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Database: PDB
Entry: 1L6J
LinkDB: 1L6J
Original site: 1L6J 
HEADER    HYDROLASE                               11-MAR-02   1L6J              
TITLE     CRYSTAL STRUCTURE OF HUMAN MATRIX METALLOPROTEINASE MMP9              
TITLE    2 (GELATINASE B).                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MATRIX METALLOPROTEINASE-9;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PRO-FORM WITH C-TERMINAL DOMAIN TRUNCATED;                 
COMPND   5 SYNONYM: MMP9, GELATINASE B, GELB;                                   
COMPND   6 EC: 3.4.24.35;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BLR (DE3)                                  
KEYWDS    TWISTED BETA SHEET FLANKED BY HELICES, HYDROLASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.A.ELKINS,Y.S.HO,W.W.SMITH,C.A.JANSON,K.J.D'ALESSIO,                 
AUTHOR   2 M.S.MCQUENEY,M.D.CUMMINGS,A.M.ROMANIC                                
REVDAT   4   24-FEB-09 1L6J    1       VERSN                                    
REVDAT   3   01-APR-03 1L6J    1       JRNL                                     
REVDAT   2   17-JUL-02 1L6J    1       DBREF                                    
REVDAT   1   03-JUL-02 1L6J    0                                                
JRNL        AUTH   P.A.ELKINS,Y.S.HO,W.W.SMITH,C.A.JANSON,                      
JRNL        AUTH 2 K.J.D'ALESSIO,M.S.MCQUENEY,M.D.CUMMINGS,A.M.ROMANIC          
JRNL        TITL   STRUCTURE OF THE C-TERMINALLY TRUNCATED HUMAN                
JRNL        TITL 2 PROMMP9, A GELATIN-BINDING MATRIX                            
JRNL        TITL 3 METALLOPROTEINASE.                                           
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  58  1182 2002              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   12077439                                                     
JRNL        DOI    10.1107/S0907444902007849                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 24477                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1265                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.53                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 20219                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2720                       
REMARK   3   BIN FREE R VALUE                    : 0.3150                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 39                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3180                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 191                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.00                          
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.29                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.013 ; 0.011                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.840 ; 2.030                
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : 0.76                                                 
REMARK   3   BSOL        : 250.03                                               
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: STRUCTURE FACTOR ANALYSIS FOR THIS        
REMARK   3  REPORT WAS MADE BY SFCHECK V 5.3.4 USING ANISOTROPIC SCALING        
REMARK   3  AND THE BABINET BULK SOLVENT CORRECTION. THE CORRELATION            
REMARK   3  BETWEEN THE EXPERIMENTAL MAP AND THE MODEL WAS COMPUTED USING       
REMARK   3  CCP4/SFALL, CCP4/FFT AND CCP4/OVERLAPMAP. THE DIFFERENCE            
REMARK   3  BETWEEN THE EXPERIMENTAL PHASES AND THE MODEL PHASES WAS            
REMARK   3  COMPUTED USING CCP4/SFALL AND CCP4/PHISTATS.                        
REMARK   4                                                                      
REMARK   4 1L6J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB015687.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.271632, 1.209997, 1.272917       
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRANDEIS                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34009                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1CK7                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CHLORIDE, TRIS, HEPES, PH         
REMARK 280  8.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.95800            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       29.97900            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       44.96850            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       14.98950            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       74.94750            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A    20                                                      
REMARK 465     PRO A    21                                                      
REMARK 465     ARG A    22                                                      
REMARK 465     GLN A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     THR A    27                                                      
REMARK 465     LEU A    28                                                      
REMARK 465     ARG A    56                                                      
REMARK 465     VAL A    57                                                      
REMARK 465     ALA A    58                                                      
REMARK 465     GLU A    59                                                      
REMARK 465     MET A    60                                                      
REMARK 465     ARG A    61                                                      
REMARK 465     GLY A    62                                                      
REMARK 465     GLU A    63                                                      
REMARK 465     SER A    64                                                      
REMARK 465     LYS A    65                                                      
REMARK 465     SER A    66                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A 174   N   -  CA  -  C   ANGL. DEV. = -16.2 DEGREES          
REMARK 500    PRO A 430   C   -  N   -  CA  ANGL. DEV. = -10.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  39      152.67    -47.37                                   
REMARK 500    ALA A 173      -81.72   -141.55                                   
REMARK 500    ALA A 189     -177.04   -175.20                                   
REMARK 500    SER A 211     -153.40   -156.08                                   
REMARK 500    ASP A 226       17.60     58.32                                   
REMARK 500    ARG A 239      146.30    -14.77                                   
REMARK 500    ASP A 266       19.97     53.92                                   
REMARK 500    ASP A 280     -137.29     58.34                                   
REMARK 500    ASP A 309       35.17    -80.68                                   
REMARK 500    ALA A 318        7.36    -65.40                                   
REMARK 500    ASN A 319      105.76   -168.62                                   
REMARK 500    SER A 342       29.89   -144.28                                   
REMARK 500    ARG A 370      152.61    -49.91                                   
REMARK 500    ASP A 390     -155.58    -97.17                                   
REMARK 500    ASP A 410     -164.60   -116.23                                   
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 500  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  99   SG                                                     
REMARK 620 2 HIS A 401   NE2 104.7                                              
REMARK 620 3 HIS A 405   NE2 117.2 107.3                                        
REMARK 620 4 HIS A 411   NE2 117.7 106.4 102.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 175   NE2                                                    
REMARK 620 2 ASP A 177   OD2 115.0                                              
REMARK 620 3 HIS A 190   NE2 112.4 116.2                                        
REMARK 620 4 HIS A 203   ND1 102.2  93.4 115.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 182   OD1                                                    
REMARK 620 2 GLY A 183   O    91.8                                              
REMARK 620 3 ASP A 205   OD2  98.5  81.8                                        
REMARK 620 4 GLU A 208   OE2 177.6  89.9  80.0                                  
REMARK 620 5 LEU A 187   O    83.9 169.5  89.4  94.1                            
REMARK 620 6 GLY A 186   N    84.5  97.1 176.8  97.0  92.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 206   O                                                      
REMARK 620 2 GLU A 208   O    96.5                                              
REMARK 620 3 ASP A 206   OD1  74.6  99.9                                        
REMARK 620 4 ASP A 131   OD2 155.5  77.8  82.9                                  
REMARK 620 5 HOH A1054   O   105.9 157.5  86.5  81.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1052   O                                                      
REMARK 620 2 HOH A1084   O    81.9                                              
REMARK 620 3 ASP A 165   O   115.2 154.4                                        
REMARK 620 4 GLY A 197   O    60.1  62.8 141.6                                  
REMARK 620 5 GLN A 199   O   103.8 124.5  72.0  72.8                            
REMARK 620 6 HOH A1174   O    52.5 132.6  70.1  81.6  65.2                      
REMARK 620 7 ASP A 201   OD1 149.8  78.2  91.7  90.5  70.3 135.2                
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 500                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 501                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 503                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 504                  
DBREF  1L6J A   20   444  UNP    P14780   MMP9_HUMAN      20    444             
SEQRES   1 A  425  ALA PRO ARG GLN ARG GLN SER THR LEU VAL LEU PHE PRO          
SEQRES   2 A  425  GLY ASP LEU ARG THR ASN LEU THR ASP ARG GLN LEU ALA          
SEQRES   3 A  425  GLU GLU TYR LEU TYR ARG TYR GLY TYR THR ARG VAL ALA          
SEQRES   4 A  425  GLU MET ARG GLY GLU SER LYS SER LEU GLY PRO ALA LEU          
SEQRES   5 A  425  LEU LEU LEU GLN LYS GLN LEU SER LEU PRO GLU THR GLY          
SEQRES   6 A  425  GLU LEU ASP SER ALA THR LEU LYS ALA MET ARG THR PRO          
SEQRES   7 A  425  ARG CYS GLY VAL PRO ASP LEU GLY ARG PHE GLN THR PHE          
SEQRES   8 A  425  GLU GLY ASP LEU LYS TRP HIS HIS HIS ASN ILE THR TYR          
SEQRES   9 A  425  TRP ILE GLN ASN TYR SER GLU ASP LEU PRO ARG ALA VAL          
SEQRES  10 A  425  ILE ASP ASP ALA PHE ALA ARG ALA PHE ALA LEU TRP SER          
SEQRES  11 A  425  ALA VAL THR PRO LEU THR PHE THR ARG VAL TYR SER ARG          
SEQRES  12 A  425  ASP ALA ASP ILE VAL ILE GLN PHE GLY VAL ALA GLU HIS          
SEQRES  13 A  425  GLY ASP GLY TYR PRO PHE ASP GLY LYS ASP GLY LEU LEU          
SEQRES  14 A  425  ALA HIS ALA PHE PRO PRO GLY PRO GLY ILE GLN GLY ASP          
SEQRES  15 A  425  ALA HIS PHE ASP ASP ASP GLU LEU TRP SER LEU GLY LYS          
SEQRES  16 A  425  GLY VAL VAL VAL PRO THR ARG PHE GLY ASN ALA ASP GLY          
SEQRES  17 A  425  ALA ALA CYS HIS PHE PRO PHE ILE PHE GLU GLY ARG SER          
SEQRES  18 A  425  TYR SER ALA CYS THR THR ASP GLY ARG SER ASP GLY LEU          
SEQRES  19 A  425  PRO TRP CYS SER THR THR ALA ASN TYR ASP THR ASP ASP          
SEQRES  20 A  425  ARG PHE GLY PHE CYS PRO SER GLU ARG LEU TYR THR ARG          
SEQRES  21 A  425  ASP GLY ASN ALA ASP GLY LYS PRO CYS GLN PHE PRO PHE          
SEQRES  22 A  425  ILE PHE GLN GLY GLN SER TYR SER ALA CYS THR THR ASP          
SEQRES  23 A  425  GLY ARG SER ASP GLY TYR ARG TRP CYS ALA THR THR ALA          
SEQRES  24 A  425  ASN TYR ASP ARG ASP LYS LEU PHE GLY PHE CYS PRO THR          
SEQRES  25 A  425  ARG ALA ASP SER THR VAL MET GLY GLY ASN SER ALA GLY          
SEQRES  26 A  425  GLU LEU CYS VAL PHE PRO PHE THR PHE LEU GLY LYS GLU          
SEQRES  27 A  425  TYR SER THR CYS THR SER GLU GLY ARG GLY ASP GLY ARG          
SEQRES  28 A  425  LEU TRP CYS ALA THR THR SER ASN PHE ASP SER ASP LYS          
SEQRES  29 A  425  LYS TRP GLY PHE CYS PRO ASP GLN GLY TYR SER LEU PHE          
SEQRES  30 A  425  LEU VAL ALA ALA HIS GLU PHE GLY HIS ALA LEU GLY LEU          
SEQRES  31 A  425  ASP HIS SER SER VAL PRO GLU ALA LEU MET TYR PRO MET          
SEQRES  32 A  425  TYR ARG PHE THR GLU GLY PRO PRO LEU HIS LYS ASP ASP          
SEQRES  33 A  425  VAL ASN GLY ILE ARG HIS LEU TYR GLY                          
HET     ZN  A 500       1                                                       
HET     ZN  A 501       1                                                       
HET     CA  A 502       1                                                       
HET     CA  A 503       1                                                       
HET     CA  A 504       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
FORMUL   2   ZN    2(ZN 2+)                                                     
FORMUL   4   CA    3(CA 2+)                                                     
FORMUL   7  HOH   *191(H2 O)                                                    
HELIX    1   1 THR A   40  TYR A   52  1                                  13    
HELIX    2   2 LEU A   67  SER A   79  1                                  13    
HELIX    3   3 ASP A   87  ARG A   95  1                                   9    
HELIX    4   4 PRO A  133  VAL A  151  1                                  19    
HELIX    5   5 ASN A  261  ASP A  266  1                                   6    
HELIX    6   6 ASN A  319  LYS A  324  1                                   6    
HELIX    7   7 ARG A  332  THR A  336  5                                   5    
HELIX    8   8 ASN A  378  LYS A  383  1                                   6    
HELIX    9   9 LEU A  395  LEU A  407  1                                  13    
HELIX   10  10 HIS A  432  TYR A  443  1                                  12    
SHEET    1   A 5 THR A 155  VAL A 159  0                                        
SHEET    2   A 5 ASN A 120  ILE A 125  1  N  TYR A 123   O  VAL A 159           
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 393  SER A 394  1  O  TYR A 393   N  SER A 211           
SHEET    1   C 2 PHE A 234  ILE A 235  0                                        
SHEET    2   C 2 SER A 240  TYR A 241 -1  O  TYR A 241   N  PHE A 234           
SHEET    1   D 2 TRP A 255  SER A 257  0                                        
SHEET    2   D 2 PHE A 268  PHE A 270 -1  O  GLY A 269   N  CYS A 256           
SHEET    1   E 2 PHE A 292  PHE A 294  0                                        
SHEET    2   E 2 GLN A 297  TYR A 299 -1  O  GLN A 297   N  PHE A 294           
SHEET    1   F 2 TRP A 313  ALA A 315  0                                        
SHEET    2   F 2 PHE A 326  PHE A 328 -1  O  GLY A 327   N  CYS A 314           
SHEET    1   G 2 PHE A 351  PHE A 353  0                                        
SHEET    2   G 2 LYS A 356  TYR A 358 -1  O  TYR A 358   N  PHE A 351           
SHEET    1   H 2 TRP A 372  ALA A 374  0                                        
SHEET    2   H 2 TRP A 385  PHE A 387 -1  O  GLY A 386   N  CYS A 373           
SSBOND   1 CYS A  230    CYS A  256                          1555   1555  2.03  
SSBOND   2 CYS A  244    CYS A  271                          1555   1555  2.03  
SSBOND   3 CYS A  288    CYS A  314                          1555   1555  2.01  
SSBOND   4 CYS A  302    CYS A  329                          1555   1555  2.04  
SSBOND   5 CYS A  347    CYS A  373                          1555   1555  2.02  
SSBOND   6 CYS A  361    CYS A  388                          1555   1555  2.03  
LINK        ZN    ZN A 500                 SG  CYS A  99     1555   1555  2.32  
LINK        ZN    ZN A 500                 NE2 HIS A 401     1555   1555  2.26  
LINK        ZN    ZN A 500                 NE2 HIS A 405     1555   1555  2.05  
LINK        ZN    ZN A 500                 NE2 HIS A 411     1555   1555  2.21  
LINK        ZN    ZN A 501                 NE2 HIS A 175     1555   1555  2.19  
LINK        ZN    ZN A 501                 OD2 ASP A 177     1555   1555  2.17  
LINK        ZN    ZN A 501                 NE2 HIS A 190     1555   1555  2.24  
LINK        ZN    ZN A 501                 ND1 HIS A 203     1555   1555  2.13  
LINK        CA    CA A 502                 OD1 ASP A 182     1555   1555  2.61  
LINK        CA    CA A 502                 O   GLY A 183     1555   1555  2.44  
LINK        CA    CA A 502                 OD2 ASP A 205     1555   1555  2.46  
LINK        CA    CA A 502                 OE2 GLU A 208     1555   1555  2.46  
LINK        CA    CA A 502                 O   LEU A 187     1555   1555  2.50  
LINK        CA    CA A 502                 N   GLY A 186     1555   1555  2.86  
LINK        CA    CA A 503                 O   ASP A 206     1555   1555  2.52  
LINK        CA    CA A 503                 O   GLU A 208     1555   1555  2.65  
LINK        CA    CA A 503                 OD1 ASP A 206     1555   1555  2.72  
LINK        CA    CA A 503                 OD2 ASP A 131     1555   1555  2.76  
LINK        CA    CA A 503                 O   HOH A1054     1555   1555  2.78  
LINK        CA    CA A 504                 O   HOH A1052     1555   1555  3.04  
LINK        CA    CA A 504                 O   HOH A1084     1555   1555  3.34  
LINK        CA    CA A 504                 O   ASP A 165     1555   1555  2.75  
LINK        CA    CA A 504                 O   GLY A 197     1555   1555  2.85  
LINK        CA    CA A 504                 O   GLN A 199     1555   1555  3.03  
LINK        CA    CA A 504                 O   HOH A1174     1555   1555  2.96  
LINK        CA    CA A 504                 OD1 ASP A 201     1555   1555  2.66  
CISPEP   1 PHE A  232    PRO A  233          0        -0.27                     
CISPEP   2 PHE A  290    PRO A  291          0         0.27                     
CISPEP   3 PHE A  349    PRO A  350          0        -0.06                     
SITE     1 AC1  4 CYS A  99  HIS A 401  HIS A 405  HIS A 411                    
SITE     1 AC2  4 HIS A 175  ASP A 177  HIS A 190  HIS A 203                    
SITE     1 AC3  6 ASP A 182  GLY A 183  GLY A 186  LEU A 187                    
SITE     2 AC3  6 ASP A 205  GLU A 208                                          
SITE     1 AC4  4 ASP A 131  ASP A 206  GLU A 208  HOH A1054                    
SITE     1 AC5  7 ALA A 164  ASP A 165  GLY A 197  GLN A 199                    
SITE     2 AC5  7 ASP A 201  HOH A1052  HOH A1174                               
CRYST1  123.685  123.685   89.937  90.00  90.00 120.00 P 65          6          
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      0.008085  0.004668  0.000000        0.00000                         
SCALE2      0.000000  0.009336  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011119        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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