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Database: PDB
Entry: 4H1Q
LinkDB: 4H1Q
Original site: 4H1Q 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           11-SEP-12   4H1Q              
TITLE     CRYSTAL STRUCTURE OF MUTANT MMP-9 CATALYTIC DOMAIN IN COMPLEX WITH A  
TITLE    2 TWIN INHIBITOR.                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MATRIX METALLOPROTEINASE-9;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 110-214;                                      
COMPND   5 SYNONYM: MMP-9, 92 KDA GELATINASE, 92 KDA TYPE IV COLLAGENASE,       
COMPND   6 GELATINASE B, GELB, 67 KDA MATRIX METALLOPROTEINASE-9, 82 KDA MATRIX 
COMPND   7 METALLOPROTEINASE-9;                                                 
COMPND   8 EC: 3.4.24.35;                                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CLG4B, MMP9;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3 STAR);                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PT7 PROMOTER;                         
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-14B                                   
KEYWDS    HYDROLASE/TWIN INHIBITOR, ZINCIN-LIKE, GELATINASE, COLLAGENASE        
KEYWDS   2 (CATALYTIC DOMAIN), HYDROLASE-HYDROLASE INHIBITOR COMPLEX            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.A.STURA,L.VERA,E.CASSAR-LAJEUNESSE,E.NUTI,M.P.CATALANI,V.DIVE,      
AUTHOR   2 A.ROSSELLO                                                           
REVDAT   4   09-AUG-17 4H1Q    1       SOURCE REMARK                            
REVDAT   3   12-AUG-15 4H1Q    1       JRNL                                     
REVDAT   2   01-MAY-13 4H1Q    1       AUTHOR                                   
REVDAT   1   24-APR-13 4H1Q    0                                                
JRNL        AUTH   C.ANTONI,L.VERA,L.DEVEL,M.P.CATALANI,B.CZARNY,               
JRNL        AUTH 2 E.CASSAR-LAJEUNESSE,E.NUTI,A.ROSSELLO,V.DIVE,E.A.STURA       
JRNL        TITL   CRYSTALLIZATION OF BI-FUNCTIONAL LIGAND PROTEIN COMPLEXES.   
JRNL        REF    J.STRUCT.BIOL.                V. 182   246 2013              
JRNL        REFN                   ISSN 1047-8477                               
JRNL        PMID   23567804                                                     
JRNL        DOI    10.1016/J.JSB.2013.03.015                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.59 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) : 1.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.09                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 36919                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1846                            
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 43.1012 -  3.7346    0.99     2844   150  0.1574 0.1838        
REMARK   3     2  3.7346 -  2.9644    0.99     2761   145  0.1456 0.1718        
REMARK   3     3  2.9644 -  2.5898    0.98     2742   145  0.1584 0.2148        
REMARK   3     4  2.5898 -  2.3530    0.98     2717   143  0.1602 0.2070        
REMARK   3     5  2.3530 -  2.1844    0.98     2724   143  0.1583 0.1980        
REMARK   3     6  2.1844 -  2.0556    0.97     2687   142  0.1539 0.2037        
REMARK   3     7  2.0556 -  1.9526    0.97     2719   143  0.1592 0.1876        
REMARK   3     8  1.9526 -  1.8676    0.96     2647   139  0.1734 0.2451        
REMARK   3     9  1.8676 -  1.7957    0.96     2685   141  0.1945 0.2309        
REMARK   3    10  1.7957 -  1.7338    0.96     2625   139  0.2076 0.2621        
REMARK   3    11  1.7338 -  1.6796    0.96     2662   140  0.2305 0.2677        
REMARK   3    12  1.6796 -  1.6315    0.96     2654   139  0.2549 0.3236        
REMARK   3    13  1.6315 -  1.5886    0.94     2606   137  0.2741 0.3163        
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)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.910           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.71                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.70                          
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      :  0.008           2931                                  
REMARK   3   ANGLE     :  1.472           4010                                  
REMARK   3   CHIRALITY :  0.083            376                                  
REMARK   3   PLANARITY :  0.007            533                                  
REMARK   3   DIHEDRAL  : 24.462           1087                                  
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 4H1Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000074908.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-NOV-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9334                             
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4R                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36921                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.590                              
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     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.01240                            
REMARK 200  R SYM                      (I) : 0.10900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.5300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.06                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.22900                            
REMARK 200  R SYM FOR SHELL            (I) : 1.07600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.350                              
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: 2OW1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: MMP9H NTER=GFQT E402Q V391Q     
REMARK 280  AT 130.3 MICRO-M WITH 5 MILLI-M AHA RESERVOIR: 40% MPEG 5K,         
REMARK 280  100MM HEPES. CRYOPROTECTANT: 35% MPEG 5K, 15% PEG 400, 15% AAB      
REMARK 280  (90/10), PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       24.33000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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     MET A  247   CG                                                  
REMARK 480     THR B  152   N    CA   C    O    CB   OG1  CG2                   
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   OD2  ASP B   235     C67  0XX B   306              1.93            
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   NE2  HIS A   119     N44  0XX B   306     2656     1.87            
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    ASP A 113      123.96     -8.91                                   
REMARK 500    ALA A 173     -134.90     49.09                                   
REMARK 500    TYR A 179       76.93   -118.17                                   
REMARK 500    ASP A 185     -164.11     57.90                                   
REMARK 500    PRO A 246       40.44    -79.34                                   
REMARK 500    ALA B 173     -136.53     44.42                                   
REMARK 500    ALA B 173     -136.70     44.42                                   
REMARK 500    ASP B 185     -164.82     62.81                                   
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 B 302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 177   OD1                                                    
REMARK 620 2 HIS B 175   NE2 110.5                                              
REMARK 620 3 HIS B 190   NE2 114.9 114.2                                        
REMARK 620 4 HIS B 203   ND1  94.2 109.5 111.7                                  
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 ASP A 177   OD1                                                    
REMARK 620 2 HIS A 190   NE2 113.9                                              
REMARK 620 3 HIS A 175   NE2 107.4 120.4                                        
REMARK 620 4 HIS A 203   ND1  91.4 113.9 105.7                                  
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 HIS B 230   NE2 101.2                                              
REMARK 620 3 HIS B 226   NE2 108.3  98.6                                        
REMARK 620 4 0XX B 306   O25  90.1 119.8 133.5                                  
REMARK 620 5 0XX B 306   O23 170.8  80.5  80.2  81.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 230   NE2                                                    
REMARK 620 2 HIS A 236   NE2 100.1                                              
REMARK 620 3 HIS A 226   NE2  98.3 108.6                                        
REMARK 620 4 0XX A 307   O25 127.1  95.5 123.7                                  
REMARK 620 5 0XX A 307   O23  84.7 167.2  82.1  72.3                            
REMARK 620 N                    1     2     3     4                             
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 GLU A 208   OE2                                                    
REMARK 620 2 LEU A 187   O    86.5                                              
REMARK 620 3 GLY A 183   O    94.0 178.3                                        
REMARK 620 4 ASP A 185   O    87.3  95.7  85.9                                  
REMARK 620 5 ASP A 182   OD1 173.0  92.4  87.3  85.9                            
REMARK 620 6 ASP A 205   OD2  96.0  90.4  87.9 173.2  90.9                      
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 GLU A 208   O                                                      
REMARK 620 2 ASP A 131   OD2  87.7                                              
REMARK 620 3 ASP A 206   OD1 122.0 101.6                                        
REMARK 620 4 ASP A 206   O    95.2 177.0  76.3                                  
REMARK 620 5 HOH A 421   O   144.7  83.9  93.3  94.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 306  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A 154   O                                                      
REMARK 620 2 SER A 149   O   126.9                                              
REMARK 620 3 SER A 149   O   123.9   3.1                                        
REMARK 620 4 THR A 152   O    95.3  74.8  73.5                                  
REMARK 620 5 SER A 149   OG   85.4  73.3  73.4 140.3                            
REMARK 620 6 HOH A 496   O    94.4 136.0 138.2  88.3 131.3                      
REMARK 620 N                    1     2     3     4     5                       
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 GLY A 197   O                                                      
REMARK 620 2 GLN A 199   O    81.4                                              
REMARK 620 3 ASP A 201   OD1  94.2  96.6                                        
REMARK 620 4 ASP A 165   O   168.4 109.1  89.5                                  
REMARK 620 5 HOH A 477   O    92.9  81.8 172.4  84.1                            
REMARK 620 6 HOH A 481   O    80.2 159.3  94.1  88.6  89.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 305  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU B 187   O                                                      
REMARK 620 2 GLU B 208   OE2  87.2                                              
REMARK 620 3 ASP B 205   OD2  92.4  97.2                                        
REMARK 620 4 GLY B 183   O   177.6  91.6  85.8                                  
REMARK 620 5 ASP B 185   O    93.1  83.2 174.5  88.8                            
REMARK 620 6 ASP B 182   OD1  92.7 171.2  91.6  88.9  88.0                      
REMARK 620 N                    1     2     3     4     5                       
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 GLY B 197   O                                                      
REMARK 620 2 ASP B 165   O   169.3                                              
REMARK 620 3 GLN B 199   O    81.4 107.2                                        
REMARK 620 4 ASP B 201   OD1  95.4  90.0  96.7                                  
REMARK 620 5 HOH B 487   O    93.3  81.7  82.9 171.2                            
REMARK 620 6 HOH B 489   O    83.2  86.9 159.8  97.6  85.1                      
REMARK 620 N                    1     2     3     4     5                       
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 206   O                                                      
REMARK 620 2 ASP B 206   OD1  73.8                                              
REMARK 620 3 GLU B 208   O    81.2 111.9                                        
REMARK 620 4 ASP B 131   OD2 146.5  89.3  78.7                                  
REMARK 620 5 ASP B 131   OD1 154.1  90.8 124.4  50.4                            
REMARK 620 6 HOH B 518   O   102.2 168.6  77.5  99.2  88.9                      
REMARK 620 7 HOH B 517   O    68.8  82.7 141.7 138.6  89.0  85.9                
REMARK 620 N                    1     2     3     4     5     6                 
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 CA A 306                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0XX 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: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0XX B 306                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2OW1   RELATED DB: PDB                                   
REMARK 900 MMP-9 ACTIVE SITE MUTANT WITH TRIFLUOROMETHYL HYDROXAMATE INHIBITOR  
REMARK 900 RELATED ID: 4H3X   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4H2E   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4H30   RELATED DB: PDB                                   
DBREF  4H1Q A  110   214  UNP    P14780   MMP9_HUMAN     110    214             
DBREF  4H1Q A  216   269  UNP    P14780   MMP9_HUMAN     391    444             
DBREF  4H1Q B  110   214  UNP    P14780   MMP9_HUMAN     110    214             
DBREF  4H1Q B  216   269  UNP    P14780   MMP9_HUMAN     391    444             
SEQADV 4H1Q GLN A  227  UNP  P14780    GLU   402 ENGINEERED MUTATION            
SEQADV 4H1Q GLN B  227  UNP  P14780    GLU   402 ENGINEERED MUTATION            
SEQRES   1 A  160  PHE GLU GLY ASP LEU LYS TRP HIS HIS HIS ASN ILE THR          
SEQRES   2 A  160  TYR TRP ILE GLN ASN TYR SER GLU ASP LEU PRO ARG ALA          
SEQRES   3 A  160  VAL ILE ASP ASP ALA PHE ALA ARG ALA PHE ALA LEU TRP          
SEQRES   4 A  160  SER ALA VAL THR PRO LEU THR PHE THR ARG VAL TYR SER          
SEQRES   5 A  160  ARG ASP ALA ASP ILE VAL ILE GLN PHE GLY VAL ALA GLU          
SEQRES   6 A  160  HIS GLY ASP GLY TYR PRO PHE ASP GLY LYS ASP GLY LEU          
SEQRES   7 A  160  LEU ALA HIS ALA PHE PRO PRO GLY PRO GLY ILE GLN GLY          
SEQRES   8 A  160  ASP ALA HIS PHE ASP ASP ASP GLU LEU TRP SER LEU GLY          
SEQRES   9 A  160  LYS GLY GLN GLY TYR SER LEU PHE LEU VAL ALA ALA HIS          
SEQRES  10 A  160  GLN PHE GLY HIS ALA LEU GLY LEU ASP HIS SER SER VAL          
SEQRES  11 A  160  PRO GLU ALA LEU MET TYR PRO MET TYR ARG PHE THR GLU          
SEQRES  12 A  160  GLY PRO PRO LEU HIS LYS ASP ASP VAL ASN GLY ILE ARG          
SEQRES  13 A  160  HIS LEU TYR GLY                                              
SEQRES   1 B  160  PHE GLU GLY ASP LEU LYS TRP HIS HIS HIS ASN ILE THR          
SEQRES   2 B  160  TYR TRP ILE GLN ASN TYR SER GLU ASP LEU PRO ARG ALA          
SEQRES   3 B  160  VAL ILE ASP ASP ALA PHE ALA ARG ALA PHE ALA LEU TRP          
SEQRES   4 B  160  SER ALA VAL THR PRO LEU THR PHE THR ARG VAL TYR SER          
SEQRES   5 B  160  ARG ASP ALA ASP ILE VAL ILE GLN PHE GLY VAL ALA GLU          
SEQRES   6 B  160  HIS GLY ASP GLY TYR PRO PHE ASP GLY LYS ASP GLY LEU          
SEQRES   7 B  160  LEU ALA HIS ALA PHE PRO PRO GLY PRO GLY ILE GLN GLY          
SEQRES   8 B  160  ASP ALA HIS PHE ASP ASP ASP GLU LEU TRP SER LEU GLY          
SEQRES   9 B  160  LYS GLY GLN GLY TYR SER LEU PHE LEU VAL ALA ALA HIS          
SEQRES  10 B  160  GLN PHE GLY HIS ALA LEU GLY LEU ASP HIS SER SER VAL          
SEQRES  11 B  160  PRO GLU ALA LEU MET TYR PRO MET TYR ARG PHE THR GLU          
SEQRES  12 B  160  GLY PRO PRO LEU HIS LYS ASP ASP VAL ASN GLY ILE ARG          
SEQRES  13 B  160  HIS LEU TYR GLY                                              
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     CA  A 306       1                                                       
HET    0XX  A 307      78                                                       
HET     ZN  B 301       1                                                       
HET     ZN  B 302       1                                                       
HET     CA  B 303       1                                                       
HET     CA  B 304       1                                                       
HET     CA  B 305       1                                                       
HET    0XX  B 306      78                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     0XX N-(4-{[(3R)-3-[(BIPHENYL-4-YLSULFONYL)(PROPAN-2-YLOXY)           
HETNAM   2 0XX  AMINO]-4-(HYDROXYAMINO)-4-OXOBUTYL]AMINO}-4-OXOBUTYL)-          
HETNAM   3 0XX  N'-(4-{[(3S)-3-[(BIPHENYL-4-YLSULFONYL)(PROPAN-2-               
HETNAM   4 0XX  YLOXY)AMINO]-4-(HYDROXYAMINO)-4-OXOBUTYL]AMINO}-4-              
HETNAM   5 0XX  OXOBUTYL)BENZENE-1,3-DICARBOXAMIDE                              
FORMUL   3   ZN    4(ZN 2+)                                                     
FORMUL   5   CA    7(CA 2+)                                                     
FORMUL   9  0XX    2(C54 H66 N8 O14 S2)                                         
FORMUL  16  HOH   *326(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  ALA B  150  1                                  18    
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 5 THR A 155  ARG A 158  0                                        
SHEET    2   A 5 ASN A 120  ILE A 125  1  N  ILE A 121   O  THR A 157           
SHEET    3   A 5 ILE A 166  GLY A 171  1  O  ILE A 168   N  TRP A 124           
SHEET    4   A 5 ALA A 202  ASP A 205  1  O  PHE A 204   N  GLN A 169           
SHEET    5   A 5 ALA A 189  ALA A 191 -1  N  HIS A 190   O  HIS A 203           
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 5 THR B 155  VAL B 159  0                                        
SHEET    2   C 5 ASN B 120  ILE B 125  1  N  TYR B 123   O  VAL B 159           
SHEET    3   C 5 ILE B 166  GLY B 171  1  O  ILE B 168   N  TRP B 124           
SHEET    4   C 5 ALA B 202  ASP B 205  1  O  PHE B 204   N  GLN B 169           
SHEET    5   C 5 ALA B 189  ALA B 191 -1  N  HIS B 190   O  HIS B 203           
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         OD1 ASP B 177                ZN    ZN B 302     1555   1555  1.87  
LINK         OD1 ASP A 177                ZN    ZN A 302     1555   1555  1.93  
LINK         NE2 HIS A 190                ZN    ZN A 302     1555   1555  1.95  
LINK         NE2 HIS A 175                ZN    ZN A 302     1555   1555  1.95  
LINK         NE2 HIS B 175                ZN    ZN B 302     1555   1555  1.99  
LINK         NE2 HIS B 236                ZN    ZN B 301     1555   1555  2.02  
LINK         NE2 HIS B 190                ZN    ZN B 302     1555   1555  2.03  
LINK         NE2 HIS B 230                ZN    ZN B 301     1555   1555  2.03  
LINK         NE2 HIS A 230                ZN    ZN A 301     1555   1555  2.04  
LINK         ND1 HIS A 203                ZN    ZN A 302     1555   1555  2.04  
LINK         NE2 HIS A 236                ZN    ZN A 301     1555   1555  2.05  
LINK         NE2 HIS A 226                ZN    ZN A 301     1555   1555  2.07  
LINK         NE2 HIS B 226                ZN    ZN B 301     1555   1555  2.08  
LINK         ND1 HIS B 203                ZN    ZN B 302     1555   1555  2.10  
LINK         OE2 GLU A 208                CA    CA A 305     1555   1555  2.18  
LINK         O   GLU A 208                CA    CA A 304     1555   1555  2.22  
LINK         O   LEU A 154                CA    CA A 306     1555   1555  2.22  
LINK         O   LEU A 187                CA    CA A 305     1555   1555  2.24  
LINK         O   GLY A 183                CA    CA A 305     1555   1555  2.25  
LINK         O   GLY A 197                CA    CA A 303     1555   1555  2.26  
LINK         O   LEU B 187                CA    CA B 305     1555   1555  2.26  
LINK         OE2 GLU B 208                CA    CA B 305     1555   1555  2.27  
LINK         O   GLY B 197                CA    CA B 303     1555   1555  2.27  
LINK         O   ASP B 206                CA    CA B 304     1555   1555  2.29  
LINK         OD2 ASP B 205                CA    CA B 305     1555   1555  2.30  
LINK         O   ASP B 165                CA    CA B 303     1555   1555  2.31  
LINK         O   GLN A 199                CA    CA A 303     1555   1555  2.31  
LINK         OD1 ASP A 201                CA    CA A 303     1555   1555  2.32  
LINK         O   GLN B 199                CA    CA B 303     1555   1555  2.32  
LINK         O   GLY B 183                CA    CA B 305     1555   1555  2.33  
LINK         O   ASP A 185                CA    CA A 305     1555   1555  2.33  
LINK         OD1 ASP B 201                CA    CA B 303     1555   1555  2.34  
LINK         OD2 ASP A 131                CA    CA A 304     1555   1555  2.34  
LINK         O   ASP A 165                CA    CA A 303     1555   1555  2.34  
LINK         OD1 ASP A 182                CA    CA A 305     1555   1555  2.35  
LINK         O  ASER A 149                CA    CA A 306     1555   1555  2.36  
LINK         O   ASP B 185                CA    CA B 305     1555   1555  2.36  
LINK         O  BSER A 149                CA    CA A 306     1555   1555  2.37  
LINK         OD1 ASP B 206                CA    CA B 304     1555   1555  2.37  
LINK         OD2 ASP A 205                CA    CA A 305     1555   1555  2.37  
LINK         OD1 ASP B 182                CA    CA B 305     1555   1555  2.39  
LINK         O   GLU B 208                CA    CA B 304     1555   1555  2.40  
LINK         OD1 ASP A 206                CA    CA A 304     1555   1555  2.41  
LINK         O   ASP A 206                CA    CA A 304     1555   1555  2.41  
LINK         OD2 ASP B 131                CA    CA B 304     1555   1555  2.46  
LINK         O   THR A 152                CA    CA A 306     1555   1555  2.57  
LINK         OD1 ASP B 131                CA    CA B 304     1555   1555  2.72  
LINK         OG BSER A 149                CA    CA A 306     1555   1555  2.93  
LINK        ZN    ZN B 301                 O25 0XX B 306     1555   1555  2.11  
LINK        ZN    ZN B 301                 O23 0XX B 306     1555   1555  2.15  
LINK        ZN    ZN A 301                 O25 0XX A 307     1555   1555  2.11  
LINK        ZN    ZN A 301                 O23 0XX A 307     1555   1555  2.32  
LINK        CA    CA B 303                 O   HOH B 487     1555   1555  2.31  
LINK        CA    CA A 303                 O   HOH A 477     1555   1555  2.34  
LINK        CA    CA B 304                 O   HOH B 518     1555   1555  2.34  
LINK        CA    CA B 303                 O   HOH B 489     1555   1555  2.38  
LINK        CA    CA B 304                 O   HOH B 517     1555   1555  2.45  
LINK        CA    CA A 304                 O   HOH A 421     1555   1555  2.46  
LINK        CA    CA A 303                 O   HOH A 481     1555   1555  2.47  
LINK        CA    CA A 306                 O   HOH A 496     1555   1555  2.47  
SITE     1 AC1  4 HIS A 226  HIS A 230  HIS A 236  0XX A 307                    
SITE     1 AC2  4 HIS A 175  ASP A 177  HIS A 190  HIS A 203                    
SITE     1 AC3  6 ASP A 165  GLY A 197  GLN A 199  ASP A 201                    
SITE     2 AC3  6 HOH A 477  HOH A 481                                          
SITE     1 AC4  4 ASP A 131  ASP A 206  GLU A 208  HOH A 421                    
SITE     1 AC5  6 ASP A 182  GLY A 183  ASP A 185  LEU A 187                    
SITE     2 AC5  6 ASP A 205  GLU A 208                                          
SITE     1 AC6  4 SER A 149  THR A 152  LEU A 154  HOH A 496                    
SITE     1 AC7 29 TYR A 179  PRO A 180  PHE A 181  ASP A 182                    
SITE     2 AC7 29 LEU A 187  LEU A 188  ALA A 189  HIS A 190                    
SITE     3 AC7 29 ALA A 191  PHE A 192  PRO A 193  LEU A 222                    
SITE     4 AC7 29 HIS A 226  GLN A 227  HIS A 230  HIS A 236                    
SITE     5 AC7 29 LEU A 243  TYR A 245  PRO A 246  MET A 247                    
SITE     6 AC7 29 TYR A 248   ZN A 301  HOH A 449  HOH A 526                    
SITE     7 AC7 29 PRO B 240  GLU B 241  TYR B 245  PRO B 246                    
SITE     8 AC7 29 ARG B 249                                                     
SITE     1 AC8  4 HIS B 226  HIS B 230  HIS B 236  0XX B 306                    
SITE     1 AC9  4 HIS B 175  ASP B 177  HIS B 190  HIS B 203                    
SITE     1 BC1  6 ASP B 165  GLY B 197  GLN B 199  ASP B 201                    
SITE     2 BC1  6 HOH B 487  HOH B 489                                          
SITE     1 BC2  5 ASP B 131  ASP B 206  GLU B 208  HOH B 517                    
SITE     2 BC2  5 HOH B 518                                                     
SITE     1 BC3  6 ASP B 182  GLY B 183  ASP B 185  LEU B 187                    
SITE     2 BC3  6 ASP B 205  GLU B 208                                          
SITE     1 BC4 30 TYR A 245  PRO A 246  HOH A 523  GLY B 112                    
SITE     2 BC4 30 LEU B 187  LEU B 188  ALA B 189  HIS B 190                    
SITE     3 BC4 30 ALA B 191  PRO B 193  LEU B 222  HIS B 226                    
SITE     4 BC4 30 GLN B 227  HIS B 230  GLY B 233  LEU B 234                    
SITE     5 BC4 30 ASP B 235  HIS B 236  LEU B 243  TYR B 245                    
SITE     6 BC4 30 PRO B 246  MET B 247  TYR B 248  HIS B 266                    
SITE     7 BC4 30  ZN B 301  HOH B 432  HOH B 433  HOH B 446                    
SITE     8 BC4 30 HOH B 483  HOH B 526                                          
CRYST1   44.140   48.660   67.920  90.00 102.55  90.00 P 1 21 1      4          
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      0.022655  0.000000  0.005043        0.00000                         
SCALE2      0.000000  0.020551  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015084        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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