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Database: PDB
Entry: 5UE3
LinkDB: 5UE3
Original site: 5UE3 
HEADER    HYDROLASE                               29-DEC-16   5UE3              
TITLE     PROMMP-9DESFNII                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MATRIX METALLOPROTEINASE-9;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MMP-9,92 KDA GELATINASE,92 KDA TYPE IV COLLAGENASE,         
COMPND   5 GELATINASE B,GELB,MMP-9,92 KDA GELATINASE,92 KDA TYPE IV COLLAGENASE,
COMPND   6 GELATINASE B,GELB;                                                   
COMPND   7 EC: 3.4.24.35;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MMP9, CLG4B;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROMMP9, ZYMOGEN, HYDROLASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.S.ALEXANDER,J.SPURLINO,C.MILLIGAN                                   
REVDAT   2   08-NOV-17 5UE3    1       JRNL                                     
REVDAT   1   13-SEP-17 5UE3    0                                                
JRNL        AUTH   R.H.SCANNEVIN,R.ALEXANDER,T.M.HAARLANDER,S.L.BURKE,M.SINGER, 
JRNL        AUTH 2 C.HUO,Y.M.ZHANG,D.MAGUIRE,J.SPURLINO,I.DECKMAN,K.I.CARROLL,  
JRNL        AUTH 3 F.LEWANDOWSKI,E.DEVINE,K.DZORDZORME,B.TOUNGE,C.MILLIGAN,     
JRNL        AUTH 4 S.BAYOUMY,R.WILLIAMS,C.SCHALK-HIHI,K.LEONARD,P.JACKSON,      
JRNL        AUTH 5 M.TODD,L.C.KUO,K.J.RHODES                                    
JRNL        TITL   DISCOVERY OF A HIGHLY SELECTIVE CHEMICAL INHIBITOR OF MATRIX 
JRNL        TITL 2 METALLOPROTEINASE-9 (MMP-9) THAT ALLOSTERICALLY INHIBITS     
JRNL        TITL 3 ZYMOGEN ACTIVATION.                                          
JRNL        REF    J. BIOL. CHEM.                V. 292 17963 2017              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   28860188                                                     
JRNL        DOI    10.1074/JBC.M117.806075                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 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) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.84                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 62702                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.158                           
REMARK   3   R VALUE            (WORKING SET) : 0.155                           
REMARK   3   FREE R VALUE                     : 0.184                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.120                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 6345                            
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 32.8469 -  4.9635    0.92     1839   187  0.1906 0.2186        
REMARK   3     2  4.9635 -  3.9418    0.98     1886   225  0.1381 0.1647        
REMARK   3     3  3.9418 -  3.4441    0.98     1877   217  0.1524 0.1543        
REMARK   3     4  3.4441 -  3.1295    0.99     1905   231  0.1533 0.1794        
REMARK   3     5  3.1295 -  2.9053    0.99     1896   237  0.1585 0.1835        
REMARK   3     6  2.9053 -  2.7341    0.99     1912   210  0.1598 0.2041        
REMARK   3     7  2.7341 -  2.5973    0.99     1915   201  0.1599 0.1987        
REMARK   3     8  2.5973 -  2.4842    0.99     1947   206  0.1645 0.1842        
REMARK   3     9  2.4842 -  2.3886    0.99     1876   230  0.1575 0.1662        
REMARK   3    10  2.3886 -  2.3062    0.99     1897   217  0.1601 0.2092        
REMARK   3    11  2.3062 -  2.2341    0.99     1906   204  0.1497 0.1802        
REMARK   3    12  2.2341 -  2.1703    0.99     1911   204  0.1454 0.1677        
REMARK   3    13  2.1703 -  2.1132    0.99     1900   210  0.1427 0.1791        
REMARK   3    14  2.1132 -  2.0616    0.99     1886   224  0.1525 0.1805        
REMARK   3    15  2.0616 -  2.0148    0.98     1863   190  0.1430 0.1639        
REMARK   3    16  2.0148 -  1.9719    0.98     1910   205  0.1383 0.1599        
REMARK   3    17  1.9719 -  1.9325    0.98     1840   227  0.1434 0.1726        
REMARK   3    18  1.9325 -  1.8960    0.98     1908   216  0.1489 0.2023        
REMARK   3    19  1.8960 -  1.8621    0.98     1853   217  0.1565 0.2171        
REMARK   3    20  1.8621 -  1.8306    0.98     1857   220  0.1595 0.1981        
REMARK   3    21  1.8306 -  1.8010    0.98     1865   209  0.1470 0.1862        
REMARK   3    22  1.8010 -  1.7733    0.98     1851   226  0.1444 0.2011        
REMARK   3    23  1.7733 -  1.7473    0.97     1879   180  0.1470 0.1951        
REMARK   3    24  1.7473 -  1.7226    0.97     1854   210  0.1501 0.1973        
REMARK   3    25  1.7226 -  1.6994    0.98     1858   227  0.1475 0.1884        
REMARK   3    26  1.6994 -  1.6773    0.98     1886   212  0.1583 0.2051        
REMARK   3    27  1.6773 -  1.6563    0.97     1828   197  0.1594 0.2020        
REMARK   3    28  1.6563 -  1.6364    0.97     1879   223  0.1636 0.1974        
REMARK   3    29  1.6364 -  1.6174    0.97     1820   199  0.1649 0.1917        
REMARK   3    30  1.6174 -  1.5992    0.94     1853   184  0.1689 0.2139        
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)     : 0.130            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.400           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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      :  0.011           3738                                  
REMARK   3   ANGLE     :  1.240           5094                                  
REMARK   3   CHIRALITY :  0.071            519                                  
REMARK   3   PLANARITY :  0.009            667                                  
REMARK   3   DIHEDRAL  : 13.095           2155                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 41 THROUGH 94 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   8.4138  29.3092  19.5053              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1133 T22:   0.1400                                     
REMARK   3      T33:   0.1099 T12:  -0.0269                                     
REMARK   3      T13:   0.0432 T23:  -0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8753 L22:   2.5143                                     
REMARK   3      L33:   2.0749 L12:   0.2570                                     
REMARK   3      L13:   0.4018 L23:   0.7760                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1299 S12:  -0.1643 S13:   0.2730                       
REMARK   3      S21:   0.2133 S22:  -0.1576 S23:   0.1917                       
REMARK   3      S31:  -0.1017 S32:  -0.0697 S33:   0.0104                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 95 THROUGH 443 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  27.6600  20.3126   7.2373              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0730 T22:   0.0980                                     
REMARK   3      T33:   0.0875 T12:   0.0038                                     
REMARK   3      T13:  -0.0032 T23:   0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6820 L22:   1.1130                                     
REMARK   3      L33:   1.2228 L12:   0.0761                                     
REMARK   3      L13:  -0.1577 L23:  -0.0853                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0342 S12:  -0.0119 S13:  -0.0051                       
REMARK   3      S21:   0.0442 S22:  -0.0461 S23:  -0.0491                       
REMARK   3      S31:  -0.0013 S32:   0.1272 S33:   0.0108                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 41 THROUGH 104 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  62.0661  53.3717  40.2322              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2524 T22:   0.2904                                     
REMARK   3      T33:   0.2802 T12:  -0.0341                                     
REMARK   3      T13:   0.1155 T23:  -0.0895                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8172 L22:   1.5553                                     
REMARK   3      L33:   1.6268 L12:  -0.2922                                     
REMARK   3      L13:  -0.6275 L23:  -0.0161                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2275 S12:   0.3403 S13:  -0.2781                       
REMARK   3      S21:  -0.5853 S22:   0.2913 S23:  -0.6429                       
REMARK   3      S31:   0.0863 S32:   0.4719 S33:  -0.0510                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 105 THROUGH 133 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  37.9858  61.4122  48.1476              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0967 T22:   0.1240                                     
REMARK   3      T33:   0.0851 T12:  -0.0149                                     
REMARK   3      T13:  -0.0486 T23:  -0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8611 L22:   2.1365                                     
REMARK   3      L33:   1.6513 L12:  -0.6845                                     
REMARK   3      L13:  -0.6622 L23:  -0.1430                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0183 S12:   0.1164 S13:   0.1167                       
REMARK   3      S21:  -0.1740 S22:   0.0273 S23:   0.1980                       
REMARK   3      S31:  -0.1056 S32:  -0.0685 S33:  -0.0400                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 134 THROUGH 444 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  43.8433  55.6598  52.0088              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0831 T22:   0.0720                                     
REMARK   3      T33:   0.0757 T12:   0.0009                                     
REMARK   3      T13:   0.0022 T23:   0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1342 L22:   1.5396                                     
REMARK   3      L33:   1.5401 L12:   0.2649                                     
REMARK   3      L13:   0.0395 L23:   0.4484                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0338 S12:   0.0592 S13:  -0.0827                       
REMARK   3      S21:  -0.0692 S22:   0.0207 S23:   0.0582                       
REMARK   3      S31:   0.0716 S32:   0.0061 S33:   0.0080                       
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 5UE3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000225721.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
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 : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62722                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.599                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.190                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 3.190                              
REMARK 200  R MERGE                    (I) : 0.04800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.4000                            
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: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 8K 1% GLYCEROL 0.2 M AMMONIUM    
REMARK 280  SULFATE 100 MM NACACODYLATE, PH 5.5, VAPOR DIFFUSION,               
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       45.15000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.60000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       45.15000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       36.60000            
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                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -242.0 KCAL/MOL                       
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   BIOMT1   2 -1.000000  0.000000  0.000000      137.09666            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      148.76982            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000       23.39833            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000       36.60000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000       74.38491            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000      113.69833            
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000       36.60000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000       74.38491            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 S    SO4 A 307  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 665  LIES ON A SPECIAL POSITION.                          
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     LEU A    35                                                      
REMARK 465     ARG A    36                                                      
REMARK 465     THR A    37                                                      
REMARK 465     ASN A    38                                                      
REMARK 465     LEU A    39                                                      
REMARK 465     THR A    40                                                      
REMARK 465     GLY A   269                                                      
REMARK 465     PRO A   270                                                      
REMARK 465     LEU B    35                                                      
REMARK 465     ARG B    36                                                      
REMARK 465     THR B    37                                                      
REMARK 465     ASN B    38                                                      
REMARK 465     LEU B    39                                                      
REMARK 465     THR B    40                                                      
REMARK 465     MET B    60                                                      
REMARK 465     ARG B    61                                                      
REMARK 465     GLY B    62                                                      
REMARK 465     GLU B    63                                                      
REMARK 465     SER B    64                                                      
REMARK 465     LYS B    65                                                      
REMARK 465     SER B    66                                                      
REMARK 465     LEU B    67                                                      
REMARK 465     PRO B   270                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A   46   CG   CD   OE1  OE2                                  
REMARK 480     SER A   64   OG                                                  
REMARK 480     LYS A   65   CD   CE   NZ                                        
REMARK 480     LYS A   92   NZ                                                  
REMARK 480     LYS A  214   CG   CD   CE   NZ                                   
REMARK 480     ARG A  249   CD   NE   CZ   NH1  NH2                             
REMARK 480     ARG B   42   NE   CZ   NH1  NH2                                  
REMARK 480     GLU B   47   CD   OE1  OE2                                       
REMARK 480     ARG B   56   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS B   76   CD   CE   NZ                                        
REMARK 480     LYS B  214   CE   NZ                                             
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   OE2  GLU B   130     O    HOH B   401              2.10            
REMARK 500   O1   TRS B   309     O    HOH B   402              2.10            
REMARK 500   NE2  GLN A    77     O    HOH A   401              2.11            
REMARK 500   NH1  ARG A    42     OE2  GLU A    46              2.11            
REMARK 500   O    HOH A   407     O    HOH A   618              2.17            
REMARK 500   NH2  ARG B   249     O2   SO4 B   308              2.18            
REMARK 500   O    HOH A   528     O    HOH A   556              2.19            
REMARK 500   O    HOH B   402     O    HOH B   403              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   560     O    HOH B   489     3444     2.15            
REMARK 500   O    HOH B   618     O    HOH B   637     2656     2.18            
REMARK 500   O    HOH A   691     O    HOH B   646     2646     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    SER A  64   C   -  N   -  CA  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    MET B 247   CG  -  SD  -  CE  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    GLU A  63       38.16   -143.90                                   
REMARK 500    SER A  64      -36.54    132.06                                   
REMARK 500    LYS A  65      -75.88   -132.47                                   
REMARK 500    ALA A 173     -133.69     47.31                                   
REMARK 500    ASP A 185     -157.79     60.18                                   
REMARK 500    ALA A 189      165.89    179.67                                   
REMARK 500    SER A 211     -158.47   -142.99                                   
REMARK 500    ALA B 173     -128.70     46.11                                   
REMARK 500    TYR B 179       71.35   -118.36                                   
REMARK 500    ASP B 185     -157.41     58.32                                   
REMARK 500    SER B 211     -158.89   -152.44                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 718        DISTANCE =  6.45 ANGSTROMS                       
REMARK 525    HOH B 669        DISTANCE =  5.83 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  99   SG                                                     
REMARK 620 2 HIS A 226   NE2 108.1                                              
REMARK 620 3 HIS A 230   NE2 117.0 105.5                                        
REMARK 620 4 HIS A 236   NE2 115.8 108.7 101.0                                  
REMARK 620 N                    1     2     3                                   
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 165   O                                                      
REMARK 620 2 GLY A 197   O   176.2                                              
REMARK 620 3 GLN A 199   O    97.1  83.8                                        
REMARK 620 4 ASP A 201   OD1  90.5  93.0  98.6                                  
REMARK 620 5 HOH A 412   O    94.9  83.2 160.8  96.2                            
REMARK 620 6 HOH A 485   O    80.8  95.8  82.0 171.3  85.2                      
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 175   NE2                                                    
REMARK 620 2 ASP A 177   OD2 108.9                                              
REMARK 620 3 HIS A 190   NE2 116.3 114.3                                        
REMARK 620 4 HIS A 203   ND1 106.3  94.0 114.6                                  
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 182   OD1                                                    
REMARK 620 2 GLY A 183   O    88.5                                              
REMARK 620 3 ASP A 185   O    88.0  89.4                                        
REMARK 620 4 LEU A 187   O    90.6 179.0  91.2                                  
REMARK 620 5 ASP A 205   OD2  92.3  88.9 178.2  90.6                            
REMARK 620 6 GLU A 208   OE2 172.9  92.0  84.9  88.9  94.8                      
REMARK 620 N                    1     2     3     4     5                       
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 206   OD2                                                    
REMARK 620 2 HOH A 487   O    97.3                                              
REMARK 620 3 HOH A 691   O   111.3 120.5                                        
REMARK 620 N                    1     2                                         
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 CYS B  99   SG                                                     
REMARK 620 2 HIS B 226   NE2 108.3                                              
REMARK 620 3 HIS B 230   NE2 117.3 106.8                                        
REMARK 620 4 HIS B 236   NE2 115.4 108.3 100.1                                  
REMARK 620 N                    1     2     3                                   
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 165   O                                                      
REMARK 620 2 GLY B 197   O   170.1                                              
REMARK 620 3 GLN B 199   O   100.2  85.1                                        
REMARK 620 4 ASP B 201   OD1  92.8  94.7  97.9                                  
REMARK 620 5 HOH B 443   O    78.4  94.2  82.0 171.1                            
REMARK 620 6 HOH B 463   O    86.8  85.8 162.2  98.0  83.4                      
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 175   NE2                                                    
REMARK 620 2 ASP B 177   OD2 110.2                                              
REMARK 620 3 HIS B 190   NE2 115.3 112.3                                        
REMARK 620 4 HIS B 203   ND1 108.3  94.2 114.6                                  
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 182   OD1                                                    
REMARK 620 2 GLY B 183   O    89.3                                              
REMARK 620 3 ASP B 185   O    88.6  89.1                                        
REMARK 620 4 LEU B 187   O    91.1 178.2  89.1                                  
REMARK 620 5 ASP B 205   OD2  92.2  89.4 178.3  92.4                            
REMARK 620 6 GLU B 208   OE2 174.8  92.2  86.5  87.2  92.8                      
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 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 SO4 A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 309                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5UE4   RELATED DB: PDB                                   
DBREF  5UE3 A   35   215  UNP    P14780   MMP9_HUMAN      35    215             
DBREF  5UE3 A  216   270  UNP    P14780   MMP9_HUMAN     391    445             
DBREF  5UE3 B   35   215  UNP    P14780   MMP9_HUMAN      35    215             
DBREF  5UE3 B  216   270  UNP    P14780   MMP9_HUMAN     391    445             
SEQRES   1 A  236  LEU ARG THR ASN LEU THR ASP ARG GLN LEU ALA GLU GLU          
SEQRES   2 A  236  TYR LEU TYR ARG TYR GLY TYR THR ARG VAL ALA GLU MET          
SEQRES   3 A  236  ARG GLY GLU SER LYS SER LEU GLY PRO ALA LEU LEU LEU          
SEQRES   4 A  236  LEU GLN LYS GLN LEU SER LEU PRO GLU THR GLY GLU LEU          
SEQRES   5 A  236  ASP SER ALA THR LEU LYS ALA MET ARG THR PRO ARG CYS          
SEQRES   6 A  236  GLY VAL PRO ASP LEU GLY ARG PHE GLN THR PHE GLU GLY          
SEQRES   7 A  236  ASP LEU LYS TRP HIS HIS HIS ASN ILE THR TYR TRP ILE          
SEQRES   8 A  236  GLN ASN TYR SER GLU ASP LEU PRO ARG ALA VAL ILE ASP          
SEQRES   9 A  236  ASP ALA PHE ALA ARG ALA PHE ALA LEU TRP SER ALA VAL          
SEQRES  10 A  236  THR PRO LEU THR PHE THR ARG VAL TYR SER ARG ASP ALA          
SEQRES  11 A  236  ASP ILE VAL ILE GLN PHE GLY VAL ALA GLU HIS GLY ASP          
SEQRES  12 A  236  GLY TYR PRO PHE ASP GLY LYS ASP GLY LEU LEU ALA HIS          
SEQRES  13 A  236  ALA PHE PRO PRO GLY PRO GLY ILE GLN GLY ASP ALA HIS          
SEQRES  14 A  236  PHE ASP ASP ASP GLU LEU TRP SER LEU GLY LYS GLY GLN          
SEQRES  15 A  236  GLY TYR SER LEU PHE LEU VAL ALA ALA HIS GLU PHE GLY          
SEQRES  16 A  236  HIS ALA LEU GLY LEU ASP HIS SER SER VAL PRO GLU ALA          
SEQRES  17 A  236  LEU MET TYR PRO MET TYR ARG PHE THR GLU GLY PRO PRO          
SEQRES  18 A  236  LEU HIS LYS ASP ASP VAL ASN GLY ILE ARG HIS LEU TYR          
SEQRES  19 A  236  GLY PRO                                                      
SEQRES   1 B  236  LEU ARG THR ASN LEU THR ASP ARG GLN LEU ALA GLU GLU          
SEQRES   2 B  236  TYR LEU TYR ARG TYR GLY TYR THR ARG VAL ALA GLU MET          
SEQRES   3 B  236  ARG GLY GLU SER LYS SER LEU GLY PRO ALA LEU LEU LEU          
SEQRES   4 B  236  LEU GLN LYS GLN LEU SER LEU PRO GLU THR GLY GLU LEU          
SEQRES   5 B  236  ASP SER ALA THR LEU LYS ALA MET ARG THR PRO ARG CYS          
SEQRES   6 B  236  GLY VAL PRO ASP LEU GLY ARG PHE GLN THR PHE GLU GLY          
SEQRES   7 B  236  ASP LEU LYS TRP HIS HIS HIS ASN ILE THR TYR TRP ILE          
SEQRES   8 B  236  GLN ASN TYR SER GLU ASP LEU PRO ARG ALA VAL ILE ASP          
SEQRES   9 B  236  ASP ALA PHE ALA ARG ALA PHE ALA LEU TRP SER ALA VAL          
SEQRES  10 B  236  THR PRO LEU THR PHE THR ARG VAL TYR SER ARG ASP ALA          
SEQRES  11 B  236  ASP ILE VAL ILE GLN PHE GLY VAL ALA GLU HIS GLY ASP          
SEQRES  12 B  236  GLY TYR PRO PHE ASP GLY LYS ASP GLY LEU LEU ALA HIS          
SEQRES  13 B  236  ALA PHE PRO PRO GLY PRO GLY ILE GLN GLY ASP ALA HIS          
SEQRES  14 B  236  PHE ASP ASP ASP GLU LEU TRP SER LEU GLY LYS GLY GLN          
SEQRES  15 B  236  GLY TYR SER LEU PHE LEU VAL ALA ALA HIS GLU PHE GLY          
SEQRES  16 B  236  HIS ALA LEU GLY LEU ASP HIS SER SER VAL PRO GLU ALA          
SEQRES  17 B  236  LEU MET TYR PRO MET TYR ARG PHE THR GLU GLY PRO PRO          
SEQRES  18 B  236  LEU HIS LYS ASP ASP VAL ASN GLY ILE ARG HIS LEU TYR          
SEQRES  19 B  236  GLY PRO                                                      
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    SO4  A 306       5                                                       
HET    SO4  A 307       5                                                       
HET     ZN  B 301       1                                                       
HET     ZN  B 302       1                                                       
HET     CA  B 303       1                                                       
HET     CA  B 304       1                                                       
HET    SO4  B 305       5                                                       
HET    SO4  B 306       5                                                       
HET    SO4  B 307       5                                                       
HET    SO4  B 308       5                                                       
HET    TRS  B 309       8                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   3   ZN    4(ZN 2+)                                                     
FORMUL   5   CA    5(CA 2+)                                                     
FORMUL   8  SO4    6(O4 S 2-)                                                   
FORMUL  18  TRS    C4 H12 N O3 1+                                               
FORMUL  19  HOH   *587(H2 O)                                                    
HELIX    1 AA1 ASP A   41  TYR A   52  1                                  12    
HELIX    2 AA2 GLY A   53  ARG A   61  1                                   9    
HELIX    3 AA3 LEU A   67  SER A   79  1                                  13    
HELIX    4 AA4 ASP A   87  ARG A   95  1                                   9    
HELIX    5 AA5 PRO A  133  ALA A  150  1                                  18    
HELIX    6 AA6 LEU A  220  LEU A  232  1                                  13    
HELIX    7 AA7 HIS A  257  HIS A  266  1                                  10    
HELIX    8 AA8 ARG B   42  TYR B   52  1                                  11    
HELIX    9 AA9 GLY B   53  GLU B   59  1                                   7    
HELIX   10 AB1 PRO B   69  SER B   79  1                                  11    
HELIX   11 AB2 ASP B   87  ARG B   95  1                                   9    
HELIX   12 AB3 PRO B  133  VAL B  151  1                                  19    
HELIX   13 AB4 LEU B  220  LEU B  232  1                                  13    
HELIX   14 AB5 HIS B  257  GLY B  269  1                                  13    
SHEET    1 AA1 5 THR A 155  VAL A 159  0                                        
SHEET    2 AA1 5 ASN A 120  ILE A 125  1  N  TYR A 123   O  VAL A 159           
SHEET    3 AA1 5 ILE A 166  GLY A 171  1  O  ILE A 168   N  TRP A 124           
SHEET    4 AA1 5 ALA A 202  ASP A 205  1  O  PHE A 204   N  GLY A 171           
SHEET    5 AA1 5 ALA A 189  ALA A 191 -1  N  HIS A 190   O  HIS A 203           
SHEET    1 AA2 2 TRP A 210  SER A 211  0                                        
SHEET    2 AA2 2 TYR A 218  SER A 219  1  O  TYR A 218   N  SER A 211           
SHEET    1 AA3 5 THR B 155  VAL B 159  0                                        
SHEET    2 AA3 5 ASN B 120  ILE B 125  1  N  TYR B 123   O  VAL B 159           
SHEET    3 AA3 5 ILE B 166  GLY B 171  1  O  ILE B 168   N  TRP B 124           
SHEET    4 AA3 5 ALA B 202  ASP B 205  1  O  PHE B 204   N  GLY B 171           
SHEET    5 AA3 5 ALA B 189  ALA B 191 -1  N  HIS B 190   O  HIS B 203           
SHEET    1 AA4 2 TRP B 210  SER B 211  0                                        
SHEET    2 AA4 2 TYR B 218  SER B 219  1  O  TYR B 218   N  SER B 211           
LINK         SG  CYS A  99                ZN    ZN A 301     1555   1555  2.26  
LINK         O   ASP A 165                CA    CA A 305     1555   1555  2.37  
LINK         NE2 HIS A 175                ZN    ZN A 302     1555   1555  2.05  
LINK         OD2 ASP A 177                ZN    ZN A 302     1555   1555  1.95  
LINK         OD1 ASP A 182                CA    CA A 303     1555   1555  2.32  
LINK         O   GLY A 183                CA    CA A 303     1555   1555  2.26  
LINK         O   ASP A 185                CA    CA A 303     1555   1555  2.33  
LINK         O   LEU A 187                CA    CA A 303     1555   1555  2.27  
LINK         NE2 HIS A 190                ZN    ZN A 302     1555   1555  2.09  
LINK         O   GLY A 197                CA    CA A 305     1555   1555  2.40  
LINK         O   GLN A 199                CA    CA A 305     1555   1555  2.33  
LINK         OD1 ASP A 201                CA    CA A 305     1555   1555  2.44  
LINK         ND1 HIS A 203                ZN    ZN A 302     1555   1555  2.02  
LINK         OD2 ASP A 205                CA    CA A 303     1555   1555  2.35  
LINK         OD2 ASP A 206                CA    CA A 304     1555   1555  2.64  
LINK         OE2 GLU A 208                CA    CA A 303     1555   1555  2.28  
LINK         NE2 HIS A 226                ZN    ZN A 301     1555   1555  2.05  
LINK         NE2 HIS A 230                ZN    ZN A 301     1555   1555  2.00  
LINK         NE2 HIS A 236                ZN    ZN A 301     1555   1555  2.03  
LINK         SG  CYS B  99                ZN    ZN B 301     1555   1555  2.26  
LINK         O   ASP B 165                CA    CA B 304     1555   1555  2.41  
LINK         NE2 HIS B 175                ZN    ZN B 302     1555   1555  2.01  
LINK         OD2 ASP B 177                ZN    ZN B 302     1555   1555  1.97  
LINK         OD1 ASP B 182                CA    CA B 303     1555   1555  2.32  
LINK         O   GLY B 183                CA    CA B 303     1555   1555  2.21  
LINK         O   ASP B 185                CA    CA B 303     1555   1555  2.33  
LINK         O   LEU B 187                CA    CA B 303     1555   1555  2.29  
LINK         NE2 HIS B 190                ZN    ZN B 302     1555   1555  2.08  
LINK         O   GLY B 197                CA    CA B 304     1555   1555  2.37  
LINK         O   GLN B 199                CA    CA B 304     1555   1555  2.31  
LINK         OD1 ASP B 201                CA    CA B 304     1555   1555  2.46  
LINK         ND1 HIS B 203                ZN    ZN B 302     1555   1555  2.06  
LINK         OD2 ASP B 205                CA    CA B 303     1555   1555  2.32  
LINK         OE2 GLU B 208                CA    CA B 303     1555   1555  2.29  
LINK         NE2 HIS B 226                ZN    ZN B 301     1555   1555  2.05  
LINK         NE2 HIS B 230                ZN    ZN B 301     1555   1555  2.01  
LINK         NE2 HIS B 236                ZN    ZN B 301     1555   1555  2.05  
LINK        CA    CA A 304                 O   HOH A 487     1555   1555  2.81  
LINK        CA    CA A 304                 O   HOH A 691     1555   1555  2.73  
LINK        CA    CA A 305                 O   HOH A 412     1555   1555  2.35  
LINK        CA    CA A 305                 O   HOH A 485     1555   1555  2.32  
LINK        CA    CA B 304                 O   HOH B 443     1555   1555  2.45  
LINK        CA    CA B 304                 O   HOH B 463     1555   1555  2.32  
CISPEP   1 GLU A   63    SER A   64          0         3.74                     
SITE     1 AC1  4 CYS A  99  HIS A 226  HIS A 230  HIS A 236                    
SITE     1 AC2  4 HIS A 175  ASP A 177  HIS A 190  HIS A 203                    
SITE     1 AC3  6 ASP A 182  GLY A 183  ASP A 185  LEU A 187                    
SITE     2 AC3  6 ASP A 205  GLU A 208                                          
SITE     1 AC4  5 SER A 129  GLU A 130  ASP A 206  HOH A 487                    
SITE     2 AC4  5 HOH A 691                                                     
SITE     1 AC5  6 ASP A 165  GLY A 197  GLN A 199  ASP A 201                    
SITE     2 AC5  6 HOH A 412  HOH A 485                                          
SITE     1 AC6  6 TRP A 116  HIS A 117  HIS A 118  HOH A 423                    
SITE     2 AC6  6 HOH A 469  HOH A 583                                          
SITE     1 AC7  4 HIS A 118  HIS A 119  ASN A 120  HOH A 512                    
SITE     1 AC8  4 CYS B  99  HIS B 226  HIS B 230  HIS B 236                    
SITE     1 AC9  4 HIS B 175  ASP B 177  HIS B 190  HIS B 203                    
SITE     1 AD1  6 ASP B 182  GLY B 183  ASP B 185  LEU B 187                    
SITE     2 AD1  6 ASP B 205  GLU B 208                                          
SITE     1 AD2  6 ASP B 165  GLY B 197  GLN B 199  ASP B 201                    
SITE     2 AD2  6 HOH B 443  HOH B 463                                          
SITE     1 AD3  8 TRP B 116  HIS B 117  HIS B 118  HOH B 435                    
SITE     2 AD3  8 HOH B 456  HOH B 457  HOH B 517  HOH B 593                    
SITE     1 AD4 10 GLY A 105  ARG A 106  SER B 211  GLY B 215                    
SITE     2 AD4 10 GLN B 216  GLY B 217  HOH B 493  HOH B 501                    
SITE     3 AD4 10 HOH B 522  HOH B 563                                          
SITE     1 AD5  4 ASP B 103  LEU B 104  GLY B 105  ASP B 235                    
SITE     1 AD6  8 GLU B 241  ARG B 249  THR B 251  HIS B 257                    
SITE     2 AD6  8 HOH B 408  HOH B 414  HOH B 415  HOH B 440                    
SITE     1 AD7 11 LEU B 222  VAL B 223  HIS B 226  LEU B 243                    
SITE     2 AD7 11 MET B 247  TYR B 248  ARG B 249  HOH B 402                    
SITE     3 AD7 11 HOH B 429  HOH B 475  HOH B 482                               
CRYST1   90.300   73.200   77.500  90.00 106.30  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011074  0.000000  0.003238        0.00000                         
SCALE2      0.000000  0.013661  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013444        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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