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Database: PDB
Entry: 4JIJ
LinkDB: 4JIJ
Original site: 4JIJ 
HEADER    HYDROLASE/SUBSTRATE                     06-MAR-13   4JIJ              
TITLE     CRYSTAL STRUCTURE OF AN INACTIVE MUTANT OF MMP-9 CATALYTIC DOMAIN IN  
TITLE    2 COMPLEX WITH A FLUOROGENIC SYNTHETIC PEPTIDIC SUBSTRATE              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FLUOROGENIC PEPTIDIC SUBSTRATE (8MC)PLG(PHI)(DNW)AR(NH2);  
COMPND   3 CHAIN: P, Q;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: MATRIX METALLOPROTEINASE-9;                                
COMPND   7 CHAIN: A, B;                                                         
COMPND   8 SYNONYM: MMP-9, 92 KDA GELATINASE, 92 KDA TYPE IV COLLAGENASE,       
COMPND   9 GELATINASE B, GELB, 67 KDA MATRIX METALLOPROTEINASE-9, 82 KDA MATRIX 
COMPND  10 METALLOPROTEINASE-9;                                                 
COMPND  11 EC: 3.4.24.35;                                                       
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 OTHER_DETAILS: FLUOROGENIC SYNTHETIC L-PEPTIDE SUBSTRATE WITH MMP-9  
SOURCE   4 SPECIFICITY.;                                                        
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 GENE: CLG4B, MMP9;                                                   
SOURCE  10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  12 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3 STAR);                           
SOURCE  13 EXPRESSION_SYSTEM_VECTOR_TYPE: PT7 PROMOTER;                         
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PET-14B                                   
KEYWDS    HYDROLASE SUBSTRATE COMPLEX, ZINCIN-LIKE, GELATINASE, COLLAGENASE,    
KEYWDS   2 CATALYTIC DOMAIN, HYDROLASE-SUBSTRATE COMPLEX                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.A.STURA,L.VERA,E.CASSAR-LAJEUNESSE,I.TRANCHANT,M.AMOURA,V.DIVE      
REVDAT   3   16-AUG-17 4JIJ    1       SOURCE REMARK                            
REVDAT   2   16-APR-14 4JIJ    1       JRNL                                     
REVDAT   1   12-MAR-14 4JIJ    0                                                
JRNL        AUTH   I.TRANCHANT,L.VERA,B.CZARNY,M.AMOURA,E.CASSAR,F.BEAU,        
JRNL        AUTH 2 E.A.STURA,V.DIVE                                             
JRNL        TITL   HALOGEN BONDING CONTROLS SELECTIVITY OF FRET SUBSTRATE       
JRNL        TITL 2 PROBES FOR MMP-9.                                            
JRNL        REF    CHEM.BIOL.                    V.  21   408 2014              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   24583051                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2014.01.008                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.57                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.010                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 38419                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1922                            
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 40.5794 -  4.0904    1.00     2825   149  0.1618 0.1802        
REMARK   3     2  4.0904 -  3.2471    1.00     2679   141  0.1385 0.1648        
REMARK   3     3  3.2471 -  2.8368    1.00     2636   139  0.1641 0.2347        
REMARK   3     4  2.8368 -  2.5775    1.00     2635   139  0.1620 0.2250        
REMARK   3     5  2.5775 -  2.3927    1.00     2587   136  0.1567 0.1886        
REMARK   3     6  2.3927 -  2.2517    1.00     2609   137  0.1518 0.1881        
REMARK   3     7  2.2517 -  2.1389    1.00     2561   135  0.1478 0.1606        
REMARK   3     8  2.1389 -  2.0458    1.00     2628   138  0.1436 0.1806        
REMARK   3     9  2.0458 -  1.9671    1.00     2575   136  0.1564 0.2036        
REMARK   3    10  1.9671 -  1.8992    1.00     2544   134  0.1579 0.1966        
REMARK   3    11  1.8992 -  1.8398    1.00     2614   138  0.1719 0.2039        
REMARK   3    12  1.8398 -  1.7872    1.00     2545   133  0.1877 0.2247        
REMARK   3    13  1.7872 -  1.7402    1.00     2585   137  0.2031 0.2380        
REMARK   3    14  1.7402 -  1.6977    0.97     2474   130  0.2362 0.2793        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.140            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.180           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.39                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.68                          
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      :  0.006           3047                                  
REMARK   3   ANGLE     :  1.084           4155                                  
REMARK   3   CHIRALITY :  0.080            399                                  
REMARK   3   PLANARITY :  0.006            554                                  
REMARK   3   DIHEDRAL  : 16.904           1043                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4JIJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000078089.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9184                             
REMARK 200  MONOCHROMATOR                  : CHANNEL CUT SI(111)                
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38427                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.698                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 8.970                              
REMARK 200  R MERGE                    (I) : 0.17400                            
REMARK 200  R SYM                      (I) : 0.16800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.9100                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.92                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.05200                            
REMARK 200  R SYM FOR SHELL            (I) : 1.08300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.060                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 4H3X                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 6 MICROL HMMP9(E402A) AT 181    
REMARK 280  MICRO-M 0.12 M ACETOHYDROXAMIC ACID AND 0.3 MICROL IT34-I AT 6.9    
REMARK 280  MILL-M. RESERVOIR: 10% PEG 20K, 0.1 M MMT (L-MALIC ACID, MES,       
REMARK 280  TRIS) 75% ACID/25% BASIC, 0.8 M NACL, 0.02 SRCL2, 0.01% AZIDE.      
REMARK 280  CRYOPROTECTANT: CRYOPROTX CM2, 0.8 M LI FORMATE, 0.1 M (MMT 75%     
REMARK 280  ACID/25% BASIC), 9% PEG 10K, PH 6.0, VAPOR DIFFUSION, SITTING       
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       17.10000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       86.01500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.70000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       86.01500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       17.10000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       28.70000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8700 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -124.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8670 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -124.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, 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 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    ALA A 173     -133.63     46.72                                   
REMARK 500    ALA A 173     -133.12     46.72                                   
REMARK 500    ASP A 185     -159.85     62.29                                   
REMARK 500    LYS A 214      -15.98     81.47                                   
REMARK 500    ALA B 173     -132.60     49.61                                   
REMARK 500    ASP B 185     -159.02     62.34                                   
REMARK 500    LEU B 212      -17.54   -143.11                                   
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 303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 177   OD1                                                    
REMARK 620 2 HIS A 203   ND1  94.2                                              
REMARK 620 3 HIS A 175   NE2 112.8 111.3                                        
REMARK 620 4 HIS A 190   NE2 111.5 113.6 112.3                                  
REMARK 620 N                    1     2     3                                   
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 ASP B 177   OD1                                                    
REMARK 620 2 HIS B 203   ND1  94.9                                              
REMARK 620 3 HIS B 190   NE2 112.1 112.8                                        
REMARK 620 4 HIS B 175   NE2 114.5 109.0 112.4                                  
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 AZI A 301   N3                                                     
REMARK 620 2 HIS A 236   NE2 138.4                                              
REMARK 620 3 HIS A 226   NE2  99.4 112.2                                        
REMARK 620 4 HIS A 230   NE2  94.6 103.9 102.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 236   NE2                                                    
REMARK 620 2 AZI Q 101   N1  135.2                                              
REMARK 620 3 HIS B 230   NE2 103.8  96.9                                        
REMARK 620 4 HIS B 226   NE2 109.6 103.7 102.7                                  
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 GLU B 208   OE2                                                    
REMARK 620 2 GLY B 183   O    93.9                                              
REMARK 620 3 LEU B 187   O    91.3 174.8                                        
REMARK 620 4 ASP B 205   OD2  91.4  89.0  90.0                                  
REMARK 620 5 ASP B 185   O    87.2  86.5  94.6 175.2                            
REMARK 620 6 ASP B 182   OD1 174.4  85.7  89.3  94.2  87.2                      
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 GLY A 183   O                                                      
REMARK 620 2 GLU A 208   OE2  91.0                                              
REMARK 620 3 ASP A 185   O    88.3  85.8                                        
REMARK 620 4 ASP A 205   OD2  87.6  93.8 175.8                                  
REMARK 620 5 LEU A 187   O   177.0  91.2  93.9  90.3                            
REMARK 620 6 ASP A 182   OD1  88.5 175.7  89.9  90.5  89.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              SR B 304  SR                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B 197   O                                                      
REMARK 620 2 ASP B 165   O   162.3                                              
REMARK 620 3 HOH B 451   O    90.1  86.0                                        
REMARK 620 4 HOH B 455   O    71.2 126.4  97.9                                  
REMARK 620 5 ASP B 201   OD1  94.1  85.6 165.0  97.1                            
REMARK 620 6 GLN B 199   O    78.8  83.5  77.7 149.7  89.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              SR A 306  SR                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 208   O                                                      
REMARK 620 2 PGO A 307   O1   87.8                                              
REMARK 620 3 ASP A 206   O    85.8 138.0                                        
REMARK 620 4 PGO A 307   O2   86.9  62.3  75.9                                  
REMARK 620 5 ASP A 131   OD2  73.3  73.8 141.9 132.4                            
REMARK 620 6 HOH A 434   O   164.9  90.0  85.8  78.9 120.4                      
REMARK 620 7 ASP A 206   OD1 102.4 158.0  63.0 136.7  90.3  85.0                
REMARK 620 8 ASP A 131   OD1 116.4  63.4 152.3 119.1  45.6  75.6  94.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              SR A 305  SR                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 165   O                                                      
REMARK 620 2 GLY A 197   O   166.3                                              
REMARK 620 3 HOH A 455   O    84.3  86.9                                        
REMARK 620 4 HOH A 565   O   102.8  84.4  71.8                                  
REMARK 620 5 GLN A 199   O    89.5  78.0  75.1 143.1                            
REMARK 620 6 ASP A 201   OD1  83.4 101.3 158.0 128.9  86.6                      
REMARK 620 7 HOH A 418   O   123.7  69.8 133.3  66.2 133.5  68.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              SR B 305  SR                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 208   O                                                      
REMARK 620 2 ASP B 206   O    85.7                                              
REMARK 620 3 ASP B 131   OD2  74.1 144.3                                        
REMARK 620 4 HOH B 422   O   163.2  85.8 120.2                                  
REMARK 620 5 PGO B 306   O1   90.5 131.4  78.9  84.3                            
REMARK 620 6 ASP B 206   OD1 104.6  67.3  89.3  85.4 157.6                      
REMARK 620 7 PGO B 306   O2   81.8  70.4 132.8  81.7  61.1 136.5                
REMARK 620 8 ASP B 131   OD1 122.4 146.4  49.2  71.0  71.4  86.4 127.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI 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 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 SR A 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SR A 306                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI Q 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SR B 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SR B 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 309                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4H3X   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF AN MMP BROAD SPECTRUM HYDROXAMATE BASED         
REMARK 900 INHIBITOR CC27 IN COMPLEX WITH THE MMP-9 CATALYTIC DOMAIN            
REMARK 900 RELATED ID: 4H1Q   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MUTANT MMP-9 CATALYTIC DOMAIN IN COMPLEX WITH   
REMARK 900 A TWIN INHIBITOR.                                                    
REMARK 900 RELATED ID: 4H2E   RELATED DB: PDB                                   
REMARK 900 CRYSTALCRYSTAL STRUCTURE OF AN MMP TWIN INHIBITOR COMPLEXING TWO     
REMARK 900 MMP-9 CATALYTIC DOMAINS STRUCTURE OF AN MMP TWIN INHIBITOR           
REMARK 900 COMPLEXING TWO MMP-9 CATALYTIC DOMAINS                               
REMARK 900 RELATED ID: 2OW1   RELATED DB: PDB                                   
REMARK 900 MMP-9 ACTIVE SITE MUTANT WITH TRIFLUOROMETHYL HYDROXAMATE INHIBITOR  
REMARK 900 RELATED ID: 2OW0   RELATED DB: PDB                                   
REMARK 900 MMP-9 ACTIVE SITE MUTANT WITH IODINE-LABELED CARBOXYLATE INHIBITOR   
REMARK 900 RELATED ID: 4HMA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF AN MMP TWIN CARBOXYLATE BASED INHIBITOR LC20    
REMARK 900 IN COMPLEX WITH THE MMP-9 CATALYTIC DOMAIN                           
REMARK 900 RELATED ID: 4H82   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MUTANT MMP-9 CATALYTIC DOMAIN IN COMPLEX WITH   
REMARK 900 A TWIN INHIBITOR.                                                    
REMARK 900 RELATED ID: 4JQG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4JXA   RELATED DB: PDB                                   
DBREF  4JIJ A  107   216  UNP    P14780   MMP9_HUMAN     107    216             
DBREF  4JIJ A  217   269  UNP    P14780   MMP9_HUMAN     392    444             
DBREF  4JIJ B  107   216  UNP    P14780   MMP9_HUMAN     107    216             
DBREF  4JIJ B  217   269  UNP    P14780   MMP9_HUMAN     392    444             
DBREF  4JIJ P    1     9  PDB    4JIJ     4JIJ             1      9             
DBREF  4JIJ Q    1     9  PDB    4JIJ     4JIJ             1      9             
SEQADV 4JIJ ALA A  227  UNP  P14780    GLU   402 ENGINEERED MUTATION            
SEQADV 4JIJ ALA B  227  UNP  P14780    GLU   402 ENGINEERED MUTATION            
SEQRES   1 P    9  8MC PRO LEU GLY PHI DNW ALA ARG NH2                          
SEQRES   1 A  164  GLY PHE GLN THR PHE GLU GLY ASP LEU LYS TRP HIS HIS          
SEQRES   2 A  164  HIS ASN ILE THR TYR TRP ILE GLN ASN TYR SER GLU ASP          
SEQRES   3 A  164  LEU PRO ARG ALA VAL ILE ASP ASP ALA PHE ALA ARG ALA          
SEQRES   4 A  164  PHE ALA LEU TRP SER ALA VAL THR PRO LEU THR PHE THR          
SEQRES   5 A  164  ARG VAL TYR SER ARG ASP ALA ASP ILE VAL ILE GLN PHE          
SEQRES   6 A  164  GLY VAL ALA GLU HIS GLY ASP GLY TYR PRO PHE ASP GLY          
SEQRES   7 A  164  LYS ASP GLY LEU LEU ALA HIS ALA PHE PRO PRO GLY PRO          
SEQRES   8 A  164  GLY ILE GLN GLY ASP ALA HIS PHE ASP ASP ASP GLU LEU          
SEQRES   9 A  164  TRP SER LEU GLY LYS GLY VAL GLY TYR SER LEU PHE LEU          
SEQRES  10 A  164  VAL ALA ALA HIS ALA PHE GLY HIS ALA LEU GLY LEU ASP          
SEQRES  11 A  164  HIS SER SER VAL PRO GLU ALA LEU MET TYR PRO MET TYR          
SEQRES  12 A  164  ARG PHE THR GLU GLY PRO PRO LEU HIS LYS ASP ASP VAL          
SEQRES  13 A  164  ASN GLY ILE ARG HIS LEU TYR GLY                              
SEQRES   1 Q    9  8MC PRO LEU GLY PHI DNW ALA ARG NH2                          
SEQRES   1 B  164  GLY PHE GLN THR PHE GLU GLY ASP LEU LYS TRP HIS HIS          
SEQRES   2 B  164  HIS ASN ILE THR TYR TRP ILE GLN ASN TYR SER GLU ASP          
SEQRES   3 B  164  LEU PRO ARG ALA VAL ILE ASP ASP ALA PHE ALA ARG ALA          
SEQRES   4 B  164  PHE ALA LEU TRP SER ALA VAL THR PRO LEU THR PHE THR          
SEQRES   5 B  164  ARG VAL TYR SER ARG ASP ALA ASP ILE VAL ILE GLN PHE          
SEQRES   6 B  164  GLY VAL ALA GLU HIS GLY ASP GLY TYR PRO PHE ASP GLY          
SEQRES   7 B  164  LYS ASP GLY LEU LEU ALA HIS ALA PHE PRO PRO GLY PRO          
SEQRES   8 B  164  GLY ILE GLN GLY ASP ALA HIS PHE ASP ASP ASP GLU LEU          
SEQRES   9 B  164  TRP SER LEU GLY LYS GLY VAL GLY TYR SER LEU PHE LEU          
SEQRES  10 B  164  VAL ALA ALA HIS ALA PHE GLY HIS ALA LEU GLY LEU ASP          
SEQRES  11 B  164  HIS SER SER VAL PRO GLU ALA LEU MET TYR PRO MET TYR          
SEQRES  12 B  164  ARG PHE THR GLU GLY PRO PRO LEU HIS LYS ASP ASP VAL          
SEQRES  13 B  164  ASN GLY ILE ARG HIS LEU TYR GLY                              
MODRES 4JIJ PHI P    5  PHE  IODO-PHENYLALANINE                                 
MODRES 4JIJ DNW P    6  ALA  3-[(2,4-DINITROPHENYL)AMINO]-L-ALANINE             
MODRES 4JIJ PHI Q    5  PHE  IODO-PHENYLALANINE                                 
MODRES 4JIJ DNW Q    6  ALA  3-[(2,4-DINITROPHENYL)AMINO]-L-ALANINE             
HET    8MC  P   1      16                                                       
HET    PHI  P   5      12                                                       
HET    DNW  P   6      18                                                       
HET    NH2  P   9       1                                                       
HET    8MC  Q   1      16                                                       
HET    PHI  Q   5      12                                                       
HET    DNW  Q   6      18                                                       
HET    NH2  Q   9       1                                                       
HET    AZI  A 301       3                                                       
HET     ZN  A 302       1                                                       
HET     ZN  A 303       1                                                       
HET     CA  A 304       1                                                       
HET     SR  A 305       1                                                       
HET     SR  A 306       1                                                       
HET    PGO  A 307       5                                                       
HET    EDO  A 308       4                                                       
HET    EDO  A 309       4                                                       
HET    PEG  A 310       7                                                       
HET    GOL  A 311      12                                                       
HET    AZI  Q 101       3                                                       
HET     ZN  B 301       1                                                       
HET     ZN  B 302       1                                                       
HET     CA  B 303       1                                                       
HET     SR  B 304       1                                                       
HET     SR  B 305       1                                                       
HET    PGO  B 306       5                                                       
HET    EDO  B 307       4                                                       
HET    EDO  B 308       4                                                       
HET    GOL  B 309       6                                                       
HETNAM     8MC (7-METHOXY-2-OXO-2H-CHROMEN-4-YL)ACETIC ACID                     
HETNAM     PHI IODO-PHENYLALANINE                                               
HETNAM     DNW 3-[(2,4-DINITROPHENYL)AMINO]-L-ALANINE                           
HETNAM     NH2 AMINO GROUP                                                      
HETNAM     AZI AZIDE ION                                                        
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM      SR STRONTIUM ION                                                    
HETNAM     PGO S-1,2-PROPANEDIOL                                                
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     GOL GLYCEROL                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  8MC    2(C12 H10 O5)                                                
FORMUL   1  PHI    2(C9 H10 I N O2)                                             
FORMUL   1  DNW    2(C9 H10 N4 O6)                                              
FORMUL   1  NH2    2(H2 N)                                                      
FORMUL   5  AZI    2(N3 1-)                                                     
FORMUL   6   ZN    4(ZN 2+)                                                     
FORMUL   8   CA    2(CA 2+)                                                     
FORMUL   9   SR    4(SR 2+)                                                     
FORMUL  11  PGO    2(C3 H8 O2)                                                  
FORMUL  12  EDO    4(C2 H6 O2)                                                  
FORMUL  14  PEG    C4 H10 O3                                                    
FORMUL  15  GOL    2(C3 H8 O3)                                                  
FORMUL  26  HOH   *410(H2 O)                                                    
HELIX    1   1 PRO A  133  ALA A  150  1                                  18    
HELIX    2   2 LEU A  220  LEU A  232  1                                  13    
HELIX    3   3 HIS A  257  GLY A  269  1                                  13    
HELIX    4   4 PRO B  133  VAL B  151  1                                  19    
HELIX    5   5 LEU B  220  LEU B  232  1                                  13    
HELIX    6   6 HIS B  257  GLY B  269  1                                  13    
SHEET    1   A 6 LEU P   3  DNW P   6  0                                        
SHEET    2   A 6 LEU A 187  ALA A 191 -1  O  LEU A 188   N  PHI P   5           
SHEET    3   A 6 ALA A 202  ASP A 205 -1  O  HIS A 203   N  HIS A 190           
SHEET    4   A 6 ILE A 166  GLY A 171  1  N  GLN A 169   O  PHE A 204           
SHEET    5   A 6 ASN A 120  ILE A 125  1  N  TRP A 124   O  ILE A 168           
SHEET    6   A 6 THR A 155  ARG A 158  1  O  THR A 157   N  ILE A 121           
SHEET    1   B 2 TRP A 210  SER A 211  0                                        
SHEET    2   B 2 TYR A 218  SER A 219  1  O  TYR A 218   N  SER A 211           
SHEET    1   C 6 LEU Q   3  DNW Q   6  0                                        
SHEET    2   C 6 LEU B 187  ALA B 191 -1  O  LEU B 188   N  PHI Q   5           
SHEET    3   C 6 ALA B 202  ASP B 205 -1  O  HIS B 203   N  HIS B 190           
SHEET    4   C 6 ILE B 166  GLY B 171  1  N  GLN B 169   O  PHE B 204           
SHEET    5   C 6 ASN B 120  ILE B 125  1  N  TRP B 124   O  ILE B 168           
SHEET    6   C 6 THR B 155  ARG B 158  1  O  THR B 155   N  ILE B 121           
SHEET    1   D 2 TRP B 210  SER B 211  0                                        
SHEET    2   D 2 TYR B 218  SER B 219  1  O  TYR B 218   N  SER B 211           
LINK         C   GLY P   4                 N   PHI P   5     1555   1555  1.33  
LINK         C   ARG P   8                 N   NH2 P   9     1555   1555  1.33  
LINK         C   GLY Q   4                 N   PHI Q   5     1555   1555  1.33  
LINK         C   ARG Q   8                 N   NH2 Q   9     1555   1555  1.33  
LINK         OD1 ASP A 177                ZN    ZN A 303     1555   1555  1.91  
LINK         OD1 ASP B 177                ZN    ZN B 302     1555   1555  1.96  
LINK         N3  AZI A 301                ZN    ZN A 302     1555   1555  1.98  
LINK         NE2 HIS A 236                ZN    ZN A 302     1555   1555  1.98  
LINK         NE2 HIS B 236                ZN    ZN B 301     1555   1555  2.00  
LINK         ND1 HIS A 203                ZN    ZN A 303     1555   1555  2.01  
LINK         NE2 HIS A 226                ZN    ZN A 302     1555   1555  2.01  
LINK         NE2 HIS A 230                ZN    ZN A 302     1555   1555  2.01  
LINK         N1  AZI Q 101                ZN    ZN B 301     1555   1555  2.02  
LINK         NE2 HIS B 230                ZN    ZN B 301     1555   1555  2.02  
LINK         NE2 HIS A 175                ZN    ZN A 303     1555   1555  2.02  
LINK         NE2 HIS A 190                ZN    ZN A 303     1555   1555  2.03  
LINK         ND1 HIS B 203                ZN    ZN B 302     1555   1555  2.04  
LINK         NE2 HIS B 226                ZN    ZN B 301     1555   1555  2.05  
LINK         NE2 HIS B 190                ZN    ZN B 302     1555   1555  2.05  
LINK         NE2 HIS B 175                ZN    ZN B 302     1555   1555  2.06  
LINK         OE2 GLU B 208                CA    CA B 303     1555   1555  2.14  
LINK         O   GLY A 183                CA    CA A 304     1555   1555  2.23  
LINK         OE2 GLU A 208                CA    CA A 304     1555   1555  2.24  
LINK         O   GLY B 183                CA    CA B 303     1555   1555  2.26  
LINK         O   LEU B 187                CA    CA B 303     1555   1555  2.27  
LINK         OD2 ASP B 205                CA    CA B 303     1555   1555  2.27  
LINK         O   ASP A 185                CA    CA A 304     1555   1555  2.27  
LINK         OD2 ASP A 205                CA    CA A 304     1555   1555  2.29  
LINK         O   LEU A 187                CA    CA A 304     1555   1555  2.30  
LINK         O   ASP B 185                CA    CA B 303     1555   1555  2.32  
LINK         OD1 ASP A 182                CA    CA A 304     1555   1555  2.37  
LINK         O   GLY B 197                SR    SR B 304     1555   1555  2.42  
LINK         O   GLU A 208                SR    SR A 306     1555   1555  2.43  
LINK         OD1 ASP B 182                CA    CA B 303     1555   1555  2.44  
LINK         O   ASP B 165                SR    SR B 304     1555   1555  2.45  
LINK         O   ASP A 165                SR    SR A 305     1555   1555  2.45  
LINK         O   GLY A 197                SR    SR A 305     1555   1555  2.46  
LINK        SR    SR A 306                 O1  PGO A 307     1555   1555  2.47  
LINK        SR    SR B 304                 O   HOH B 451     1555   1555  2.48  
LINK         O   GLU B 208                SR    SR B 305     1555   1555  2.48  
LINK         O   ASP B 206                SR    SR B 305     1555   1555  2.49  
LINK        SR    SR A 305                 O   HOH A 455     1555   1555  2.50  
LINK         O   ASP A 206                SR    SR A 306     1555   1555  2.50  
LINK        SR    SR B 304                 O   HOH B 455     1555   1555  2.50  
LINK         OD1 ASP B 201                SR    SR B 304     1555   1555  2.51  
LINK        SR    SR A 305                 O   HOH A 565     1555   1555  2.53  
LINK         O   GLN A 199                SR    SR A 305     1555   1555  2.54  
LINK         OD2 ASP B 131                SR    SR B 305     1555   1555  2.55  
LINK        SR    SR B 305                 O   HOH B 422     1555   1555  2.55  
LINK        SR    SR A 306                 O2  PGO A 307     1555   1555  2.56  
LINK        SR    SR B 305                 O1  PGO B 306     1555   1555  2.56  
LINK         OD2 ASP A 131                SR    SR A 306     1555   1555  2.56  
LINK         O   GLN B 199                SR    SR B 304     1555   1555  2.56  
LINK         OD1 ASP B 206                SR    SR B 305     1555   1555  2.57  
LINK         OD1 ASP A 201                SR    SR A 305     1555   1555  2.59  
LINK        SR    SR B 305                 O2  PGO B 306     1555   1555  2.61  
LINK        SR    SR A 306                 O   HOH A 434     1555   1555  2.62  
LINK         OD1 ASP A 206                SR    SR A 306     1555   1555  2.70  
LINK         OD1 ASP B 131                SR    SR B 305     1555   1555  2.71  
LINK        SR    SR A 305                 O   HOH A 418     1555   1555  2.71  
LINK         OD1 ASP A 131                SR    SR A 306     1555   1555  2.98  
LINK         C   8MC P   1                 N   PRO P   2     1555   1555  1.34  
LINK         C   8MC Q   1                 N   PRO Q   2     1555   1555  1.34  
LINK         C   PHI P   5                 N   DNW P   6     1555   1555  1.33  
LINK         C   DNW P   6                 N   ALA P   7     1555   1555  1.33  
LINK         C   PHI Q   5                 N   DNW Q   6     1555   1555  1.33  
LINK         C   DNW Q   6                 N   ALA Q   7     1555   1555  1.33  
SITE     1 AC1  9 ALA A 189  HIS A 190  HIS A 226  ALA A 227                    
SITE     2 AC1  9 HIS A 230   ZN A 302  LEU P   3  GLY P   4                    
SITE     3 AC1  9 PHI P   5                                                     
SITE     1 AC2  5 HIS A 226  HIS A 230  HIS A 236  AZI A 301                    
SITE     2 AC2  5 GLY P   4                                                     
SITE     1 AC3  4 HIS A 175  ASP A 177  HIS A 190  HIS A 203                    
SITE     1 AC4  6 ASP A 182  GLY A 183  ASP A 185  LEU A 187                    
SITE     2 AC4  6 ASP A 205  GLU A 208                                          
SITE     1 AC5  7 ASP A 165  GLY A 197  GLN A 199  ASP A 201                    
SITE     2 AC5  7 HOH A 418  HOH A 455  HOH A 565                               
SITE     1 AC6  5 ASP A 131  ASP A 206  GLU A 208  PGO A 307                    
SITE     2 AC6  5 HOH A 434                                                     
SITE     1 AC7 12 ASP A 131  GLY A 197  ASP A 206  ASP A 207                    
SITE     2 AC7 12 GLU A 208  LEU A 209   SR A 306  HOH A 424                    
SITE     3 AC7 12 HOH A 457  HOH A 532  HOH A 551  HOH A 569                    
SITE     1 AC8  5 HIS A 266  GLY A 269  HOH A 539  GLY B 106                    
SITE     2 AC8  5 PHE B 107                                                     
SITE     1 AC9  3 LEU A 187  HIS A 190  HOH A 413                               
SITE     1 BC1  4 VAL A 216  GLY A 217  TYR A 248  HOH A 437                    
SITE     1 BC2  5 LEU A 114  GLY A 233  HOH A 428  HOH A 430                    
SITE     2 BC2  5 HOH A 548                                                     
SITE     1 BC3  9 ALA B 189  HIS B 190  HIS B 226  ALA B 227                    
SITE     2 BC3  9 HIS B 230   ZN B 301  LEU Q   3  GLY Q   4                    
SITE     3 BC3  9 PHI Q   5                                                     
SITE     1 BC4  5 HIS B 226  HIS B 230  HIS B 236  GLY Q   4                    
SITE     2 BC4  5 AZI Q 101                                                     
SITE     1 BC5  4 HIS B 175  ASP B 177  HIS B 190  HIS B 203                    
SITE     1 BC6  6 ASP B 182  GLY B 183  ASP B 185  LEU B 187                    
SITE     2 BC6  6 ASP B 205  GLU B 208                                          
SITE     1 BC7  7 ALA B 164  ASP B 165  GLY B 197  GLN B 199                    
SITE     2 BC7  7 ASP B 201  HOH B 451  HOH B 455                               
SITE     1 BC8  5 ASP B 131  ASP B 206  GLU B 208  PGO B 306                    
SITE     2 BC8  5 HOH B 422                                                     
SITE     1 BC9  7 ASP B 131  ASP B 206  ASP B 207  GLU B 208                    
SITE     2 BC9  7  SR B 305  HOH B 423  HOH B 573                               
SITE     1 CC1  2 HIS B 117  HOH B 523                                          
SITE     1 CC2  4 TYR B 245  MET B 247  HOH B 593  ARG Q   8                    
SITE     1 CC3  3 GLY B 217  TYR B 218  HOH B 576                               
CRYST1   34.200   57.400  172.030  90.00  90.00  90.00 P 21 21 21    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      0.029240  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017422  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005813        0.00000                         
HETATM    1  C   8MC P   1      -8.489   6.831 -35.016  1.00 15.78           C  
HETATM    2  O   8MC P   1      -8.442   6.757 -33.770  1.00 14.95           O  
HETATM    3  CA  8MC P   1      -7.852   8.015 -35.738  1.00 13.42           C  
HETATM    4  C9  8MC P   1      -8.241   9.297 -35.011  1.00 14.14           C  
HETATM    5  C10 8MC P   1      -7.459   9.787 -33.979  1.00 15.55           C  
HETATM    6  C1  8MC P   1      -7.879  10.952 -33.333  1.00 16.08           C  
HETATM    7  O2  8MC P   1      -7.185  11.407 -32.396  1.00 17.62           O  
HETATM    8  C8  8MC P   1      -9.400  10.005 -35.316  1.00 12.96           C  
HETATM    9  C7  8MC P   1     -10.246   9.581 -36.333  1.00 14.25           C  
HETATM   10  C6  8MC P   1     -11.398  10.300 -36.636  1.00 13.42           C  
HETATM   11  C5  8MC P   1     -11.716  11.444 -35.911  1.00 14.29           C  
HETATM   12  O4  8MC P   1     -12.864  12.128 -36.226  1.00 15.56           O  
HETATM   13  C11 8MC P   1     -13.397  13.114 -35.342  1.00 18.81           C  
HETATM   14  C4  8MC P   1     -10.859  11.878 -34.893  1.00 13.86           C  
HETATM   15  C2  8MC P   1      -9.701  11.161 -34.588  1.00 15.04           C  
HETATM   16  O3  8MC P   1      -8.935  11.553 -33.660  1.00 13.88           O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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