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Database: PDB
Entry: 4FVL
LinkDB: 4FVL
Original site: 4FVL 
HEADER    HYDROLASE                               29-JUN-12   4FVL              
TITLE     HUMAN COLLAGENASE 3 (MMP-13) FULL FORM WITH PEPTIDES FROM PRO-DOMAIN  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COLLAGENASE 3;                                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: INACTIVE FULL FORM (UNP RESIDUES 104-471);                 
COMPND   5 SYNONYM: MATRIX METALLOPROTEINASE-13, MMP-13;                        
COMPND   6 EC: 3.4.24.-;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: COLLAGENASE 3, PRO-DOMAIN PEPTIDE;                         
COMPND  11 CHAIN: C, D;                                                         
COMPND  12 FRAGMENT: PRO-DOMAIN FRAGMENT (UNP RESIDUES 31-50);                  
COMPND  13 SYNONYM: MATRIX METALLOPROTEINASE-13, MMP-13;                        
COMPND  14 EC: 3.4.24.-;                                                        
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MMP13;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET3A;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: MMP13;                                                         
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET3A                                     
KEYWDS    PROTEIN-PEPTIDE COMPLEX, COLLAGENASE, CLEAVAGE WITH MMP3, HYDROLASE,  
KEYWDS   2 PRO-PEPTIDE, METZINCIN, ZINC METALLOPROTEASE, COLLAGEN CLEAVAGE,     
KEYWDS   3 COLLAGEN                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.A.STURA,L.VERA,R.VISSE,H.NAGASE,V.DIVE                              
REVDAT   2   05-FEB-14 4FVL    1       JRNL                                     
REVDAT   1   21-AUG-13 4FVL    0                                                
JRNL        AUTH   E.A.STURA,R.VISSE,P.CUNIASSE,V.DIVE,H.NAGASE                 
JRNL        TITL   CRYSTAL STRUCTURE OF FULL-LENGTH HUMAN COLLAGENASE 3         
JRNL        TITL 2 (MMP-13) WITH PEPTIDES IN THE ACTIVE SITE DEFINES EXOSITES   
JRNL        TITL 3 IN THE CATALYTIC DOMAIN.                                     
JRNL        REF    FASEB J.                      V.  27  4395 2013              
JRNL        REFN                   ISSN 0892-6638                               
JRNL        PMID   23913860                                                     
JRNL        DOI    10.1096/FJ.13-233601                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.44 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.44                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.11                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 37795                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1890                            
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 49.1243 -  5.7240    0.90     2747   144  0.1667 0.1781        
REMARK   3     2  5.7240 -  4.5444    0.92     2687   142  0.1499 0.1959        
REMARK   3     3  4.5444 -  3.9702    0.93     2732   144  0.1317 0.1717        
REMARK   3     4  3.9702 -  3.6073    0.95     2741   144  0.1457 0.1929        
REMARK   3     5  3.6073 -  3.3488    0.96     2765   145  0.1600 0.2483        
REMARK   3     6  3.3488 -  3.1514    0.97     2763   146  0.1656 0.2186        
REMARK   3     7  3.1514 -  2.9936    0.97     2783   146  0.1722 0.2705        
REMARK   3     8  2.9936 -  2.8633    0.98     2795   147  0.1775 0.2244        
REMARK   3     9  2.8633 -  2.7531    0.98     2807   148  0.1789 0.2670        
REMARK   3    10  2.7531 -  2.6581    0.98     2781   147  0.1892 0.2740        
REMARK   3    11  2.6581 -  2.5750    0.98     2793   147  0.2070 0.2948        
REMARK   3    12  2.5750 -  2.5014    0.98     2831   148  0.2154 0.3381        
REMARK   3    13  2.5014 -  2.4356    0.95     2680   142  0.2359 0.3116        
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)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.490           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.07                          
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      :  0.009           6764                                  
REMARK   3   ANGLE     :  1.196           9108                                  
REMARK   3   CHIRALITY :  0.083            922                                  
REMARK   3   PLANARITY :  0.005           1161                                  
REMARK   3   DIHEDRAL  : 16.547           2485                                  
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 4FVL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073410.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.980110                           
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37803                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.440                              
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     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 5.820                              
REMARK 200  R MERGE                    (I) : 0.16500                            
REMARK 200  R SYM                      (I) : 0.15000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.1500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.44                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.69                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.02500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.92000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.710                              
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: 4FU4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROPEPTIDE IMPURITY INDUCES              
REMARK 280  CRYSTALLIZATION ON COLD STORAGE CRYOPROTECTANT: 10% DI-ETHYLENE     
REMARK 280  GLYCOL, 10% 1.2-PROPANEDIOL, 10% GLYCEROL, 10% PEG 10K, 10% PCTP    
REMARK 280  80/20, 0.2 M NACL, PH 7.5, SLOW COOLING, TEMPERATURE 277.0K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.77500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.77500            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       62.89000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       78.63500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       62.89000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       78.63500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       52.77500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       62.89000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       78.63500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       52.77500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       62.89000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       78.63500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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     LEU C    31                                                      
REMARK 465     SER C    32                                                      
REMARK 465     GLU C    33                                                      
REMARK 465     GLU C    34                                                      
REMARK 465     ASP C    35                                                      
REMARK 465     LEU C    36                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 109       -0.67     72.14                                   
REMARK 500    LEU A 111      103.41    -58.62                                   
REMARK 500    LYS A 170     -127.92     39.55                                   
REMARK 500    ASP A 174     -159.84   -114.31                                   
REMARK 500    SER A 182     -158.85     50.74                                   
REMARK 500    ASN A 194     -117.70     56.95                                   
REMARK 500    ASP A 305     -132.98     52.97                                   
REMARK 500    LYS B 170     -118.29     44.27                                   
REMARK 500    ASP B 179       19.51   -140.10                                   
REMARK 500    SER B 182     -160.49     57.29                                   
REMARK 500    ASN B 194     -115.10     60.09                                   
REMARK 500    SER B 210     -155.34   -129.77                                   
REMARK 500    ASN B 274       76.73   -119.84                                   
REMARK 500    PRO B 275       37.51    -79.15                                   
REMARK 500    ASP B 305     -128.84     54.48                                   
REMARK 500    LYS B 414     -159.13    -70.66                                   
REMARK 500    ASP B 415      -16.50     51.94                                   
REMARK 500    TRP B 470       30.07     71.08                                   
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 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 172   NE2                                                    
REMARK 620 2 HIS A 200   ND1 109.3                                              
REMARK 620 3 ASP A 174   OD2 105.3  97.0                                        
REMARK 620 4 HIS A 187   NE2 116.5 115.9 110.7                                  
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 226   NE2                                                    
REMARK 620 2 HIS A 232   NE2 101.9                                              
REMARK 620 3 HIS A 222   NE2 105.2 100.0                                        
REMARK 620 4 HOH C 204   O    95.1 141.4 108.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 172   NE2                                                    
REMARK 620 2 HIS B 200   ND1 108.2                                              
REMARK 620 3 ASP B 174   OD2 118.4  92.3                                        
REMARK 620 4 HIS B 187   NE2 116.6 111.8 107.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 222   NE2                                                    
REMARK 620 2 HIS B 232   NE2  99.7                                              
REMARK 620 3 HIS B 226   NE2  98.7  95.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B 180   O                                                      
REMARK 620 2 GLU B 205   OE2  91.1                                              
REMARK 620 3 SER B 182   O    83.7  82.0                                        
REMARK 620 4 ASP B 202   OD2  94.3  94.4 175.9                                  
REMARK 620 5 LEU B 184   O   170.8  87.8  87.0  94.9                            
REMARK 620 6 ASP B 179   OD1  87.8 174.2  92.2  91.3  92.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 162   O                                                      
REMARK 620 2 ASN B 194   O   164.4                                              
REMARK 620 3 HOH B 633   O    82.7  84.8                                        
REMARK 620 4 GLY B 196   O    92.6  96.6 162.4                                  
REMARK 620 5 ASP B 198   OD1  98.1  94.1 104.8  92.6                            
REMARK 620 6 HOH B 713   O    79.8  88.5  78.4  84.1 176.0                      
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 LEU A 184   O                                                      
REMARK 620 2 ASP A 202   OD2 104.4                                              
REMARK 620 3 GLU A 205   OE2  91.4  90.3                                        
REMARK 620 4 GLY A 180   O   163.8  89.0  79.2                                  
REMARK 620 5 ASP A 179   OD1  94.6  92.9 172.3  93.8                            
REMARK 620 6 SER A 182   O    89.1 166.3  86.7  77.3  88.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 507  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 203   O                                                      
REMARK 620 2 GLU A 205   O    98.3                                              
REMARK 620 3 ASP A 128   OD2 145.3  80.0                                        
REMARK 620 4 ASP A 203   OD2  72.9  99.6  73.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 506  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 385   O                                                      
REMARK 620 2 ILE A 293   O   167.4                                              
REMARK 620 3 ALA A 337   O    90.0  86.8                                        
REMARK 620 4 VAL A 434   O    88.2  93.1 171.3                                  
REMARK 620 N                    1     2     3                                   
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 ASN A 194   O                                                      
REMARK 620 2 ASP A 162   O   173.3                                              
REMARK 620 3 HOH A 663   O    77.5  96.0                                        
REMARK 620 4 HOH A 619   O    90.4  88.3  90.5                                  
REMARK 620 5 GLY A 196   O   101.3  84.2 158.0  67.5                            
REMARK 620 6 ASP A 198   OD1  87.2  95.0  96.6 171.8 105.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 505  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 291   O                                                      
REMARK 620 2 ASP A 432   O    74.7                                              
REMARK 620 3 ASP A 335   O    80.2 118.9                                        
REMARK 620 4 HOH A 669   O    84.0 140.9  88.4                                  
REMARK 620 5 SER A 383   O   117.3  68.1  76.3 150.3                            
REMARK 620 6 HOH A 605   O    97.3  83.5 155.3  66.9 125.1                      
REMARK 620 7 HOH A 612   O   150.8 130.4  95.6  66.9  89.2  74.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 507  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 203   O                                                      
REMARK 620 2 GLU B 205   O    86.9                                              
REMARK 620 3 ASP B 128   OD2 148.2  75.7                                        
REMARK 620 4 ASP B 203   OD2  71.0 107.6  89.0                                  
REMARK 620 5 ASP B 128   OD1 163.3 109.2  45.7 107.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 506  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA B 385   O                                                      
REMARK 620 2 ALA B 337   O    82.2                                              
REMARK 620 3 ILE B 293   O   176.2  95.8                                        
REMARK 620 4 VAL B 434   O    94.9 176.4  87.2                                  
REMARK 620 5 HOH B 617   O    89.4  92.0  87.4  90.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 505  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 291   O                                                      
REMARK 620 2 ASP B 335   O    83.6                                              
REMARK 620 3 SER B 383   O   116.7  70.8                                        
REMARK 620 4 ASP B 432   O    73.4 116.0  68.7                                  
REMARK 620 5 HOH B 606   O    90.6 164.0 125.0  76.2                            
REMARK 620 6 HOH B 661   O   161.6 100.2  81.3 119.5  80.9                      
REMARK 620 7 HOH B 615   O    86.8  92.7 148.2 142.2  72.1  75.1                
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 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 523                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 524                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 525                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 526                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 527                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 528                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 529                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 530                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 531                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 532                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 524                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 525                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 526                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 527                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 528                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 529                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 530                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO C 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 101                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4FU4   RELATED DB: PDB                                   
REMARK 900 HUMAN COLLAGENASE 3 (MMP-13) WITH PEPTIDE FROM PRO-DOMAIN            
REMARK 900 RELATED ID: 3TVC   RELATED DB: PDB                                   
REMARK 900 HUMAN MMP13 IN COMPLEX WITH L-GLUTAMATE MOTIF INHIBITOR              
REMARK 900 RELATED ID: 1PEX   RELATED DB: PDB                                   
REMARK 900 COLLAGENASE-3 (MMP-13) C-TERMINAL HEMOPEXIN-LIKE DOMAIN              
REMARK 900 METALLOPROTEASE                                                      
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AFTER CLEAVAGE WITH PROTEASE MMP3 TO CLEAVE OFF THE PRO-DOMAIN TO    
REMARK 999 GIVE RISE TO THE MATURE (INACTIVE) PROTEASE (E223A), A FRAGMENT OF   
REMARK 999 THE PRO-PEPTIDE IS BOUND BACK ONTO THE INACTIVE PROTEASE. THUS       
REMARK 999 CHAIN C BELONGS TO CHAIN A, AND CHAIN D BELONGS TO CHAIN B.          
DBREF  4FVL A  104   471  UNP    P45452   MMP13_HUMAN    104    471             
DBREF  4FVL B  104   471  UNP    P45452   MMP13_HUMAN    104    471             
DBREF  4FVL C   31    50  UNP    P45452   MMP13_HUMAN     31     50             
DBREF  4FVL D   31    50  UNP    P45452   MMP13_HUMAN     31     50             
SEQADV 4FVL ALA A  223  UNP  P45452    GLU   223 ENGINEERED MUTATION            
SEQADV 4FVL ALA B  223  UNP  P45452    GLU   223 ENGINEERED MUTATION            
SEQRES   1 A  368  TYR ASN VAL PHE PRO ARG THR LEU LYS TRP SER LYS MET          
SEQRES   2 A  368  ASN LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP MET          
SEQRES   3 A  368  THR HIS SER GLU VAL GLU LYS ALA PHE LYS LYS ALA PHE          
SEQRES   4 A  368  LYS VAL TRP SER ASP VAL THR PRO LEU ASN PHE THR ARG          
SEQRES   5 A  368  LEU HIS ASP GLY ILE ALA ASP ILE MET ILE SER PHE GLY          
SEQRES   6 A  368  ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO          
SEQRES   7 A  368  SER GLY LEU LEU ALA HIS ALA PHE PRO PRO GLY PRO ASN          
SEQRES   8 A  368  TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP GLU THR TRP          
SEQRES   9 A  368  THR SER SER SER LYS GLY TYR ASN LEU PHE LEU VAL ALA          
SEQRES  10 A  368  ALA HIS ALA PHE GLY HIS SER LEU GLY LEU ASP HIS SER          
SEQRES  11 A  368  LYS ASP PRO GLY ALA LEU MET PHE PRO ILE TYR THR TYR          
SEQRES  12 A  368  THR GLY LYS SER HIS PHE MET LEU PRO ASP ASP ASP VAL          
SEQRES  13 A  368  GLN GLY ILE GLN SER LEU TYR GLY PRO GLY ASP GLU ASP          
SEQRES  14 A  368  PRO ASN PRO LYS HIS PRO LYS THR PRO ASP LYS CYS ASP          
SEQRES  15 A  368  PRO SER LEU SER LEU ASP ALA ILE THR SER LEU ARG GLY          
SEQRES  16 A  368  GLU THR MET ILE PHE LYS ASP ARG PHE PHE TRP ARG LEU          
SEQRES  17 A  368  HIS PRO GLN GLN VAL ASP ALA GLU LEU PHE LEU THR LYS          
SEQRES  18 A  368  SER PHE TRP PRO GLU LEU PRO ASN ARG ILE ASP ALA ALA          
SEQRES  19 A  368  TYR GLU HIS PRO SER HIS ASP LEU ILE PHE ILE PHE ARG          
SEQRES  20 A  368  GLY ARG LYS PHE TRP ALA LEU ASN GLY TYR ASP ILE LEU          
SEQRES  21 A  368  GLU GLY TYR PRO LYS LYS ILE SER GLU LEU GLY LEU PRO          
SEQRES  22 A  368  LYS GLU VAL LYS LYS ILE SER ALA ALA VAL HIS PHE GLU          
SEQRES  23 A  368  ASP THR GLY LYS THR LEU LEU PHE SER GLY ASN GLN VAL          
SEQRES  24 A  368  TRP ARG TYR ASP ASP THR ASN HIS ILE MET ASP LYS ASP          
SEQRES  25 A  368  TYR PRO ARG LEU ILE GLU GLU ASP PHE PRO GLY ILE GLY          
SEQRES  26 A  368  ASP LYS VAL ASP ALA VAL TYR GLU LYS ASN GLY TYR ILE          
SEQRES  27 A  368  TYR PHE PHE ASN GLY PRO ILE GLN PHE GLU TYR SER ILE          
SEQRES  28 A  368  TRP SER ASN ARG ILE VAL ARG VAL MET PRO ALA ASN SER          
SEQRES  29 A  368  ILE LEU TRP CYS                                              
SEQRES   1 B  368  TYR ASN VAL PHE PRO ARG THR LEU LYS TRP SER LYS MET          
SEQRES   2 B  368  ASN LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP MET          
SEQRES   3 B  368  THR HIS SER GLU VAL GLU LYS ALA PHE LYS LYS ALA PHE          
SEQRES   4 B  368  LYS VAL TRP SER ASP VAL THR PRO LEU ASN PHE THR ARG          
SEQRES   5 B  368  LEU HIS ASP GLY ILE ALA ASP ILE MET ILE SER PHE GLY          
SEQRES   6 B  368  ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO          
SEQRES   7 B  368  SER GLY LEU LEU ALA HIS ALA PHE PRO PRO GLY PRO ASN          
SEQRES   8 B  368  TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP GLU THR TRP          
SEQRES   9 B  368  THR SER SER SER LYS GLY TYR ASN LEU PHE LEU VAL ALA          
SEQRES  10 B  368  ALA HIS ALA PHE GLY HIS SER LEU GLY LEU ASP HIS SER          
SEQRES  11 B  368  LYS ASP PRO GLY ALA LEU MET PHE PRO ILE TYR THR TYR          
SEQRES  12 B  368  THR GLY LYS SER HIS PHE MET LEU PRO ASP ASP ASP VAL          
SEQRES  13 B  368  GLN GLY ILE GLN SER LEU TYR GLY PRO GLY ASP GLU ASP          
SEQRES  14 B  368  PRO ASN PRO LYS HIS PRO LYS THR PRO ASP LYS CYS ASP          
SEQRES  15 B  368  PRO SER LEU SER LEU ASP ALA ILE THR SER LEU ARG GLY          
SEQRES  16 B  368  GLU THR MET ILE PHE LYS ASP ARG PHE PHE TRP ARG LEU          
SEQRES  17 B  368  HIS PRO GLN GLN VAL ASP ALA GLU LEU PHE LEU THR LYS          
SEQRES  18 B  368  SER PHE TRP PRO GLU LEU PRO ASN ARG ILE ASP ALA ALA          
SEQRES  19 B  368  TYR GLU HIS PRO SER HIS ASP LEU ILE PHE ILE PHE ARG          
SEQRES  20 B  368  GLY ARG LYS PHE TRP ALA LEU ASN GLY TYR ASP ILE LEU          
SEQRES  21 B  368  GLU GLY TYR PRO LYS LYS ILE SER GLU LEU GLY LEU PRO          
SEQRES  22 B  368  LYS GLU VAL LYS LYS ILE SER ALA ALA VAL HIS PHE GLU          
SEQRES  23 B  368  ASP THR GLY LYS THR LEU LEU PHE SER GLY ASN GLN VAL          
SEQRES  24 B  368  TRP ARG TYR ASP ASP THR ASN HIS ILE MET ASP LYS ASP          
SEQRES  25 B  368  TYR PRO ARG LEU ILE GLU GLU ASP PHE PRO GLY ILE GLY          
SEQRES  26 B  368  ASP LYS VAL ASP ALA VAL TYR GLU LYS ASN GLY TYR ILE          
SEQRES  27 B  368  TYR PHE PHE ASN GLY PRO ILE GLN PHE GLU TYR SER ILE          
SEQRES  28 B  368  TRP SER ASN ARG ILE VAL ARG VAL MET PRO ALA ASN SER          
SEQRES  29 B  368  ILE LEU TRP CYS                                              
SEQRES   1 C   20  LEU SER GLU GLU ASP LEU GLN PHE ALA GLU ARG TYR LEU          
SEQRES   2 C   20  ARG SER TYR TYR HIS PRO THR                                  
SEQRES   1 D   20  LEU SER GLU GLU ASP LEU GLN PHE ALA GLU ARG TYR LEU          
SEQRES   2 D   20  ARG SER TYR TYR HIS PRO THR                                  
HET     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET     CA  A 503       1                                                       
HET     CA  A 504       1                                                       
HET     CA  A 505       1                                                       
HET     CA  A 506       1                                                       
HET     CA  A 507       1                                                       
HET     CL  A 508       1                                                       
HET     CL  A 509       1                                                       
HET    GOL  A 510       6                                                       
HET    GOL  A 511       6                                                       
HET    GOL  A 512       6                                                       
HET    PGO  A 513       5                                                       
HET    PGO  A 514       5                                                       
HET    PGO  A 515       5                                                       
HET    PGO  A 516       5                                                       
HET    PGO  A 517       5                                                       
HET    PGO  A 518       5                                                       
HET    PGO  A 519       5                                                       
HET    PGO  A 520       5                                                       
HET    PGO  A 521       5                                                       
HET    PGO  A 522       5                                                       
HET    PGO  A 523       5                                                       
HET    PGO  A 524       5                                                       
HET    PGO  A 525       5                                                       
HET    PGO  A 526       5                                                       
HET    PGO  A 527       5                                                       
HET    PEG  A 528       7                                                       
HET    PEG  A 529       7                                                       
HET    PEG  A 530       7                                                       
HET    PEG  A 531       7                                                       
HET    PEG  A 532       7                                                       
HET     ZN  B 501       1                                                       
HET     ZN  B 502       1                                                       
HET     CA  B 503       1                                                       
HET     CA  B 504       1                                                       
HET     CA  B 505       1                                                       
HET     CA  B 506       1                                                       
HET     CA  B 507       1                                                       
HET     CL  B 508       1                                                       
HET    GOL  B 509       6                                                       
HET    GOL  B 510       6                                                       
HET    GOL  B 511       6                                                       
HET    GOL  B 512       6                                                       
HET    GOL  B 513       6                                                       
HET    GOL  B 514       6                                                       
HET    GOL  B 515       6                                                       
HET    PGO  B 516       5                                                       
HET    PGO  B 517       5                                                       
HET    PGO  B 518       5                                                       
HET    PGO  B 519       5                                                       
HET    PGO  B 520       5                                                       
HET    PGO  B 521       5                                                       
HET    PGO  B 522       5                                                       
HET    PGO  B 523       5                                                       
HET    PGO  B 524       5                                                       
HET    PGO  B 525       5                                                       
HET    PGO  B 526       5                                                       
HET    PGO  B 527       5                                                       
HET    PEG  B 528       7                                                       
HET    PEG  B 529       7                                                       
HET    PEG  B 530       7                                                       
HET    PGO  C 101       5                                                       
HET    PEG  D 101       7                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM     PGO S-1,2-PROPANEDIOL                                                
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   7   CA    10(CA 2+)                                                    
FORMUL  12   CL    3(CL 1-)                                                     
FORMUL  14  GOL    10(C3 H8 O3)                                                 
FORMUL  17  PGO    28(C3 H8 O2)                                                 
FORMUL  32  PEG    9(C4 H10 O3)                                                 
FORMUL  69  HOH   *234(H2 O)                                                    
HELIX    1   1 PRO A  108  LEU A  111  5                                   4    
HELIX    2   2 THR A  130  ASP A  147  1                                  18    
HELIX    3   3 LEU A  216  GLY A  229  1                                  14    
HELIX    4   4 PRO A  255  GLY A  267  1                                  13    
HELIX    5   5 THR A  323  TRP A  327  1                                   5    
HELIX    6   6 PRO A  341  ASP A  344  5                                   4    
HELIX    7   7 SER A  371  GLY A  374  5                                   4    
HELIX    8   8 ILE A  420  PHE A  424  1                                   5    
HELIX    9   9 ASN A  466  TRP A  470  5                                   5    
HELIX   10  10 THR B  130  ASP B  147  1                                  18    
HELIX   11  11 LEU B  216  GLY B  229  1                                  14    
HELIX   12  12 PRO B  255  GLY B  267  1                                  13    
HELIX   13  13 LYS B  324  PHE B  326  5                                   3    
HELIX   14  14 SER B  371  GLY B  374  5                                   4    
HELIX   15  15 ILE B  420  PHE B  424  1                                   5    
HELIX   16  16 ASN B  466  TRP B  470  5                                   5    
HELIX   17  17 SER D   32  LEU D   43  1                                  12    
SHEET    1   A 2 ASN A 105  VAL A 106  0                                        
SHEET    2   A 2 LEU A 230  ASP A 231 -1  O  ASP A 231   N  ASN A 105           
SHEET    1   B 6 ASN A 152  ARG A 155  0                                        
SHEET    2   B 6 ASN A 117  ILE A 122  1  N  LEU A 118   O  ASN A 152           
SHEET    3   B 6 ILE A 163  GLY A 168  1  O  ILE A 165   N  ARG A 121           
SHEET    4   B 6 ALA A 199  ASP A 202  1  O  PHE A 201   N  GLY A 168           
SHEET    5   B 6 GLY A 183  ALA A 188 -1  N  HIS A 187   O  HIS A 200           
SHEET    6   B 6 ARG C  44  HIS C  48 -1  O  TYR C  46   N  LEU A 185           
SHEET    1   C 2 TRP A 207  THR A 208  0                                        
SHEET    2   C 2 TYR A 214  ASN A 215  1  O  TYR A 214   N  THR A 208           
SHEET    1   D 4 ALA A 292  LEU A 296  0                                        
SHEET    2   D 4 GLU A 299  LYS A 304 -1  O  MET A 301   N  THR A 294           
SHEET    3   D 4 PHE A 307  LEU A 311 -1  O  TRP A 309   N  ILE A 302           
SHEET    4   D 4 GLU A 319  LEU A 322 -1  O  PHE A 321   N  PHE A 308           
SHEET    1   E 4 ALA A 336  HIS A 340  0                                        
SHEET    2   E 4 LEU A 345  ARG A 350 -1  O  PHE A 347   N  TYR A 338           
SHEET    3   E 4 LYS A 353  ASN A 358 -1  O  LEU A 357   N  ILE A 346           
SHEET    4   E 4 ASP A 361  ILE A 362 -1  O  ASP A 361   N  ASN A 358           
SHEET    1   F 4 ALA A 336  HIS A 340  0                                        
SHEET    2   F 4 LEU A 345  ARG A 350 -1  O  PHE A 347   N  TYR A 338           
SHEET    3   F 4 LYS A 353  ASN A 358 -1  O  LEU A 357   N  ILE A 346           
SHEET    4   F 4 LYS A 368  LYS A 369 -1  O  LYS A 368   N  PHE A 354           
SHEET    1   G 4 ALA A 384  HIS A 387  0                                        
SHEET    2   G 4 LYS A 393  SER A 398 -1  O  LEU A 395   N  VAL A 386           
SHEET    3   G 4 GLN A 401  ASP A 406 -1  O  TYR A 405   N  THR A 394           
SHEET    4   G 4 ILE A 411  MET A 412 -1  O  ILE A 411   N  ASP A 406           
SHEET    1   H 4 ALA A 384  HIS A 387  0                                        
SHEET    2   H 4 LYS A 393  SER A 398 -1  O  LEU A 395   N  VAL A 386           
SHEET    3   H 4 GLN A 401  ASP A 406 -1  O  TYR A 405   N  THR A 394           
SHEET    4   H 4 ARG A 418  LEU A 419 -1  O  ARG A 418   N  VAL A 402           
SHEET    1   I 4 ALA A 433  LYS A 437  0                                        
SHEET    2   I 4 TYR A 440  ASN A 445 -1  O  TYR A 442   N  TYR A 435           
SHEET    3   I 4 ILE A 448  SER A 453 -1  O  TYR A 452   N  ILE A 441           
SHEET    4   I 4 ARG A 458  PRO A 464 -1  O  ARG A 458   N  SER A 453           
SHEET    1   J 2 ASN B 105  VAL B 106  0                                        
SHEET    2   J 2 LEU B 230  ASP B 231 -1  O  ASP B 231   N  ASN B 105           
SHEET    1   K 6 ASN B 152  ARG B 155  0                                        
SHEET    2   K 6 ASN B 117  ILE B 122  1  N  LEU B 118   O  ASN B 152           
SHEET    3   K 6 ILE B 163  GLY B 168  1  O  ILE B 165   N  ARG B 121           
SHEET    4   K 6 ALA B 199  ASP B 202  1  O  PHE B 201   N  GLY B 168           
SHEET    5   K 6 GLY B 183  ALA B 188 -1  N  HIS B 187   O  HIS B 200           
SHEET    6   K 6 ARG D  44  HIS D  48 -1  O  TYR D  46   N  LEU B 185           
SHEET    1   L 2 TRP B 207  THR B 208  0                                        
SHEET    2   L 2 TYR B 214  ASN B 215  1  O  TYR B 214   N  THR B 208           
SHEET    1   M 4 ALA B 292  LEU B 296  0                                        
SHEET    2   M 4 GLU B 299  LYS B 304 -1  O  MET B 301   N  THR B 294           
SHEET    3   M 4 PHE B 307  LEU B 311 -1  O  TRP B 309   N  ILE B 302           
SHEET    4   M 4 GLU B 319  LEU B 322 -1  O  GLU B 319   N  ARG B 310           
SHEET    1   N 4 ALA B 336  HIS B 340  0                                        
SHEET    2   N 4 LEU B 345  ARG B 350 -1  O  PHE B 347   N  TYR B 338           
SHEET    3   N 4 LYS B 353  ASN B 358 -1  O  LEU B 357   N  ILE B 346           
SHEET    4   N 4 ASP B 361  ILE B 362 -1  O  ASP B 361   N  ASN B 358           
SHEET    1   O 4 ALA B 336  HIS B 340  0                                        
SHEET    2   O 4 LEU B 345  ARG B 350 -1  O  PHE B 347   N  TYR B 338           
SHEET    3   O 4 LYS B 353  ASN B 358 -1  O  LEU B 357   N  ILE B 346           
SHEET    4   O 4 LYS B 368  LYS B 369 -1  O  LYS B 368   N  PHE B 354           
SHEET    1   P 4 ALA B 384  HIS B 387  0                                        
SHEET    2   P 4 LYS B 393  SER B 398 -1  O  PHE B 397   N  ALA B 384           
SHEET    3   P 4 GLN B 401  ASP B 406 -1  O  TRP B 403   N  LEU B 396           
SHEET    4   P 4 ILE B 411  MET B 412 -1  O  ILE B 411   N  ASP B 406           
SHEET    1   Q 4 ALA B 384  HIS B 387  0                                        
SHEET    2   Q 4 LYS B 393  SER B 398 -1  O  PHE B 397   N  ALA B 384           
SHEET    3   Q 4 GLN B 401  ASP B 406 -1  O  TRP B 403   N  LEU B 396           
SHEET    4   Q 4 ARG B 418  LEU B 419 -1  O  ARG B 418   N  VAL B 402           
SHEET    1   R 4 ALA B 433  LYS B 437  0                                        
SHEET    2   R 4 TYR B 440  ASN B 445 -1  O  TYR B 442   N  TYR B 435           
SHEET    3   R 4 ILE B 448  SER B 453 -1  O  TYR B 452   N  ILE B 441           
SHEET    4   R 4 ARG B 458  PRO B 464 -1  O  MET B 463   N  GLN B 449           
SSBOND   1 CYS B  284    CYS B  471                          1555   1555  2.05  
LINK         NE2 HIS A 172                ZN    ZN A 502     1555   1555  1.82  
LINK         NE2 HIS A 226                ZN    ZN A 501     1555   1555  1.97  
LINK         NE2 HIS B 172                ZN    ZN B 502     1555   1555  2.00  
LINK         NE2 HIS B 222                ZN    ZN B 501     1555   1555  2.01  
LINK         ND1 HIS A 200                ZN    ZN A 502     1555   1555  2.02  
LINK         ND1 HIS B 200                ZN    ZN B 502     1555   1555  2.02  
LINK         OD2 ASP B 174                ZN    ZN B 502     1555   1555  2.03  
LINK         OD2 ASP A 174                ZN    ZN A 502     1555   1555  2.05  
LINK         NE2 HIS B 232                ZN    ZN B 501     1555   1555  2.05  
LINK         NE2 HIS A 232                ZN    ZN A 501     1555   1555  2.06  
LINK         NE2 HIS B 187                ZN    ZN B 502     1555   1555  2.09  
LINK         NE2 HIS B 226                ZN    ZN B 501     1555   1555  2.12  
LINK         NE2 HIS A 187                ZN    ZN A 502     1555   1555  2.12  
LINK         O   GLY B 180                CA    CA B 503     1555   1555  2.18  
LINK         NE2 HIS A 222                ZN    ZN A 501     1555   1555  2.18  
LINK         OE2 GLU B 205                CA    CA B 503     1555   1555  2.20  
LINK         O   ASP B 162                CA    CA B 504     1555   1555  2.20  
LINK         O   LEU A 184                CA    CA A 503     1555   1555  2.23  
LINK         O   ASP A 203                CA    CA A 507     1555   1555  2.23  
LINK         OD2 ASP A 202                CA    CA A 503     1555   1555  2.24  
LINK         O   ALA A 385                CA    CA A 506     1555   1555  2.24  
LINK         O   SER B 182                CA    CA B 503     1555   1555  2.25  
LINK         O   ASN B 194                CA    CA B 504     1555   1555  2.25  
LINK         OE2 GLU A 205                CA    CA A 503     1555   1555  2.26  
LINK         OD2 ASP B 202                CA    CA B 503     1555   1555  2.27  
LINK         O   ASN A 194                CA    CA A 504     1555   1555  2.27  
LINK         O   ASP A 162                CA    CA A 504     1555   1555  2.27  
LINK         O   ASP A 291                CA    CA A 505     1555   1555  2.27  
LINK        CA    CA B 504                 O   HOH B 633     1555   1555  2.28  
LINK         O   GLY A 180                CA    CA A 503     1555   1555  2.29  
LINK         O   ASP B 203                CA    CA B 507     1555   1555  2.32  
LINK         O   ASP A 432                CA    CA A 505     1555   1555  2.33  
LINK         O   ALA B 385                CA    CA B 506     1555   1555  2.33  
LINK         O   ILE A 293                CA    CA A 506     1555   1555  2.34  
LINK         O   ASP B 291                CA    CA B 505     1555   1555  2.35  
LINK         O   LEU B 184                CA    CA B 503     1555   1555  2.35  
LINK         O   GLY B 196                CA    CA B 504     1555   1555  2.35  
LINK         O   ASP B 335                CA    CA B 505     1555   1555  2.35  
LINK         O   ASP A 335                CA    CA A 505     1555   1555  2.36  
LINK         OD1 ASP B 179                CA    CA B 503     1555   1555  2.36  
LINK         O   SER B 383                CA    CA B 505     1555   1555  2.36  
LINK         O   GLU A 205                CA    CA A 507     1555   1555  2.38  
LINK         O   ALA B 337                CA    CA B 506     1555   1555  2.38  
LINK        CA    CA A 505                 O   HOH A 669     1555   1555  2.38  
LINK         O   ILE B 293                CA    CA B 506     1555   1555  2.38  
LINK         O   VAL B 434                CA    CA B 506     1555   1555  2.39  
LINK         O   ALA A 337                CA    CA A 506     1555   1555  2.40  
LINK        CA    CA A 504                 O   HOH A 663     1555   1555  2.42  
LINK         O   ASP B 432                CA    CA B 505     1555   1555  2.43  
LINK         O   GLU B 205                CA    CA B 507     1555   1555  2.43  
LINK         OD2 ASP A 128                CA    CA A 507     1555   1555  2.46  
LINK         OD2 ASP B 128                CA    CA B 507     1555   1555  2.47  
LINK         O   SER A 383                CA    CA A 505     1555   1555  2.47  
LINK         OD1 ASP B 198                CA    CA B 504     1555   1555  2.47  
LINK        ZN    ZN A 501                 O  BHOH C 204     1555   1555  2.49  
LINK         OD1 ASP A 179                CA    CA A 503     1555   1555  2.49  
LINK        CA    CA B 505                 O   HOH B 606     1555   1555  2.49  
LINK        CA    CA A 505                 O   HOH A 605     1555   1555  2.50  
LINK        CA    CA A 504                 O   HOH A 619     1555   1555  2.51  
LINK         O   VAL A 434                CA    CA A 506     1555   1555  2.51  
LINK         O   SER A 182                CA    CA A 503     1555   1555  2.52  
LINK        CA    CA B 504                 O   HOH B 713     1555   1555  2.57  
LINK        CA    CA B 505                 O   HOH B 661     1555   1555  2.58  
LINK         O   GLY A 196                CA    CA A 504     1555   1555  2.58  
LINK         OD1 ASP A 198                CA    CA A 504     1555   1555  2.60  
LINK        CA    CA A 505                 O   HOH A 612     1555   1555  2.61  
LINK         OD2 ASP B 203                CA    CA B 507     1555   1555  2.65  
LINK        CA    CA B 505                 O   HOH B 615     1555   1555  2.71  
LINK        CA    CA B 506                 O   HOH B 617     1555   1555  2.73  
LINK         OD2 ASP A 203                CA    CA A 507     1555   1555  2.88  
LINK         OD1 ASP B 128                CA    CA B 507     1555   1555  3.03  
CISPEP   1 TYR A  366    PRO A  367          0         3.54                     
CISPEP   2 TYR A  416    PRO A  417          0         8.23                     
CISPEP   3 TYR B  366    PRO B  367          0         4.39                     
CISPEP   4 TYR B  416    PRO B  417          0         5.25                     
SITE     1 AC1  5 HIS A 222  HIS A 226  HIS A 232  SER C  45                    
SITE     2 AC1  5 HOH C 204                                                     
SITE     1 AC2  4 HIS A 172  ASP A 174  HIS A 187  HIS A 200                    
SITE     1 AC3  6 ASP A 179  GLY A 180  SER A 182  LEU A 184                    
SITE     2 AC3  6 ASP A 202  GLU A 205                                          
SITE     1 AC4  6 ASP A 162  ASN A 194  GLY A 196  ASP A 198                    
SITE     2 AC4  6 HOH A 619  HOH A 663                                          
SITE     1 AC5  7 ASP A 291  ASP A 335  SER A 383  ASP A 432                    
SITE     2 AC5  7 HOH A 605  HOH A 612  HOH A 669                               
SITE     1 AC6  6 ILE A 293  ALA A 337  ALA A 385  VAL A 434                    
SITE     2 AC6  6  CL A 508   CL A 509                                          
SITE     1 AC7  3 ASP A 128  ASP A 203  GLU A 205                               
SITE     1 AC8  7 ALA A 292  ILE A 293  ALA A 337  ALA A 385                    
SITE     2 AC8  7 ALA A 433  VAL A 434   CA A 506                               
SITE     1 AC9  5 ILE A 293  THR A 294   CA A 506  HOH A 621                    
SITE     2 AC9  5 HOH A 647                                                     
SITE     1 BC1  9 LYS A 140  ASN A 215  TYR A 246  GLY A 248                    
SITE     2 BC1  9 LYS A 249  SER A 250  HIS A 251  PHE A 252                    
SITE     3 BC1  9 PGO A 520                                                     
SITE     1 BC2  4 SER A 289  LEU A 290  ASP A 291  ASP A 432                    
SITE     1 BC3  3 THR A 247  MET A 253  ARG A 306                               
SITE     1 BC4  9 PRO A 236  GLY A 237  ALA A 238  ILE A 243                    
SITE     2 BC4  9 THR A 245  LEU A 322  HOH A 631  TYR C  46                    
SITE     3 BC4  9 HOH C 202                                                     
SITE     1 BC5  1 ASP A 270                                                     
SITE     1 BC6  3 GLY A 439  PGO A 517  ASP B 128                               
SITE     1 BC7  5 TYR A 440  TRP A 455  PGO A 516  HOH A 675                    
SITE     2 BC7  5 PRO B 127                                                     
SITE     1 BC8  3 GLU A 389  THR A 391  GLY A 392                               
SITE     1 BC9  7 PRO A 281  ASP A 282  ASP A 285  SER A 287                    
SITE     2 BC9  7 LEU A 288  LYS A 304  PEG A 531                               
SITE     1 CC1  5 LYS A 136  SER A 209  ASN A 215  GOL A 510                    
SITE     2 CC1  5 HOH A 650                                                     
SITE     1 CC2  4 THR A 208  SER A 210  HOH A 680  TRP B 455                    
SITE     1 CC3  2 GLN A 401  PRO A 417                                          
SITE     1 CC4  3 TYR A 125  HIS A 131  LEU A 419                               
SITE     1 CC5  7 SER A 295  GLU A 339  PRO A 341  HIS A 387                    
SITE     2 CC5  7 GLU A 389  GLU A 436  HOH A 647                               
SITE     1 CC6  5 TYR A 440  SER A 453  TRP A 455  SER A 456                    
SITE     2 CC6  5 VAL A 460                                                     
SITE     1 CC7  3 TYR A 416  ARG A 418  ASP A 423                               
SITE     1 CC8  2 TYR A 366  PRO A 367                                          
SITE     1 CC9  6 THR A 300  LEU A 311  ILE A 468  TRP A 470                    
SITE     2 CC9  6 HOH A 651  HOH A 654                                          
SITE     1 DC1  7 GLY A 248  LYS A 324  PRO A 331  ASN A 332                    
SITE     2 DC1  7 ARG A 333  ARG A 350  GLU D  33                               
SITE     1 DC2  2 THR A 280  ASP A 282                                          
SITE     1 DC3  7 SER A 287  LEU A 288  SER A 289  LYS A 304                    
SITE     2 DC3  7 GLY A 446  PRO A 447  PGO A 519                               
SITE     1 DC4  5 PRO A 313  GLN A 314  SER A 325  PRO C  49                    
SITE     2 DC4  5 THR C  50                                                     
SITE     1 DC5  5 HIS B 222  HIS B 226  HIS B 232  SER D  45                    
SITE     2 DC5  5 HOH D 207                                                     
SITE     1 DC6  4 HIS B 172  ASP B 174  HIS B 187  HIS B 200                    
SITE     1 DC7  6 ASP B 179  GLY B 180  SER B 182  LEU B 184                    
SITE     2 DC7  6 ASP B 202  GLU B 205                                          
SITE     1 DC8  6 ASP B 162  ASN B 194  GLY B 196  ASP B 198                    
SITE     2 DC8  6 HOH B 633  HOH B 713                                          
SITE     1 DC9  7 ASP B 291  ASP B 335  SER B 383  ASP B 432                    
SITE     2 DC9  7 HOH B 606  HOH B 615  HOH B 661                               
SITE     1 EC1  6 ILE B 293  ALA B 337  ALA B 385  VAL B 434                    
SITE     2 EC1  6  CL B 508  HOH B 617                                          
SITE     1 EC2  3 ASP B 128  ASP B 203  GLU B 205                               
SITE     1 EC3  5 ILE B 293  ALA B 337  ALA B 385  VAL B 434                    
SITE     2 EC3  5  CA B 506                                                     
SITE     1 EC4  6 GLU B 133  LYS B 136  LYS B 140  SER B 209                    
SITE     2 EC4  6 ASN B 215  GOL B 513                                          
SITE     1 EC5  3 HIS B 343  ASN B 358  HOH B 690                               
SITE     1 EC6  3 PRO A 464  ASN B 445  ILE B 448                               
SITE     1 EC7  9 ARG A 458  ILE A 459  VAL A 460  ARG A 461                    
SITE     2 EC7  9 GLU B 421  GLY B 426  ILE B 427  GLY B 428                    
SITE     3 EC7  9 HOH B 625                                                     
SITE     1 EC8  8 LYS B 140  ASN B 215  TYR B 246  GLY B 248                    
SITE     2 EC8  8 LYS B 249  SER B 250  PHE B 252  GOL B 509                    
SITE     1 EC9  2 LYS B 380  SER B 398                                          
SITE     1 FC1  6 PRO B 313  LYS B 437  HOH B 637  HOH B 658                    
SITE     2 FC1  6 PRO D  49  THR D  50                                          
SITE     1 FC2  4 LYS B 234  ASP B 235  PRO B 236  HOH B 687                    
SITE     1 FC3  3 TYR B 195  ASP B 198  HIS B 200                               
SITE     1 FC4  3 PRO B 376  GLU B 378  GLN B 401                               
SITE     1 FC5  5 SER B 146  THR B 149  PRO B 150  LEU B 151                    
SITE     2 FC5  5 HOH B 715                                                     
SITE     1 FC6  5 HIS B 232  SER B 233  LYS B 234  PRO B 242                    
SITE     2 FC6  5 PEG D 101                                                     
SITE     1 FC7  5 THR B 110  LYS B 112  SER B 114  GLY B 192                    
SITE     2 FC7  5 HOH B 708                                                     
SITE     1 FC8  4 TYR B 435  LYS B 437  GLN B 449  MET B 463                    
SITE     1 FC9  4 MET B 253  PRO B 255  PRO B 278  ARG B 306                    
SITE     1 GC1  4 HIS B 340  HIS B 387  ASP B 407  HOH B 691                    
SITE     1 GC2  2 ARG B 297  ASP B 344                                          
SITE     1 GC3  2 ASP B 282  ASP B 285                                          
SITE     1 GC4  5 SER B 211  THR B 245  TYR B 246  HOH B 712                    
SITE     2 GC4  5 HIS D  48                                                     
SITE     1 GC5  2 TYR B 104  HOH B 669                                          
SITE     1 GC6  9 PRO B 236  PHE B 241  ILE B 243  THR B 245                    
SITE     2 GC6  9 GLN B 314  LEU B 322  SER B 325  HOH B 624                    
SITE     3 GC6  9 HOH B 692                                                     
SITE     1 GC7  3 ALA C  39  ARG C  41  TYR C  42                               
SITE     1 GC8  7 PRO B 242  PGO B 520  ARG D  44  SER D  45                    
SITE     2 GC8  7 TYR D  47  HOH D 206  HOH D 210                               
CRYST1  125.780  157.270  105.550  90.00  90.00  90.00 C 2 2 21     16          
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      0.007950  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006358  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009474        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system