   SER B 182     1555   1555  2.47  
LINK        CA    CA B 403                 OD1 ASP B 179     1555   1555  2.26  
SITE     1 AC1  4 HIS A 222  HIS A 226  HIS A 232  PFD A 998                    
SITE     1 AC2  4 HIS A 172  ASP A 174  HIS A 187  HIS A 200                    
SITE     1 AC3  4 HIS B 222  HIS B 226  HIS B 232  PFD B 999                    
SITE     1 AC4  4 HIS B 172  ASP B 174  HIS B 187  HIS B 200                    
SITE     1 AC5  6 ASP A 179  GLY A 180  SER A 182  LEU A 184                    
SITE     2 AC5  6 ASP A 202  GLU A 205                                          
SITE     1 AC6  6 ASP B 179  GLY B 180  SER B 182  LEU B 184                    
SITE     2 AC6  6 ASP B 202  GLU B 205                                          
SITE     1 AC7  4 THR A 130  HIS A 131  THR B 130  HIS B 131                    
SITE     1 AC8  3 LYS A 115  MET A 116  ASN A 117                               
SITE     1 AC9  4 LYS B 115  MET B 116  ASN B 117  LYS B 234                    
SITE     1 BC1 14 LEU A 184  LEU A 185  ALA A 186  HIS A 222                    
SITE     2 BC1 14 GLU A 223  HIS A 226  HIS A 232  LEU A 239                    
SITE     3 BC1 14 PHE A 241  PRO A 242  ILE A 243  TYR A 244                    
SITE     4 BC1 14 THR A 245   ZN A 301                                          
SITE     1 BC2 15 LEU B 184  LEU B 185  ALA B 186  VAL B 219                    
SITE     2 BC2 15 HIS B 222  GLU B 223  HIS B 226  HIS B 232                    
SITE     3 BC2 15 LEU B 239  PHE B 241  PRO B 242  ILE B 243                    
SITE     4 BC2 15 TYR B 244  THR B 245   ZN B 303                               
CRYST1   81.089  108.223   36.035  90.00  90.00  90.00 P 21 21 2     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      0.012332  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009240  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.027751        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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