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Database: PDB
Entry: 4HMA
LinkDB: 4HMA
Original site: 4HMA 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           18-OCT-12   4HMA              
TITLE     CRYSTAL STRUCTURE OF AN MMP TWIN CARBOXYLATE BASED INHIBITOR LC20 IN  
TITLE    2 COMPLEX WITH THE MMP-9 CATALYTIC DOMAIN                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MATRIX METALLOPROTEINASE-9;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: MMP-9 CATALYTIC DOMAIN 107-215,391-443;                    
COMPND   5 SYNONYM: MMP-9, 92 KDA GELATINASE, 92 KDA TYPE IV COLLAGENASE,       
COMPND   6 GELATINASE B, GELB, 67 KDA MATRIX METALLOPROTEINASE-9, 82 KDA MATRIX 
COMPND   7 METALLOPROTEINASE-9;                                                 
COMPND   8 EC: 3.4.24.35;                                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CLG4B, MMP9;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3 STAR);                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PT7 PROMOTER;                         
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-14B                                   
KEYWDS    HYDROLASE/TWIN INHIBITOR, ZINCIN-LIKE, GELATINASE, COLLAGENASE        
KEYWDS   2 (CATALYTIC DOMAIN), HYDROLASE-HYDROLASE INHIBITOR COMPLEX            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.A.STURA,C.ANTONI,L.VERA,E.NUTI,L.CARAFA,E.CASSAR-LAJEUNESSE,V.DIVE, 
AUTHOR   2 A.ROSSELLO                                                           
REVDAT   5   09-AUG-17 4HMA    1       SOURCE REMARK                            
REVDAT   4   12-AUG-15 4HMA    1       JRNL                                     
REVDAT   3   08-OCT-14 4HMA    1       AUTHOR                                   
REVDAT   2   01-MAY-13 4HMA    1       AUTHOR                                   
REVDAT   1   24-APR-13 4HMA    0                                                
JRNL        AUTH   C.ANTONI,L.VERA,L.DEVEL,M.P.CATALANI,B.CZARNY,               
JRNL        AUTH 2 E.CASSAR-LAJEUNESSE,E.NUTI,A.ROSSELLO,V.DIVE,E.A.STURA       
JRNL        TITL   CRYSTALLIZATION OF BI-FUNCTIONAL LIGAND PROTEIN COMPLEXES.   
JRNL        REF    J.STRUCT.BIOL.                V. 182   246 2013              
JRNL        REFN                   ISSN 1047-8477                               
JRNL        PMID   23567804                                                     
JRNL        DOI    10.1016/J.JSB.2013.03.015                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.ROSSELLO,E.NUTI,M.P.CATALANI,P.CARELLI,E.ORLANDINI,        
REMARK   1  AUTH 2 S.RAPPOSELLI,T.TUCCINARDI,S.J.ATKINSON,G.MURPHY,A.BALSAMO    
REMARK   1  TITL   A NEW DEVELOPMENT OF MATRIX METALLOPROTEINASE INHIBITORS:    
REMARK   1  TITL 2 TWIN HYDROXAMIC ACIDS AS POTENT INHIBITORS OF MMPS.          
REMARK   1  REF    BIOORG.MED.CHEM.LETT.         V.  15  2311 2005              
REMARK   1  REFN                   ISSN 0960-894X                               
REMARK   1  PMID   15837315                                                     
REMARK   1  DOI    10.1016/J.BMCL.2005.03.002                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.94 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.72                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 24713                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1301                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.94                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.99                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1674                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3200                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 88                           
REMARK   3   BIN FREE R VALUE                    : 0.3730                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2550                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 190                                     
REMARK   3   SOLVENT ATOMS            : 345                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.56                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.82000                                              
REMARK   3    B22 (A**2) : -0.65000                                             
REMARK   3    B33 (A**2) : -0.18000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.212         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.199         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.145         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.156         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2871 ; 0.022 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3886 ; 1.966 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   331 ; 6.740 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   144 ;35.336 ;23.611       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   371 ;16.531 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;24.017 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   374 ; 0.158 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2296 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1627 ; 1.241 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2599 ; 2.120 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1244 ; 3.114 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1287 ; 4.572 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4HMA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000075643.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
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) : 0.98011                            
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : BENT CYLINDRICAL MIRROR            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26019                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.940                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 7.980                              
REMARK 200  R MERGE                    (I) : 0.16600                            
REMARK 200  R SYM                      (I) : 0.15500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1900                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.87                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.53300                            
REMARK 200  R SYM FOR SHELL            (I) : 1.43200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
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: 4H82                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: HUMAN MMP9 (E402Q) AT 308.7     
REMARK 280  MICRO-M TWIN INHIBITOR LC20 AT 154 MICRO-M (STOICHIOMETRY 2:1)      
REMARK 280  AND 120MM ACETOHYDROXAMIC ACID. RESERVOIR: 12% POLYETHYLENE         
REMARK 280  GLYCOL 20,000, 1.5M NACL, 0.1 M PCTP (NA PROPIONATE, NA             
REMARK 280  CACODYLATE, BIS-TRIS-PROPANE RATIO 2:1:2; 75% PH 4, 25% PH 9.5)     
REMARK 280  CRYOPROTECTANT: 40% C2 (25 % DI-ETHYLENE GLYCOL + 25 % GLYCEROL +   
REMARK 280  25 % 1,2-PROPANEDIOL), 9% PEG 10,000 1.5M NACL, 0.1M PCTP 80/2,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K, PH 6               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.93500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.12000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.93500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.12000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE TWIN INHIBITOR 0Z CAUSE THE ENZYME TO FORM A DIMER       
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: 4570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A 173     -119.27     49.55                                   
REMARK 500    ASP A 185     -169.00     69.23                                   
REMARK 500    PRO A 246       30.77    -72.70                                   
REMARK 500    ALA B 173     -132.27     54.61                                   
REMARK 500    ASP B 185     -167.90     70.71                                   
REMARK 500    PRO B 246       44.58    -90.15                                   
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 302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 177   OD2                                                    
REMARK 620 2 HIS A 175   NE2 124.1                                              
REMARK 620 3 HIS A 203   ND1  89.7 116.1                                        
REMARK 620 4 HIS A 190   NE2  96.3 116.5 110.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 0ZD A 306   O22                                                    
REMARK 620 2 HIS A 236   NE2  93.6                                              
REMARK 620 3 HIS A 230   NE2 122.7  94.2                                        
REMARK 620 4 HIS A 226   NE2 127.3 108.8 103.0                                  
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 226   NE2                                                    
REMARK 620 2 0ZD A 306   O62 110.4                                              
REMARK 620 3 HIS B 230   NE2 100.9 134.8                                        
REMARK 620 4 HIS B 236   NE2 113.7  99.6  96.4                                  
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 ASP B 177   OD1                                                    
REMARK 620 2 HIS B 203   ND1  99.6                                              
REMARK 620 3 HIS B 175   NE2 124.0  96.2                                        
REMARK 620 4 HIS B 190   NE2 103.1 114.2 118.3                                  
REMARK 620 N                    1     2     3                                   
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 GLU B 208   OE1                                                    
REMARK 620 2 ASP B 205   OD2  92.6                                              
REMARK 620 3 GLY B 183   O    93.4  87.3                                        
REMARK 620 4 ASP B 185   O    82.7 173.6  88.7                                  
REMARK 620 5 LEU B 187   O    85.0  93.4 178.3  90.4                            
REMARK 620 6 ASP B 182   OD1 166.2 100.3  82.5  84.0  98.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 305  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 208   O                                                      
REMARK 620 2 ASP A 131   OD1  93.2                                              
REMARK 620 3 ASP A 206   OD1 125.0  97.9                                        
REMARK 620 4 ASP A 206   O    91.9 170.6  72.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 304  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 208   OE1                                                    
REMARK 620 2 ASP A 182   OD2 160.2                                              
REMARK 620 3 LEU A 187   O    86.6 101.4                                        
REMARK 620 4 GLY A 183   O    93.1  78.8 179.7                                  
REMARK 620 5 ASP A 185   O    82.3  78.5 100.9  79.0                            
REMARK 620 6 ASP A 205   OD2  94.6 102.6  94.7  85.4 163.8                      
REMARK 620 N                    1     2     3     4     5                       
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 GLU B 208   O                                                      
REMARK 620 2 ASP B 131   OD2  91.8                                              
REMARK 620 3 ASP B 206   OD1 106.6  94.2                                        
REMARK 620 4 ASP B 206   O    88.9 163.9  70.3                                  
REMARK 620 5 HOH B 681   O    82.2 105.2 158.6  90.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 303  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 165   O                                                      
REMARK 620 2 ASP A 201   OD1  92.6                                              
REMARK 620 3 GLY A 197   O   168.0  93.0                                        
REMARK 620 4 GLN A 199   O   105.6  99.3  84.0                                  
REMARK 620 5 GLN A 199   O   105.4 100.7  84.1   1.4                            
REMARK 620 6 HOH A 446   O    91.7  94.2  77.3 157.5 156.7                      
REMARK 620 7 HOH A 445   O    84.9 176.0  90.0  78.5  77.1  89.0                
REMARK 620 N                    1     2     3     4     5     6                 
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 GLN B 199   O                                                      
REMARK 620 2 ASP B 165   O   109.4                                              
REMARK 620 3 ASP B 201   OD1  94.6  89.8                                        
REMARK 620 4 GLY B 197   O    82.0 168.6  87.9                                  
REMARK 620 5 HOH B 612   O   163.6  86.7  88.5  82.0                            
REMARK 620 6 HOH B 611   O    86.5  88.5 178.2  93.7  90.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0ZD A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 312                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 313                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 314                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 315                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 316                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 317                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLT B 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 513                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4H2E   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF AN MMP TWIN INHIBITOR COMPLEXING TWO MMP-9      
REMARK 900 CATALYTIC DOMAINS                                                    
REMARK 900 RELATED ID: 4H1Q   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MUTANT MMP-9 CATALYTIC DOMAIN IN COMPLEX WITH   
REMARK 900 A TWIN INHIBITOR.                                                    
REMARK 900 RELATED ID: 4H82   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MUTANT MMP-9 CATALYTIC DOMAIN IN COMPLEX WITH   
REMARK 900 A TWIN INHIBITOR.                                                    
REMARK 900 RELATED ID: 4H3X   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF AN MMP BROAD SPECTRUM HYDROXAMATE BASED         
REMARK 900 INHIBITOR CC27 IN COMPLEX WITH THE MMP-9 CATALYTIC DOMAIN            
REMARK 900 RELATED ID: 4H30   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF MMP-12 IN COMPLEX WITH  
REMARK 900 A TWIN INHIBITOR.                                                    
DBREF  4HMA A  110   214  UNP    P14780   MMP9_HUMAN     110    214             
DBREF  4HMA A  216   269  UNP    P14780   MMP9_HUMAN     391    444             
DBREF  4HMA B  110   214  UNP    P14780   MMP9_HUMAN     110    214             
DBREF  4HMA B  216   269  UNP    P14780   MMP9_HUMAN     391    444             
SEQADV 4HMA GLN A  227  UNP  P14780    GLU   402 ENGINEERED MUTATION            
SEQADV 4HMA GLN B  227  UNP  P14780    GLU   402 ENGINEERED MUTATION            
SEQRES   1 A  160  PHE GLU GLY ASP LEU LYS TRP HIS HIS HIS ASN ILE THR          
SEQRES   2 A  160  TYR TRP ILE GLN ASN TYR SER GLU ASP LEU PRO ARG ALA          
SEQRES   3 A  160  VAL ILE ASP ASP ALA PHE ALA ARG ALA PHE ALA LEU TRP          
SEQRES   4 A  160  SER ALA VAL THR PRO LEU THR PHE THR ARG VAL TYR SER          
SEQRES   5 A  160  ARG ASP ALA ASP ILE VAL ILE GLN PHE GLY VAL ALA GLU          
SEQRES   6 A  160  HIS GLY ASP GLY TYR PRO PHE ASP GLY LYS ASP GLY LEU          
SEQRES   7 A  160  LEU ALA HIS ALA PHE PRO PRO GLY PRO GLY ILE GLN GLY          
SEQRES   8 A  160  ASP ALA HIS PHE ASP ASP ASP GLU LEU TRP SER LEU GLY          
SEQRES   9 A  160  LYS GLY GLN GLY TYR SER LEU PHE LEU VAL ALA ALA HIS          
SEQRES  10 A  160  GLN PHE GLY HIS ALA LEU GLY LEU ASP HIS SER SER VAL          
SEQRES  11 A  160  PRO GLU ALA LEU MET TYR PRO MET TYR ARG PHE THR GLU          
SEQRES  12 A  160  GLY PRO PRO LEU HIS LYS ASP ASP VAL ASN GLY ILE ARG          
SEQRES  13 A  160  HIS LEU TYR GLY                                              
SEQRES   1 B  160  PHE GLU GLY ASP LEU LYS TRP HIS HIS HIS ASN ILE THR          
SEQRES   2 B  160  TYR TRP ILE GLN ASN TYR SER GLU ASP LEU PRO ARG ALA          
SEQRES   3 B  160  VAL ILE ASP ASP ALA PHE ALA ARG ALA PHE ALA LEU TRP          
SEQRES   4 B  160  SER ALA VAL THR PRO LEU THR PHE THR ARG VAL TYR SER          
SEQRES   5 B  160  ARG ASP ALA ASP ILE VAL ILE GLN PHE GLY VAL ALA GLU          
SEQRES   6 B  160  HIS GLY ASP GLY TYR PRO PHE ASP GLY LYS ASP GLY LEU          
SEQRES   7 B  160  LEU ALA HIS ALA PHE PRO PRO GLY PRO GLY ILE GLN GLY          
SEQRES   8 B  160  ASP ALA HIS PHE ASP ASP ASP GLU LEU TRP SER LEU GLY          
SEQRES   9 B  160  LYS GLY GLN GLY TYR SER LEU PHE LEU VAL ALA ALA HIS          
SEQRES  10 B  160  GLN PHE GLY HIS ALA LEU GLY LEU ASP HIS SER SER VAL          
SEQRES  11 B  160  PRO GLU ALA LEU MET TYR PRO MET TYR ARG PHE THR GLU          
SEQRES  12 B  160  GLY PRO PRO LEU HIS LYS ASP ASP VAL ASN GLY ILE ARG          
SEQRES  13 B  160  HIS LEU TYR GLY                                              
HET     ZN  A 301       1                                                       
HET     ZN  A 302       1                                                       
HET     CA  A 303       1                                                       
HET     CA  A 304       1                                                       
HET     CA  A 305       1                                                       
HET    0ZD  A 306      62                                                       
HET    GOL  A 307       6                                                       
HET    GOL  A 308       6                                                       
HET    GOL  A 309       6                                                       
HET    PGO  A 310       5                                                       
HET    PGO  A 311       5                                                       
HET    PGO  A 312       5                                                       
HET    PEG  A 313       7                                                       
HET    PEG  A 314       7                                                       
HET    PEG  A 315       7                                                       
HET    PEG  A 316       7                                                       
HET    PEG  A 317       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    MLT  B 506       9                                                       
HET    GOL  B 507       6                                                       
HET    GOL  B 508       6                                                       
HET    PGO  B 509       5                                                       
HET    PGO  B 510       5                                                       
HET    PGO  B 511       5                                                       
HET    PEG  B 512       7                                                       
HET    PEG  B 513       7                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     0ZD N,N'-BIS(2-[(BIPHENYL-4YLSULFONYL)[(2R)-1-HYDROXY-3-             
HETNAM   2 0ZD  METHYL-1-OXOBUTAN-2-YL]-AMINO]ETHYL)BENZENE-1,3-                
HETNAM   3 0ZD  DICARBOXAMIDE                                                   
HETNAM     GOL GLYCEROL                                                         
HETNAM     PGO S-1,2-PROPANEDIOL                                                
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     MLT D-MALATE                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     MLT (2R)-2-HYDROXYBUTANEDIOIC ACID; 2-HYDROXY-SUCCINIC ACID          
FORMUL   3   ZN    4(ZN 2+)                                                     
FORMUL   5   CA    6(CA 2+)                                                     
FORMUL   8  0ZD    C46 H50 N4 O10 S2                                            
FORMUL   9  GOL    5(C3 H8 O3)                                                  
FORMUL  12  PGO    6(C3 H8 O2)                                                  
FORMUL  15  PEG    7(C4 H10 O3)                                                 
FORMUL  25  MLT    C4 H6 O5                                                     
FORMUL  33  HOH   *345(H2 O)                                                    
HELIX    1   1 PRO A  133  THR A  152  1                                  20    
HELIX    2   2 LEU A  220  LEU A  232  1                                  13    
HELIX    3   3 HIS A  257  GLY A  269  1                                  13    
HELIX    4   4 PRO B  133  VAL B  151  1                                  19    
HELIX    5   5 LEU B  220  GLY B  233  1                                  14    
HELIX    6   6 HIS B  257  GLY B  269  1                                  13    
SHEET    1   A 5 THR A 155  ARG A 158  0                                        
SHEET    2   A 5 ASN A 120  ILE A 125  1  N  ILE A 121   O  THR A 155           
SHEET    3   A 5 ILE A 166  GLY A 171  1  O  ILE A 168   N  TRP A 124           
SHEET    4   A 5 ALA A 202  ASP A 205  1  O  PHE A 204   N  GLN A 169           
SHEET    5   A 5 ALA A 189  ALA A 191 -1  N  HIS A 190   O  HIS A 203           
SHEET    1   B 2 TRP A 210  SER A 211  0                                        
SHEET    2   B 2 TYR A 218  SER A 219  1  O  TYR A 218   N  SER A 211           
SHEET    1   C 5 THR B 155  ARG B 158  0                                        
SHEET    2   C 5 ASN B 120  ILE B 125  1  N  ILE B 121   O  THR B 155           
SHEET    3   C 5 ILE B 166  GLY B 171  1  O  ILE B 168   N  TRP B 124           
SHEET    4   C 5 ALA B 202  ASP B 205  1  O  PHE B 204   N  GLN B 169           
SHEET    5   C 5 ALA B 189  ALA B 191 -1  N  HIS B 190   O  HIS B 203           
SHEET    1   D 2 TRP B 210  SER B 211  0                                        
SHEET    2   D 2 TYR B 218  SER B 219  1  O  TYR B 218   N  SER B 211           
LINK         OD2 ASP A 177                ZN    ZN A 302     1555   1555  1.89  
LINK        ZN    ZN A 301                 O22 0ZD A 306     1555   1555  1.90  
LINK         NE2 HIS B 226                ZN    ZN B 501     1555   1555  1.95  
LINK         O62 0ZD A 306                ZN    ZN B 501     1555   1555  1.97  
LINK         NE2 HIS A 236                ZN    ZN A 301     1555   1555  1.99  
LINK         OD1 ASP B 177                ZN    ZN B 502     1555   1555  2.00  
LINK         NE2 HIS A 230                ZN    ZN A 301     1555   1555  2.00  
LINK         ND1 HIS B 203                ZN    ZN B 502     1555   1555  2.00  
LINK         NE2 HIS A 175                ZN    ZN A 302     1555   1555  2.05  
LINK         NE2 HIS B 175                ZN    ZN B 502     1555   1555  2.05  
LINK         NE2 HIS B 230                ZN    ZN B 501     1555   1555  2.05  
LINK         NE2 HIS B 190                ZN    ZN B 502     1555   1555  2.06  
LINK         NE2 HIS A 226                ZN    ZN A 301     1555   1555  2.07  
LINK         ND1 HIS A 203                ZN    ZN A 302     1555   1555  2.08  
LINK         NE2 HIS B 236                ZN    ZN B 501     1555   1555  2.12  
LINK         OE1 GLU B 208                CA    CA B 504     1555   1555  2.15  
LINK         O   GLU A 208                CA    CA A 305     1555   1555  2.18  
LINK         OD1 ASP A 131                CA    CA A 305     1555   1555  2.20  
LINK         OE1 GLU A 208                CA    CA A 304     1555   1555  2.21  
LINK         OD2 ASP B 205                CA    CA B 504     1555   1555  2.22  
LINK         O   GLU B 208                CA    CA B 505     1555   1555  2.23  
LINK         NE2 HIS A 190                ZN    ZN A 302     1555   1555  2.24  
LINK         O   GLY B 183                CA    CA B 504     1555   1555  2.24  
LINK         O   ASP A 165                CA    CA A 303     1555   1555  2.27  
LINK         O   ASP B 185                CA    CA B 504     1555   1555  2.27  
LINK         O   GLN B 199                CA    CA B 503     1555   1555  2.28  
LINK         OD1 ASP A 201                CA    CA A 303     1555   1555  2.28  
LINK         O   ASP B 165                CA    CA B 503     1555   1555  2.29  
LINK         OD2 ASP B 131                CA    CA B 505     1555   1555  2.30  
LINK         OD2 ASP A 182                CA    CA A 304     1555   1555  2.32  
LINK         O   GLY A 197                CA    CA A 303     1555   1555  2.34  
LINK         O   LEU A 187                CA    CA A 304     1555   1555  2.36  
LINK         OD1 ASP B 201                CA    CA B 503     1555   1555  2.38  
LINK         O   LEU B 187                CA    CA B 504     1555   1555  2.40  
LINK         O   GLY A 183                CA    CA A 304     1555   1555  2.40  
LINK         OD1 ASP B 182                CA    CA B 504     1555   1555  2.41  
LINK         O   ASP A 185                CA    CA A 304     1555   1555  2.42  
LINK         O   GLY B 197                CA    CA B 503     1555   1555  2.43  
LINK         O  BGLN A 199                CA    CA A 303     1555   1555  2.43  
LINK         OD2 ASP A 205                CA    CA A 304     1555   1555  2.45  
LINK         OD1 ASP A 206                CA    CA A 305     1555   1555  2.45  
LINK         O  AGLN A 199                CA    CA A 303     1555   1555  2.47  
LINK         O   ASP A 206                CA    CA A 305     1555   1555  2.48  
LINK         OD1 ASP B 206                CA    CA B 505     1555   1555  2.58  
LINK         O   ASP B 206                CA    CA B 505     1555   1555  2.63  
LINK        CA    CA A 303                 O   HOH A 446     1555   1555  2.24  
LINK        CA    CA A 303                 O   HOH A 445     1555   1555  2.29  
LINK        CA    CA B 503                 O   HOH B 612     1555   1555  2.37  
LINK        CA    CA B 503                 O   HOH B 611     1555   1555  2.38  
LINK        CA    CA B 505                 O   HOH B 681     1555   1555  2.53  
CISPEP   1 GLY A  112    ASP A  113          0         6.13                     
SITE     1 AC1  4 HIS A 226  HIS A 230  HIS A 236  0ZD A 306                    
SITE     1 AC2  4 HIS A 175  ASP A 177  HIS A 190  HIS A 203                    
SITE     1 AC3  6 ASP A 165  GLY A 197  GLN A 199  ASP A 201                    
SITE     2 AC3  6 HOH A 445  HOH A 446                                          
SITE     1 AC4  6 ASP A 182  GLY A 183  ASP A 185  LEU A 187                    
SITE     2 AC4  6 ASP A 205  GLU A 208                                          
SITE     1 AC5  3 ASP A 131  ASP A 206  GLU A 208                               
SITE     1 AC6 34 LEU A 187  LEU A 188  ALA A 189  LEU A 222                    
SITE     2 AC6 34 VAL A 223  HIS A 226  GLN A 227  HIS A 230                    
SITE     3 AC6 34 HIS A 236  LEU A 243  TYR A 245  PRO A 246                    
SITE     4 AC6 34 MET A 247  TYR A 248   ZN A 301  GOL A 307                    
SITE     5 AC6 34 HOH A 417  HOH A 437  HOH A 520  LEU B 187                    
SITE     6 AC6 34 LEU B 188  ALA B 189  LEU B 222  HIS B 226                    
SITE     7 AC6 34 GLN B 227  HIS B 230  HIS B 236  LEU B 243                    
SITE     8 AC6 34 TYR B 245  PRO B 246  MET B 247  TYR B 248                    
SITE     9 AC6 34  ZN B 501  MLT B 506                                          
SITE     1 AC7  8 TYR A 179  LEU A 187  HIS A 190  0ZD A 306                    
SITE     2 AC7  8 HOH A 440  PRO B 240  TYR B 245  HOH B 615                    
SITE     1 AC8  6 PHE A 110  ASN A 262  PEG A 317  HOH A 457                    
SITE     2 AC8  6 HOH A 479  HOH A 518                                          
SITE     1 AC9  4 PEG A 314  HOH A 559  HOH A 584  HOH A 587                    
SITE     1 BC1  5 GLU A 111  LEU A 114  GLY A 233  ASP A 235                    
SITE     2 BC1  5 HOH A 577                                                     
SITE     1 BC2  3 ASP A 207  HOH A 471  HOH A 529                               
SITE     1 BC3  3 GLY A 217  TYR A 218  HOH A 566                               
SITE     1 BC4  1 GLN A 199                                                     
SITE     1 BC5  3 GOL A 309  HOH A 557  HOH A 559                               
SITE     1 BC6  3 PHE A 156  THR A 157  PGO B 510                               
SITE     1 BC7  3 HOH A 444  HOH A 511  HOH A 537                               
SITE     1 BC8  4 LYS A 184  GOL A 308  HOH A 518  HOH A 594                    
SITE     1 BC9  4 0ZD A 306  HIS B 226  HIS B 230  HIS B 236                    
SITE     1 CC1  4 HIS B 175  ASP B 177  HIS B 190  HIS B 203                    
SITE     1 CC2  6 ASP B 165  GLY B 197  GLN B 199  ASP B 201                    
SITE     2 CC2  6 HOH B 611  HOH B 612                                          
SITE     1 CC3  6 ASP B 182  GLY B 183  ASP B 185  LEU B 187                    
SITE     2 CC3  6 ASP B 205  GLU B 208                                          
SITE     1 CC4  4 ASP B 131  ASP B 206  GLU B 208  HOH B 681                    
SITE     1 CC5  8 0ZD A 306  GLU B 241  THR B 251  PRO B 254                    
SITE     2 CC5  8 PRO B 255  HIS B 257  PGO B 509  HOH B 617                    
SITE     1 CC6  2 PEG B 512  HOH B 701                                          
SITE     1 CC7  4 HOH B 701  HOH B 742  HOH B 743  HOH B 746                    
SITE     1 CC8  4 THR B 251  GLY B 253  PRO B 254  MLT B 506                    
SITE     1 CC9  3 PEG A 315  HOH B 714  HOH B 739                               
SITE     1 DC1  2 SER B 238  HOH B 729                                          
SITE     1 DC2  2 GOL B 507  HOH B 743                                          
SITE     1 DC3  5 ASP B 259  ASN B 262  GLY B 263  HIS B 266                    
SITE     2 DC3  5 HOH B 735                                                     
CRYST1   73.870   98.240   47.440  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013537  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010179  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021079        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system