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Database: PDB
Entry: 2OZR
LinkDB: 2OZR
Original site: 2OZR 
HEADER    HYDROLASE                               27-FEB-07   2OZR              
TITLE     MMP13 CATALYTIC DOMAIN COMPLEXED WITH 4-{[1-METHYL-2,4-DIOXO-6-(3-    
TITLE    2 PHENYLPROP-1-YN-1-YL)-1,4-DIHYDROQUINAZOLIN-3(2H)-YL]METHYL}BENZOIC  
TITLE    3 ACID                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COLLAGENASE 3;                                             
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 FRAGMENT: CATALYTIC DOMAIN;                                          
COMPND   5 SYNONYM: MATRIX METALLOPROTEINASE-13, MMP-13;                        
COMPND   6 EC: 3.4.24.-;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MMP13;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PLYSS;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEMEX1                                   
KEYWDS    CRYSTAL COMPLEX STRUCTURE, MATRIX METALLOPROTEINASE, MMP13 CATALYTIC  
KEYWDS   2 DOMAIN, MMP13 SPECIFIC INHIBITOR, HYDROLASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.R.JOHNSON,A.G.PAVLOVSKY,D.F.ORTWINE,F.PRIOR,C.-F.MAN,               
AUTHOR   2 D.A.BORNEMEIER,C.A.BANOTAI,W.T.MUELLER,P.MCCONNELL,C.H.YAN,V.BARAGI, 
AUTHOR   3 C.LESCH,W.H.ROARK,J.J.LIE,V.FASQUELLE,M.WILSON,D.ROBERTSON,K.DATTA,  
AUTHOR   4 R.GUZMAN,H.-K.HAN,R.D.DYER                                           
REVDAT   5   18-OCT-17 2OZR    1       REMARK                                   
REVDAT   4   13-JUL-11 2OZR    1       VERSN                                    
REVDAT   3   24-FEB-09 2OZR    1       VERSN                                    
REVDAT   2   09-OCT-07 2OZR    1       JRNL                                     
REVDAT   1   24-JUL-07 2OZR    0                                                
JRNL        AUTH   A.R.JOHNSON,A.G.PAVLOVSKY,D.F.ORTWINE,F.PRIOR,C.F.MAN,       
JRNL        AUTH 2 D.A.BORNEMEIER,C.A.BANOTAI,W.T.MUELLER,P.MCCONNELL,C.YAN,    
JRNL        AUTH 3 V.BARAGI,C.LESCH,W.H.ROARK,M.WILSON,K.DATTA,R.GUZMAN,        
JRNL        AUTH 4 H.K.HAN,R.D.DYER                                             
JRNL        TITL   DISCOVERY AND CHARACTERIZATION OF A NOVEL INHIBITOR OF       
JRNL        TITL 2 MATRIX METALLOPROTEASE-13 THAT REDUCES CARTILAGE DAMAGE IN   
JRNL        TITL 3 VIVO WITHOUT JOINT FIBROPLASIA SIDE EFFECTS.                 
JRNL        REF    J.BIOL.CHEM.                  V. 282 27781 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17623656                                                     
JRNL        DOI    10.1074/JBC.M703286200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 53427                          
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) : 0.253                           
REMARK   3   R VALUE            (WORKING SET) : 0.248                           
REMARK   3   FREE R VALUE                     : 0.340                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2869                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3659                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3170                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 192                          
REMARK   3   BIN FREE R VALUE                    : 0.3920                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10558                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 316                                     
REMARK   3   SOLVENT ATOMS            : 1024                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 26.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.74                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.841         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.380         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.264         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.324        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.898                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11233 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15278 ; 1.172 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1317 ; 6.291 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   523 ;35.381 ;23.939       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1609 ;16.114 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;17.244 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1495 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8972 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  5262 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  7487 ; 0.315 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   785 ; 0.173 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):   103 ; 0.125 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   268 ; 0.216 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    64 ; 0.217 ; 0.200       
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):  6734 ; 0.506 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10626 ; 0.885 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5657 ; 0.889 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4652 ; 1.367 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D E F G H                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     83       A     249      4                      
REMARK   3           1     B     83       B     249      4                      
REMARK   3           1     C     83       C     249      4                      
REMARK   3           1     D     84       D     249      4                      
REMARK   3           1     E     83       E     249      4                      
REMARK   3           1     F     83       F     249      4                      
REMARK   3           1     G     83       G     248      4                      
REMARK   3           1     H     83       H     248      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1279 ; 0.960 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1279 ; 0.940 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1279 ; 0.840 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   1279 ; 0.840 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):   1279 ; 1.050 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    F    (A):   1279 ; 1.040 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    G    (A):   1279 ; 0.960 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    H    (A):   1279 ; 0.910 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1279 ; 0.480 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1279 ; 0.550 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1279 ; 0.630 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   1279 ; 0.610 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    E (A**2):   1279 ; 0.730 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    F (A**2):   1279 ; 0.670 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    G (A**2):   1279 ; 0.470 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    H (A**2):   1279 ; 0.440 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 8                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    83        A   249                          
REMARK   3    RESIDUE RANGE :   B    83        B   249                          
REMARK   3    RESIDUE RANGE :   C    83        C   249                          
REMARK   3    RESIDUE RANGE :   D    84        D   249                          
REMARK   3    RESIDUE RANGE :   E    83        E   249                          
REMARK   3    RESIDUE RANGE :   F    83        F   249                          
REMARK   3    RESIDUE RANGE :   G    83        G   248                          
REMARK   3    RESIDUE RANGE :   H    83        H   248                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.4251   0.0314  28.1447              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0062 T22:   0.0182                                     
REMARK   3      T33:   0.0283 T12:   0.0047                                     
REMARK   3      T13:  -0.0259 T23:   0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0304 L22:   0.0216                                     
REMARK   3      L33:   0.2536 L12:  -0.0061                                     
REMARK   3      L13:  -0.0301 L23:  -0.0615                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0218 S12:  -0.0320 S13:   0.0061                       
REMARK   3      S21:   0.0588 S22:  -0.0134 S23:  -0.0349                       
REMARK   3      S31:   0.0299 S32:   0.1155 S33:   0.0352                       
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: USED NCS RESTRAINTS                       
REMARK   4                                                                      
REMARK   4 2OZR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000041787.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-NOV-01                          
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               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69624                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.7                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 62.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.34200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: PDB ENTRY 2OW9                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: DISSOLVED IN DMSO INHIBITOR WAS MIXED    
REMARK 280  WITH PROTEIN (PROTEIN CONCENTRATION: 1MG/ML) AT 5:1 RATIO, 0.1 M    
REMARK 280  ACETOHYDROHAMIC ACID ADDED. TERNARY COMPLEX WAS CONCENTRATED (TO    
REMARK 280  17 MG/ML PROTIEN CONCENTRATION). 1-2 UL HAGIND DROPS WERE MIXED     
REMARK 280  WITH SAME AMOUNT OF RESERVOIT SOLUTION (2.1 M AMMONIUM SULFATE      
REMARK 280  IN 0.1 M HEPES BUFFER) , PH 7.5, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       80.91800            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.98700            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       80.91800            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       35.98700            
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 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: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H                
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     MET A    80                                                      
REMARK 465     ALA A    81                                                      
REMARK 465     SER A    82                                                      
REMARK 465     MET B    80                                                      
REMARK 465     ALA B    81                                                      
REMARK 465     SER B    82                                                      
REMARK 465     MET C    80                                                      
REMARK 465     ALA C    81                                                      
REMARK 465     SER C    82                                                      
REMARK 465     MET D    80                                                      
REMARK 465     ALA D    81                                                      
REMARK 465     SER D    82                                                      
REMARK 465     TYR D    83                                                      
REMARK 465     MET E    80                                                      
REMARK 465     ALA E    81                                                      
REMARK 465     SER E    82                                                      
REMARK 465     LYS E   228                                                      
REMARK 465     SER E   229                                                      
REMARK 465     HIS E   230                                                      
REMARK 465     MET F    80                                                      
REMARK 465     ALA F    81                                                      
REMARK 465     SER F    82                                                      
REMARK 465     MET G    80                                                      
REMARK 465     ALA G    81                                                      
REMARK 465     SER G    82                                                      
REMARK 465     ASP G   249                                                      
REMARK 465     MET H    80                                                      
REMARK 465     ALA H    81                                                      
REMARK 465     SER H    82                                                      
REMARK 465     LYS H   228                                                      
REMARK 465     SER H   229                                                      
REMARK 465     HIS H   230                                                      
REMARK 465     ASP H   249                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  4132     O    HOH G  4052              1.97            
REMARK 500   O    HOH B  4024     O    HOH H  4155              2.05            
REMARK 500   O    THR A   128     O    HOH A  4106              2.10            
REMARK 500   O    HOH E  4028     O    HOH E  4109              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   ND2  ASN A    84     O    HIS H   211     4555     1.92            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  87      157.25    -45.20                                   
REMARK 500    LEU A  90       95.78    -62.19                                   
REMARK 500    LYS A 149     -125.01     38.97                                   
REMARK 500    PHE A 157     -176.83    -69.65                                   
REMARK 500    ASP A 158       28.04   -140.25                                   
REMARK 500    SER A 161     -170.49     59.63                                   
REMARK 500    ASN A 173     -118.50     57.81                                   
REMARK 500    SER A 188       40.98   -103.51                                   
REMARK 500    LYS A 228      101.45    -48.89                                   
REMARK 500    SER B  93       39.48    -90.21                                   
REMARK 500    LYS B 149     -126.39     49.18                                   
REMARK 500    SER B 161     -168.65     52.05                                   
REMARK 500    ALA B 165      148.64   -178.33                                   
REMARK 500    ASN B 173     -113.93     61.07                                   
REMARK 500    SER B 188       40.43   -102.93                                   
REMARK 500    SER B 189     -154.82   -159.32                                   
REMARK 500    THR B 226       40.77   -105.74                                   
REMARK 500    ASN C  84      110.83   -166.10                                   
REMARK 500    LEU C  90       94.80    -61.23                                   
REMARK 500    LYS C 149     -125.47     49.43                                   
REMARK 500    HIS C 151       16.69   -141.13                                   
REMARK 500    SER C 161      179.46     63.02                                   
REMARK 500    ASN C 173     -118.09     62.40                                   
REMARK 500    SER C 189     -154.47   -129.63                                   
REMARK 500    LYS D 149     -133.02     49.27                                   
REMARK 500    SER D 161     -173.86     60.39                                   
REMARK 500    ASN D 173     -107.37     50.92                                   
REMARK 500    SER D 189     -155.07   -120.91                                   
REMARK 500    SER D 229      138.70     83.16                                   
REMARK 500    LYS E 149     -136.61     51.02                                   
REMARK 500    SER E 161     -171.62     61.36                                   
REMARK 500    ASN E 173     -106.55     61.60                                   
REMARK 500    SER E 189     -156.88   -155.93                                   
REMARK 500    GLN E 239      -71.30    -64.51                                   
REMARK 500    LYS F  91      121.69   -174.37                                   
REMARK 500    LYS F 149     -133.81     47.40                                   
REMARK 500    TYR F 155       72.02   -110.49                                   
REMARK 500    SER F 161     -160.73     67.77                                   
REMARK 500    ASN F 173     -107.02     57.45                                   
REMARK 500    ARG G  88      129.98     77.35                                   
REMARK 500    THR G  89       43.05     79.44                                   
REMARK 500    LEU G  90       57.39    -60.74                                   
REMARK 500    LYS G 149     -140.39     45.71                                   
REMARK 500    SER G 161     -165.93     62.25                                   
REMARK 500    PRO G 169      155.54    -48.87                                   
REMARK 500    ASN G 173     -124.60     55.37                                   
REMARK 500    SER G 189     -154.15   -141.89                                   
REMARK 500    LYS G 228       92.43     74.29                                   
REMARK 500    HIS G 230       95.35     97.55                                   
REMARK 500    VAL H  85     -151.73    -97.96                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      59 RAMACHANDRAN OUTLIERS.                        
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 A4001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 201   NE2                                                    
REMARK 620 2 HIS A 205   NE2 100.7                                              
REMARK 620 3 HIS A 211   NE2 110.7  99.3                                        
REMARK 620 4 HOH A4024   O   102.2 109.5 130.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A4002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 153   OD2                                                    
REMARK 620 2 HIS A 166   NE2 118.5                                              
REMARK 620 3 HIS A 151   NE2 116.5  98.9                                        
REMARK 620 4 HIS A 179   ND1  93.3 124.9 105.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A4003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A 163   O                                                      
REMARK 620 2 GLU A 184   OE2  95.2                                              
REMARK 620 3 ASP A 181   OD2  83.0  88.8                                        
REMARK 620 4 ASP A 158   OD1  82.7 176.6  93.7                                  
REMARK 620 5 GLY A 159   O   169.3  92.1  89.4  90.3                            
REMARK 620 6 SER A 161   O   101.3  88.5 175.1  89.3  86.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A4004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A4016   O                                                      
REMARK 620 2 ASP A 141   O    91.7                                              
REMARK 620 3 HOH A4115   O    85.0  90.8                                        
REMARK 620 4 GLY A 175   O    77.9  90.3 162.8                                  
REMARK 620 5 ASP A 177   OD1 173.5  83.3  99.2  97.9                            
REMARK 620 6 ASN A 173   O    83.0 165.6  75.4 101.6 102.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A4005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 107   OD2                                                    
REMARK 620 2 ASP A 182   OD1 101.4                                              
REMARK 620 3 HOH A4088   O    87.8 120.0                                        
REMARK 620 4 GLU A 184   O    93.1 119.3 119.2                                  
REMARK 620 5 ASP A 182   O   177.3  77.4  90.7  89.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B4006  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 201   NE2                                                    
REMARK 620 2 HIS B 205   NE2  94.7                                              
REMARK 620 3 HIS B 211   NE2 103.9 103.6                                        
REMARK 620 4 HOH B4058   O    85.7 165.8  90.0                                  
REMARK 620 5 HOH B4022   O   128.8 103.4 117.1  66.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B4007  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 153   OD2                                                    
REMARK 620 2 HIS B 166   NE2 117.2                                              
REMARK 620 3 HIS B 151   NE2 118.6 101.1                                        
REMARK 620 4 HIS B 179   ND1  98.3 111.3 110.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B4008  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU B 163   O                                                      
REMARK 620 2 GLU B 184   OE2  83.4                                              
REMARK 620 3 ASP B 181   OD2  95.0  77.8                                        
REMARK 620 4 ASP B 158   OD1 100.2 173.9 106.6                                  
REMARK 620 5 GLY B 159   O   169.7  86.8  79.8  89.8                            
REMARK 620 6 SER B 161   O    97.5  88.6 160.3  86.1  85.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B4009  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B4017   O                                                      
REMARK 620 2 ASP B 141   O    83.4                                              
REMARK 620 3 HOH B4097   O    90.8  85.6                                        
REMARK 620 4 GLY B 175   O    76.3  89.8 166.7                                  
REMARK 620 5 ASP B 177   OD1 167.4  86.4  95.7  96.4                            
REMARK 620 6 ASN B 173   O    88.5 162.1  78.6 103.8 103.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B4010  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 107   OD2                                                    
REMARK 620 2 ASP B 182   OD1 104.1                                              
REMARK 620 3 HOH B4018   O    98.5 122.6                                        
REMARK 620 4 GLU B 184   O    86.8 117.7 115.6                                  
REMARK 620 5 ASP B 182   O   171.7  73.6  89.3  87.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C4011  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 201   NE2                                                    
REMARK 620 2 HAE C3001   O   124.4                                              
REMARK 620 3 HIS C 205   NE2 100.9 107.3                                        
REMARK 620 4 HIS C 211   NE2 111.4 113.6  93.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C4012  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 151   NE2                                                    
REMARK 620 2 ASP C 153   OD2 110.3                                              
REMARK 620 3 HIS C 166   NE2 121.0 107.6                                        
REMARK 620 4 HIS C 179   ND1 104.8  95.8 114.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C4013  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 184   OE2                                                    
REMARK 620 2 GLY C 159   O    91.3                                              
REMARK 620 3 LEU C 163   O    86.4 171.1                                        
REMARK 620 4 ASP C 158   OD1 173.9  92.9  88.8                                  
REMARK 620 5 ASP C 181   OD2  86.5  85.1  86.2  89.5                            
REMARK 620 6 SER C 161   O    94.1  89.4  99.3  90.4 174.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C4014  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C4147   O                                                      
REMARK 620 2 ASP C 177   OD1  98.2                                              
REMARK 620 3 ASP C 141   O    97.2  91.7                                        
REMARK 620 4 ASN C 173   O    71.9 100.7 164.4                                  
REMARK 620 5 HOH C4020   O    85.4 172.0  80.8  87.1                            
REMARK 620 6 GLY C 175   O   162.6  97.1  90.7  97.0  80.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C4015  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 107   OD1                                                    
REMARK 620 2 ASP C 107   OD2  45.0                                              
REMARK 620 3 HOH C4150   O    70.8 104.9                                        
REMARK 620 4 ASP C 182   OD1 104.4  93.2 144.3                                  
REMARK 620 5 ASP C 182   O   147.7 160.5  94.6  70.4                            
REMARK 620 6 GLU C 184   O   117.3  83.6  99.6 113.1  92.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D4016  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 201   NE2                                                    
REMARK 620 2 HAE D3002   O2  106.2                                              
REMARK 620 3 HIS D 205   NE2  97.6 112.4                                        
REMARK 620 4 HIS D 211   NE2 107.0 134.0  93.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D4017  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 151   NE2                                                    
REMARK 620 2 ASP D 153   OD2 111.2                                              
REMARK 620 3 HIS D 166   NE2 120.6 107.3                                        
REMARK 620 4 HIS D 179   ND1 106.1  95.5 113.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D4018  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY D 159   O                                                      
REMARK 620 2 GLU D 184   OE2  90.1                                              
REMARK 620 3 SER D 161   O    81.1  87.8                                        
REMARK 620 4 ASP D 181   OD2  87.1  93.4 168.1                                  
REMARK 620 5 LEU D 163   O   178.5  88.9  97.7  94.1                            
REMARK 620 6 ASP D 158   OD1  84.3 172.3  86.1  91.6  96.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D4019  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 177   OD1                                                    
REMARK 620 2 HOH D4126   O    91.8                                              
REMARK 620 3 GLY D 175   O    97.5 170.6                                        
REMARK 620 4 ASP D 141   O    88.8  89.7  91.5                                  
REMARK 620 5 ASN D 173   O    92.3  76.7 101.8 166.4                            
REMARK 620 6 HOH D4133   O   172.9  94.0  76.7  87.1  93.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D4020  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D4150   O                                                      
REMARK 620 2 ASP D 107   OD2  97.2                                              
REMARK 620 3 ASP D 182   OD1 150.5 104.9                                        
REMARK 620 4 GLU D 184   O    76.4  86.7 123.6                                  
REMARK 620 5 ASP D 182   O    83.6 178.9  74.1  94.2                            
REMARK 620 6 HOH D4139   O    50.4  96.9 106.8 126.7  83.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E4021  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HAE E3003   O2                                                     
REMARK 620 2 HIS E 211   NE2  78.9                                              
REMARK 620 3 HIS E 205   NE2 174.6 102.6                                        
REMARK 620 4 HAE E3003   O    70.3  87.9 104.5                                  
REMARK 620 5 HIS E 201   NE2  66.0 117.3 117.1 122.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E4022  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E 151   NE2                                                    
REMARK 620 2 ASP E 153   OD2 106.1                                              
REMARK 620 3 HIS E 179   ND1 115.4  86.7                                        
REMARK 620 4 HIS E 166   NE2 113.0 113.8 118.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E4023  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 158   OD1                                                    
REMARK 620 2 GLU E 184   OE2 167.0                                              
REMARK 620 3 ASP E 181   OD2 100.3  92.2                                        
REMARK 620 4 GLY E 159   O    84.1  99.7  89.3                                  
REMARK 620 5 SER E 161   O    81.7  86.6 169.5  80.7                            
REMARK 620 6 LEU E 163   O    95.0  81.3  91.0 179.0  99.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E4024  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN E 173   O                                                      
REMARK 620 2 GLY E 175   O   105.9                                              
REMARK 620 3 ASP E 177   OD1  96.1  95.8                                        
REMARK 620 4 ASP E 141   O   171.1  79.7  90.1                                  
REMARK 620 5 HOH E4032   O    87.5  66.3 162.0  88.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E4025  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 107   OD1                                                    
REMARK 620 2 ASP E 182   OD1 116.1                                              
REMARK 620 3 ASP E 182   O   146.8  79.3                                        
REMARK 620 4 HOH E4095   O    58.9 149.9  92.5                                  
REMARK 620 5 ASP E 107   OD2  41.7 105.2 167.4  89.0                            
REMARK 620 6 GLU E 184   O    98.5 122.3  96.4  87.2  71.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F4026  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HAE F3004   O                                                      
REMARK 620 2 HIS F 201   NE2  74.6                                              
REMARK 620 3 HIS F 205   NE2 159.9 119.4                                        
REMARK 620 4 HAE F3004   N    19.6  93.0 141.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F4027  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F 179   ND1                                                    
REMARK 620 2 HIS F 151   NE2 113.4                                              
REMARK 620 3 ASP F 153   OD2  92.8 101.1                                        
REMARK 620 4 HIS F 166   NE2 122.6 111.5 111.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F4028  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU F 163   O                                                      
REMARK 620 2 ASP F 181   OD2  95.0                                              
REMARK 620 3 GLU F 184   OE2  80.4 108.7                                        
REMARK 620 4 ASP F 158   OD1  88.0  89.4 159.2                                  
REMARK 620 5 GLY F 159   O   170.5  94.4  95.7  93.1                            
REMARK 620 6 SER F 161   O    82.9 176.3  73.9  87.6  87.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F4029  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN F 173   O                                                      
REMARK 620 2 GLY F 175   O    98.9                                              
REMARK 620 3 ASP F 177   OD1  96.5  95.3                                        
REMARK 620 4 ASP F 141   O   172.8  76.0  89.1                                  
REMARK 620 5 HOH F4038   O    89.6  72.5 167.1  84.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F4030  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 182   O                                                      
REMARK 620 2 HOH F4125   O    69.5                                              
REMARK 620 3 GLU F 184   O    90.1 106.7                                        
REMARK 620 4 ASP F 107   OD2 166.7 122.7  91.2                                  
REMARK 620 5 ASP F 182   OD1  69.4 122.4 111.9  97.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G4031  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH G4090   O                                                      
REMARK 620 2 HIS G 205   NE2 107.9                                              
REMARK 620 3 HIS G 211   NE2 138.1  98.6                                        
REMARK 620 4 HIS G 201   NE2  95.6  98.8 112.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G4032  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G 179   ND1                                                    
REMARK 620 2 HIS G 166   NE2 123.5                                              
REMARK 620 3 ASP G 153   OD1  96.0 100.4                                        
REMARK 620 4 HIS G 151   NE2 108.1 116.7 108.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G4033  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER G 161   O                                                      
REMARK 620 2 ASP G 181   OD2 168.4                                              
REMARK 620 3 GLU G 184   OE2  77.0  92.3                                        
REMARK 620 4 ASP G 158   OD1  92.5  98.4 169.0                                  
REMARK 620 5 GLY G 159   O    87.2  87.9  87.2  96.1                            
REMARK 620 6 LEU G 163   O    90.7  91.6  79.6  97.1 166.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G4034  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN G 173   O                                                      
REMARK 620 2 ASP G 177   OD1  88.7                                              
REMARK 620 3 HOH G4131   O    89.1  95.5                                        
REMARK 620 4 ASP G 141   O   171.0  85.5  98.3                                  
REMARK 620 5 GLY G 175   O    79.4  90.7 166.8  93.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G4035  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G 182   OD1                                                    
REMARK 620 2 ASP G 107   OD1 105.9                                              
REMARK 620 3 ASP G 182   O    69.1 152.4                                        
REMARK 620 4 GLU G 184   O   108.0 119.3  87.3                                  
REMARK 620 5 ASP G 107   OD2  96.7  45.5 158.4  81.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H4036  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH H4124   O                                                      
REMARK 620 2 HIS H 205   NE2 115.0                                              
REMARK 620 3 HIS H 211   NE2 123.5 112.2                                        
REMARK 620 4 HIS H 201   NE2 100.9  97.0 102.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H4037  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H 179   ND1                                                    
REMARK 620 2 ASP H 153   OD2  89.6                                              
REMARK 620 3 HIS H 151   NE2 106.5 117.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H4038  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU H 184   OE2                                                    
REMARK 620 2 ASP H 158   OD1 172.6                                              
REMARK 620 3 LEU H 163   O    84.7  91.5                                        
REMARK 620 4 ASP H 181   OD2  89.7  96.4  87.0                                  
REMARK 620 5 SER H 161   O    87.6  86.4  94.3 176.9                            
REMARK 620 6 GLY H 159   O    96.3  88.0 175.4  88.5  90.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H4039  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH H4110   O                                                      
REMARK 620 2 GLY H 175   O    90.3                                              
REMARK 620 3 ASP H 141   O    87.8  90.3                                        
REMARK 620 4 ASP H 177   OD1 178.4  88.4  93.1                                  
REMARK 620 5 ASN H 173   O    91.3  84.9 175.1  87.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H4040  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH H4133   O                                                      
REMARK 620 2 ASP H 107   OD2  88.7                                              
REMARK 620 3 ASP H 182   OD1 158.8  97.8                                        
REMARK 620 4 HOH H4125   O    56.8  98.2 102.2                                  
REMARK 620 5 GLU H 184   O    79.0  77.6 122.0 135.8                            
REMARK 620 6 ASP H 182   O    98.2 173.0  75.4  84.9 104.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2OW9   RELATED DB: PDB                                   
DBREF  2OZR A   83   249  UNP    P45452   MMP13_HUMAN    104    270             
DBREF  2OZR B   83   249  UNP    P45452   MMP13_HUMAN    104    270             
DBREF  2OZR C   83   249  UNP    P45452   MMP13_HUMAN    104    270             
DBREF  2OZR D   83   249  UNP    P45452   MMP13_HUMAN    104    270             
DBREF  2OZR E   83   249  UNP    P45452   MMP13_HUMAN    104    270             
DBREF  2OZR F   83   249  UNP    P45452   MMP13_HUMAN    104    270             
DBREF  2OZR G   83   249  UNP    P45452   MMP13_HUMAN    104    270             
DBREF  2OZR H   83   249  UNP    P45452   MMP13_HUMAN    104    270             
SEQADV 2OZR MET A   80  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR ALA A   81  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR SER A   82  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR MET B   80  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR ALA B   81  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR SER B   82  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR MET C   80  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR ALA C   81  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR SER C   82  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR MET D   80  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR ALA D   81  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR SER D   82  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR MET E   80  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR ALA E   81  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR SER E   82  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR MET F   80  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR ALA F   81  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR SER F   82  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR MET G   80  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR ALA G   81  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR SER G   82  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR MET H   80  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR ALA H   81  UNP  P45452              EXPRESSION TAG                 
SEQADV 2OZR SER H   82  UNP  P45452              EXPRESSION TAG                 
SEQRES   1 A  170  MET ALA SER TYR ASN VAL PHE PRO ARG THR LEU LYS TRP          
SEQRES   2 A  170  SER LYS MET ASN LEU THR TYR ARG ILE VAL ASN TYR THR          
SEQRES   3 A  170  PRO ASP MET THR HIS SER GLU VAL GLU LYS ALA PHE LYS          
SEQRES   4 A  170  LYS ALA PHE LYS VAL TRP SER ASP VAL THR PRO LEU ASN          
SEQRES   5 A  170  PHE THR ARG LEU HIS ASP GLY ILE ALA ASP ILE MET ILE          
SEQRES   6 A  170  SER PHE GLY ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE          
SEQRES   7 A  170  ASP GLY PRO SER GLY LEU LEU ALA HIS ALA PHE PRO PRO          
SEQRES   8 A  170  GLY PRO ASN TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP          
SEQRES   9 A  170  GLU THR TRP THR SER SER SER LYS GLY TYR ASN LEU PHE          
SEQRES  10 A  170  LEU VAL ALA ALA HIS GLU PHE GLY HIS SER LEU GLY LEU          
SEQRES  11 A  170  ASP HIS SER LYS ASP PRO GLY ALA LEU MET PHE PRO ILE          
SEQRES  12 A  170  TYR THR TYR THR GLY LYS SER HIS PHE MET LEU PRO ASP          
SEQRES  13 A  170  ASP ASP VAL GLN GLY ILE GLN SER LEU TYR GLY PRO GLY          
SEQRES  14 A  170  ASP                                                          
SEQRES   1 B  170  MET ALA SER TYR ASN VAL PHE PRO ARG THR LEU LYS TRP          
SEQRES   2 B  170  SER LYS MET ASN LEU THR TYR ARG ILE VAL ASN TYR THR          
SEQRES   3 B  170  PRO ASP MET THR HIS SER GLU VAL GLU LYS ALA PHE LYS          
SEQRES   4 B  170  LYS ALA PHE LYS VAL TRP SER ASP VAL THR PRO LEU ASN          
SEQRES   5 B  170  PHE THR ARG LEU HIS ASP GLY ILE ALA ASP ILE MET ILE          
SEQRES   6 B  170  SER PHE GLY ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE          
SEQRES   7 B  170  ASP GLY PRO SER GLY LEU LEU ALA HIS ALA PHE PRO PRO          
SEQRES   8 B  170  GLY PRO ASN TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP          
SEQRES   9 B  170  GLU THR TRP THR SER SER SER LYS GLY TYR ASN LEU PHE          
SEQRES  10 B  170  LEU VAL ALA ALA HIS GLU PHE GLY HIS SER LEU GLY LEU          
SEQRES  11 B  170  ASP HIS SER LYS ASP PRO GLY ALA LEU MET PHE PRO ILE          
SEQRES  12 B  170  TYR THR TYR THR GLY LYS SER HIS PHE MET LEU PRO ASP          
SEQRES  13 B  170  ASP ASP VAL GLN GLY ILE GLN SER LEU TYR GLY PRO GLY          
SEQRES  14 B  170  ASP                                                          
SEQRES   1 C  170  MET ALA SER TYR ASN VAL PHE PRO ARG THR LEU LYS TRP          
SEQRES   2 C  170  SER LYS MET ASN LEU THR TYR ARG ILE VAL ASN TYR THR          
SEQRES   3 C  170  PRO ASP MET THR HIS SER GLU VAL GLU LYS ALA PHE LYS          
SEQRES   4 C  170  LYS ALA PHE LYS VAL TRP SER ASP VAL THR PRO LEU ASN          
SEQRES   5 C  170  PHE THR ARG LEU HIS ASP GLY ILE ALA ASP ILE MET ILE          
SEQRES   6 C  170  SER PHE GLY ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE          
SEQRES   7 C  170  ASP GLY PRO SER GLY LEU LEU ALA HIS ALA PHE PRO PRO          
SEQRES   8 C  170  GLY PRO ASN TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP          
SEQRES   9 C  170  GLU THR TRP THR SER SER SER LYS GLY TYR ASN LEU PHE          
SEQRES  10 C  170  LEU VAL ALA ALA HIS GLU PHE GLY HIS SER LEU GLY LEU          
SEQRES  11 C  170  ASP HIS SER LYS ASP PRO GLY ALA LEU MET PHE PRO ILE          
SEQRES  12 C  170  TYR THR TYR THR GLY LYS SER HIS PHE MET LEU PRO ASP          
SEQRES  13 C  170  ASP ASP VAL GLN GLY ILE GLN SER LEU TYR GLY PRO GLY          
SEQRES  14 C  170  ASP                                                          
SEQRES   1 D  170  MET ALA SER TYR ASN VAL PHE PRO ARG THR LEU LYS TRP          
SEQRES   2 D  170  SER LYS MET ASN LEU THR TYR ARG ILE VAL ASN TYR THR          
SEQRES   3 D  170  PRO ASP MET THR HIS SER GLU VAL GLU LYS ALA PHE LYS          
SEQRES   4 D  170  LYS ALA PHE LYS VAL TRP SER ASP VAL THR PRO LEU ASN          
SEQRES   5 D  170  PHE THR ARG LEU HIS ASP GLY ILE ALA ASP ILE MET ILE          
SEQRES   6 D  170  SER PHE GLY ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE          
SEQRES   7 D  170  ASP GLY PRO SER GLY LEU LEU ALA HIS ALA PHE PRO PRO          
SEQRES   8 D  170  GLY PRO ASN TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP          
SEQRES   9 D  170  GLU THR TRP THR SER SER SER LYS GLY TYR ASN LEU PHE          
SEQRES  10 D  170  LEU VAL ALA ALA HIS GLU PHE GLY HIS SER LEU GLY LEU          
SEQRES  11 D  170  ASP HIS SER LYS ASP PRO GLY ALA LEU MET PHE PRO ILE          
SEQRES  12 D  170  TYR THR TYR THR GLY LYS SER HIS PHE MET LEU PRO ASP          
SEQRES  13 D  170  ASP ASP VAL GLN GLY ILE GLN SER LEU TYR GLY PRO GLY          
SEQRES  14 D  170  ASP                                                          
SEQRES   1 E  170  MET ALA SER TYR ASN VAL PHE PRO ARG THR LEU LYS TRP          
SEQRES   2 E  170  SER LYS MET ASN LEU THR TYR ARG ILE VAL ASN TYR THR          
SEQRES   3 E  170  PRO ASP MET THR HIS SER GLU VAL GLU LYS ALA PHE LYS          
SEQRES   4 E  170  LYS ALA PHE LYS VAL TRP SER ASP VAL THR PRO LEU ASN          
SEQRES   5 E  170  PHE THR ARG LEU HIS ASP GLY ILE ALA ASP ILE MET ILE          
SEQRES   6 E  170  SER PHE GLY ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE          
SEQRES   7 E  170  ASP GLY PRO SER GLY LEU LEU ALA HIS ALA PHE PRO PRO          
SEQRES   8 E  170  GLY PRO ASN TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP          
SEQRES   9 E  170  GLU THR TRP THR SER SER SER LYS GLY TYR ASN LEU PHE          
SEQRES  10 E  170  LEU VAL ALA ALA HIS GLU PHE GLY HIS SER LEU GLY LEU          
SEQRES  11 E  170  ASP HIS SER LYS ASP PRO GLY ALA LEU MET PHE PRO ILE          
SEQRES  12 E  170  TYR THR TYR THR GLY LYS SER HIS PHE MET LEU PRO ASP          
SEQRES  13 E  170  ASP ASP VAL GLN GLY ILE GLN SER LEU TYR GLY PRO GLY          
SEQRES  14 E  170  ASP                                                          
SEQRES   1 F  170  MET ALA SER TYR ASN VAL PHE PRO ARG THR LEU LYS TRP          
SEQRES   2 F  170  SER LYS MET ASN LEU THR TYR ARG ILE VAL ASN TYR THR          
SEQRES   3 F  170  PRO ASP MET THR HIS SER GLU VAL GLU LYS ALA PHE LYS          
SEQRES   4 F  170  LYS ALA PHE LYS VAL TRP SER ASP VAL THR PRO LEU ASN          
SEQRES   5 F  170  PHE THR ARG LEU HIS ASP GLY ILE ALA ASP ILE MET ILE          
SEQRES   6 F  170  SER PHE GLY ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE          
SEQRES   7 F  170  ASP GLY PRO SER GLY LEU LEU ALA HIS ALA PHE PRO PRO          
SEQRES   8 F  170  GLY PRO ASN TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP          
SEQRES   9 F  170  GLU THR TRP THR SER SER SER LYS GLY TYR ASN LEU PHE          
SEQRES  10 F  170  LEU VAL ALA ALA HIS GLU PHE GLY HIS SER LEU GLY LEU          
SEQRES  11 F  170  ASP HIS SER LYS ASP PRO GLY ALA LEU MET PHE PRO ILE          
SEQRES  12 F  170  TYR THR TYR THR GLY LYS SER HIS PHE MET LEU PRO ASP          
SEQRES  13 F  170  ASP ASP VAL GLN GLY ILE GLN SER LEU TYR GLY PRO GLY          
SEQRES  14 F  170  ASP                                                          
SEQRES   1 G  170  MET ALA SER TYR ASN VAL PHE PRO ARG THR LEU LYS TRP          
SEQRES   2 G  170  SER LYS MET ASN LEU THR TYR ARG ILE VAL ASN TYR THR          
SEQRES   3 G  170  PRO ASP MET THR HIS SER GLU VAL GLU LYS ALA PHE LYS          
SEQRES   4 G  170  LYS ALA PHE LYS VAL TRP SER ASP VAL THR PRO LEU ASN          
SEQRES   5 G  170  PHE THR ARG LEU HIS ASP GLY ILE ALA ASP ILE MET ILE          
SEQRES   6 G  170  SER PHE GLY ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE          
SEQRES   7 G  170  ASP GLY PRO SER GLY LEU LEU ALA HIS ALA PHE PRO PRO          
SEQRES   8 G  170  GLY PRO ASN TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP          
SEQRES   9 G  170  GLU THR TRP THR SER SER SER LYS GLY TYR ASN LEU PHE          
SEQRES  10 G  170  LEU VAL ALA ALA HIS GLU PHE GLY HIS SER LEU GLY LEU          
SEQRES  11 G  170  ASP HIS SER LYS ASP PRO GLY ALA LEU MET PHE PRO ILE          
SEQRES  12 G  170  TYR THR TYR THR GLY LYS SER HIS PHE MET LEU PRO ASP          
SEQRES  13 G  170  ASP ASP VAL GLN GLY ILE GLN SER LEU TYR GLY PRO GLY          
SEQRES  14 G  170  ASP                                                          
SEQRES   1 H  170  MET ALA SER TYR ASN VAL PHE PRO ARG THR LEU LYS TRP          
SEQRES   2 H  170  SER LYS MET ASN LEU THR TYR ARG ILE VAL ASN TYR THR          
SEQRES   3 H  170  PRO ASP MET THR HIS SER GLU VAL GLU LYS ALA PHE LYS          
SEQRES   4 H  170  LYS ALA PHE LYS VAL TRP SER ASP VAL THR PRO LEU ASN          
SEQRES   5 H  170  PHE THR ARG LEU HIS ASP GLY ILE ALA ASP ILE MET ILE          
SEQRES   6 H  170  SER PHE GLY ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE          
SEQRES   7 H  170  ASP GLY PRO SER GLY LEU LEU ALA HIS ALA PHE PRO PRO          
SEQRES   8 H  170  GLY PRO ASN TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP          
SEQRES   9 H  170  GLU THR TRP THR SER SER SER LYS GLY TYR ASN LEU PHE          
SEQRES  10 H  170  LEU VAL ALA ALA HIS GLU PHE GLY HIS SER LEU GLY LEU          
SEQRES  11 H  170  ASP HIS SER LYS ASP PRO GLY ALA LEU MET PHE PRO ILE          
SEQRES  12 H  170  TYR THR TYR THR GLY LYS SER HIS PHE MET LEU PRO ASP          
SEQRES  13 H  170  ASP ASP VAL GLN GLY ILE GLN SER LEU TYR GLY PRO GLY          
SEQRES  14 H  170  ASP                                                          
HET     ZN  A4001       1                                                       
HET     ZN  A4002       1                                                       
HET     CA  A4003       1                                                       
HET     CA  A4004       1                                                       
HET     CA  A4005       1                                                       
HET    GG1  A2001      32                                                       
HET     ZN  B4006       1                                                       
HET     ZN  B4007       1                                                       
HET     CA  B4008       1                                                       
HET     CA  B4009       1                                                       
HET     CA  B4010       1                                                       
HET    GG1  B2002      32                                                       
HET     ZN  C4011       1                                                       
HET     ZN  C4012       1                                                       
HET     CA  C4013       1                                                       
HET     CA  C4014       1                                                       
HET     CA  C4015       1                                                       
HET    GG1  C2003      32                                                       
HET    HAE  C3001       5                                                       
HET     ZN  D4016       1                                                       
HET     ZN  D4017       1                                                       
HET     CA  D4018       1                                                       
HET     CA  D4019       1                                                       
HET     CA  D4020       1                                                       
HET    GG1  D2004      32                                                       
HET    HAE  D3002       5                                                       
HET     ZN  E4021       1                                                       
HET     ZN  E4022       1                                                       
HET     CA  E4023       1                                                       
HET     CA  E4024       1                                                       
HET     CA  E4025       1                                                       
HET    GG1  E2005      32                                                       
HET    HAE  E3003       5                                                       
HET     ZN  F4026       1                                                       
HET     ZN  F4027       1                                                       
HET     CA  F4028       1                                                       
HET     CA  F4029       1                                                       
HET     CA  F4030       1                                                       
HET    GG1  F2006      32                                                       
HET    HAE  F3004       5                                                       
HET     ZN  G4031       1                                                       
HET     ZN  G4032       1                                                       
HET     CA  G4033       1                                                       
HET     CA  G4034       1                                                       
HET     CA  G4035       1                                                       
HET    GG1  G2007      32                                                       
HET     ZN  H4036       1                                                       
HET     ZN  H4037       1                                                       
HET     CA  H4038       1                                                       
HET     CA  H4039       1                                                       
HET     CA  H4040       1                                                       
HET    GG1  H2008      32                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     GG1 4-{[1-METHYL-2,4-DIOXO-6-(3-PHENYLPROP-1-YN-1-YL)-1,4-           
HETNAM   2 GG1  DIHYDROQUINAZOLIN-3(2H)-YL]METHYL}BENZOIC ACID                  
HETNAM     HAE ACETOHYDROXAMIC ACID                                             
FORMUL   9   ZN    16(ZN 2+)                                                    
FORMUL  11   CA    24(CA 2+)                                                    
FORMUL  14  GG1    8(C26 H20 N2 O4)                                             
FORMUL  27  HAE    4(C2 H5 N O2)                                                
FORMUL  61  HOH   *1024(H2 O)                                                   
HELIX    1   1 THR A  109  ASP A  126  1                                  18    
HELIX    2   2 LEU A  195  LEU A  207  1                                  13    
HELIX    3   3 PRO A  234  GLY A  246  1                                  13    
HELIX    4   4 THR B  109  ASP B  126  1                                  18    
HELIX    5   5 LEU B  195  LEU B  207  1                                  13    
HELIX    6   6 PRO B  234  GLY B  246  1                                  13    
HELIX    7   7 THR C  109  ASP C  126  1                                  18    
HELIX    8   8 LEU C  195  LEU C  207  1                                  13    
HELIX    9   9 PRO C  234  GLY C  246  1                                  13    
HELIX   10  10 THR D  109  ASP D  126  1                                  18    
HELIX   11  11 LEU D  195  LEU D  207  1                                  13    
HELIX   12  12 PRO D  234  GLY D  246  1                                  13    
HELIX   13  13 THR E  109  VAL E  127  1                                  19    
HELIX   14  14 LEU E  195  GLY E  208  1                                  14    
HELIX   15  15 PRO E  234  GLY E  246  1                                  13    
HELIX   16  16 THR F  109  ASP F  126  1                                  18    
HELIX   17  17 LEU F  195  GLY F  208  1                                  14    
HELIX   18  18 PRO F  234  GLY F  246  1                                  13    
HELIX   19  19 THR G  109  ASP G  126  1                                  18    
HELIX   20  20 LEU G  195  LEU G  207  1                                  13    
HELIX   21  21 PRO G  234  GLY G  246  1                                  13    
HELIX   22  22 THR H  109  ASP H  126  1                                  18    
HELIX   23  23 LEU H  195  LEU H  207  1                                  13    
HELIX   24  24 PRO H  234  GLY H  246  1                                  13    
SHEET    1   A 5 ASN A 131  LEU A 135  0                                        
SHEET    2   A 5 ASN A  96  ILE A 101  1  N  TYR A  99   O  LEU A 135           
SHEET    3   A 5 ILE A 142  GLY A 147  1  O  ILE A 144   N  ARG A 100           
SHEET    4   A 5 ALA A 178  ASP A 181  1  O  PHE A 180   N  GLY A 147           
SHEET    5   A 5 ALA A 165  ALA A 167 -1  N  HIS A 166   O  HIS A 179           
SHEET    1   B 2 TRP A 186  THR A 187  0                                        
SHEET    2   B 2 TYR A 193  ASN A 194  1  O  TYR A 193   N  THR A 187           
SHEET    1   C 5 ASN B 131  ARG B 134  0                                        
SHEET    2   C 5 ASN B  96  ILE B 101  1  N  LEU B  97   O  ASN B 131           
SHEET    3   C 5 ILE B 142  GLY B 147  1  O  ILE B 144   N  ARG B 100           
SHEET    4   C 5 ALA B 178  ASP B 181  1  O  PHE B 180   N  GLY B 147           
SHEET    5   C 5 ALA B 165  ALA B 167 -1  N  HIS B 166   O  HIS B 179           
SHEET    1   D 2 TRP B 186  THR B 187  0                                        
SHEET    2   D 2 TYR B 193  ASN B 194  1  O  TYR B 193   N  THR B 187           
SHEET    1   E 5 ASN C 131  LEU C 135  0                                        
SHEET    2   E 5 ASN C  96  ILE C 101  1  N  LEU C  97   O  ASN C 131           
SHEET    3   E 5 ILE C 142  GLY C 147  1  O  ILE C 144   N  ARG C 100           
SHEET    4   E 5 ALA C 178  ASP C 181  1  O  PHE C 180   N  GLY C 147           
SHEET    5   E 5 ALA C 165  ALA C 167 -1  N  HIS C 166   O  HIS C 179           
SHEET    1   F 2 TRP C 186  THR C 187  0                                        
SHEET    2   F 2 TYR C 193  ASN C 194  1  O  TYR C 193   N  THR C 187           
SHEET    1   G 5 ASN D 131  ARG D 134  0                                        
SHEET    2   G 5 ASN D  96  ILE D 101  1  N  LEU D  97   O  ASN D 131           
SHEET    3   G 5 ILE D 142  GLY D 147  1  O  ILE D 144   N  ARG D 100           
SHEET    4   G 5 ALA D 178  ASP D 181  1  O  PHE D 180   N  GLY D 147           
SHEET    5   G 5 ALA D 165  ALA D 167 -1  N  HIS D 166   O  HIS D 179           
SHEET    1   H 2 TRP D 186  THR D 187  0                                        
SHEET    2   H 2 TYR D 193  ASN D 194  1  O  TYR D 193   N  THR D 187           
SHEET    1   I 5 ASN E 131  ARG E 134  0                                        
SHEET    2   I 5 ASN E  96  ILE E 101  1  N  LEU E  97   O  THR E 133           
SHEET    3   I 5 ILE E 142  GLY E 147  1  O  ILE E 144   N  ARG E 100           
SHEET    4   I 5 ALA E 178  ASP E 181  1  O  PHE E 180   N  SER E 145           
SHEET    5   I 5 ALA E 165  ALA E 167 -1  N  HIS E 166   O  HIS E 179           
SHEET    1   J 2 TRP E 186  THR E 187  0                                        
SHEET    2   J 2 TYR E 193  ASN E 194  1  O  TYR E 193   N  THR E 187           
SHEET    1   K 5 ASN F 131  LEU F 135  0                                        
SHEET    2   K 5 ASN F  96  ILE F 101  1  N  TYR F  99   O  LEU F 135           
SHEET    3   K 5 ILE F 142  GLY F 147  1  O  ILE F 144   N  ARG F 100           
SHEET    4   K 5 ALA F 178  ASP F 181  1  O  PHE F 180   N  GLY F 147           
SHEET    5   K 5 ALA F 165  ALA F 167 -1  N  HIS F 166   O  HIS F 179           
SHEET    1   L 2 TRP F 186  THR F 187  0                                        
SHEET    2   L 2 TYR F 193  ASN F 194  1  O  TYR F 193   N  THR F 187           
SHEET    1   M 5 ASN G 131  ARG G 134  0                                        
SHEET    2   M 5 ASN G  96  ILE G 101  1  N  TYR G  99   O  THR G 133           
SHEET    3   M 5 ILE G 142  GLY G 147  1  O  ILE G 144   N  ARG G 100           
SHEET    4   M 5 ALA G 178  ASP G 181  1  O  PHE G 180   N  GLY G 147           
SHEET    5   M 5 ALA G 165  ALA G 167 -1  N  HIS G 166   O  HIS G 179           
SHEET    1   N 2 TRP G 186  THR G 187  0                                        
SHEET    2   N 2 TYR G 193  ASN G 194  1  O  TYR G 193   N  THR G 187           
SHEET    1   O 5 ASN H 131  ARG H 134  0                                        
SHEET    2   O 5 ASN H  96  ILE H 101  1  N  LEU H  97   O  ASN H 131           
SHEET    3   O 5 ILE H 142  GLY H 147  1  O  ILE H 144   N  ARG H 100           
SHEET    4   O 5 ALA H 178  ASP H 181  1  O  PHE H 180   N  GLY H 147           
SHEET    5   O 5 ALA H 165  ALA H 167 -1  N  HIS H 166   O  HIS H 179           
SHEET    1   P 2 TRP H 186  THR H 187  0                                        
SHEET    2   P 2 TYR H 193  ASN H 194  1  O  TYR H 193   N  THR H 187           
LINK        ZN    ZN A4001                 NE2 HIS A 201     1555   1555  2.21  
LINK        ZN    ZN A4001                 NE2 HIS A 205     1555   1555  2.15  
LINK        ZN    ZN A4001                 NE2 HIS A 211     1555   1555  2.09  
LINK        ZN    ZN A4001                 O   HOH A4024     1555   1555  2.12  
LINK        ZN    ZN A4002                 OD2 ASP A 153     1555   1555  1.96  
LINK        ZN    ZN A4002                 NE2 HIS A 166     1555   1555  2.31  
LINK        ZN    ZN A4002                 NE2 HIS A 151     1555   1555  2.05  
LINK        ZN    ZN A4002                 ND1 HIS A 179     1555   1555  2.09  
LINK        CA    CA A4003                 O   LEU A 163     1555   1555  2.44  
LINK        CA    CA A4003                 OE2 GLU A 184     1555   1555  2.24  
LINK        CA    CA A4003                 OD2 ASP A 181     1555   1555  2.28  
LINK        CA    CA A4003                 OD1 ASP A 158     1555   1555  2.55  
LINK        CA    CA A4003                 O   GLY A 159     1555   1555  2.29  
LINK        CA    CA A4003                 O   SER A 161     1555   1555  2.33  
LINK        CA    CA A4004                 O   HOH A4016     1555   1555  2.48  
LINK        CA    CA A4004                 O   ASP A 141     1555   1555  2.32  
LINK        CA    CA A4004                 O   HOH A4115     1555   1555  2.28  
LINK        CA    CA A4004                 O   GLY A 175     1555   1555  2.25  
LINK        CA    CA A4004                 OD1 ASP A 177     1555   1555  2.61  
LINK        CA    CA A4004                 O   ASN A 173     1555   1555  2.45  
LINK        CA    CA A4005                 OD2 ASP A 107     1555   1555  2.12  
LINK        CA    CA A4005                 OD1 ASP A 182     1555   1555  2.63  
LINK        CA    CA A4005                 O   HOH A4088     1555   1555  2.41  
LINK        CA    CA A4005                 O   GLU A 184     1555   1555  2.31  
LINK        CA    CA A4005                 O   ASP A 182     1555   1555  2.57  
LINK        ZN    ZN B4006                 NE2 HIS B 201     1555   1555  2.20  
LINK        ZN    ZN B4006                 NE2 HIS B 205     1555   1555  2.27  
LINK        ZN    ZN B4006                 NE2 HIS B 211     1555   1555  2.15  
LINK        ZN    ZN B4006                 O   HOH B4058     1555   1555  2.21  
LINK        ZN    ZN B4006                 O   HOH B4022     1555   1555  2.36  
LINK        ZN    ZN B4007                 OD2 ASP B 153     1555   1555  2.09  
LINK        ZN    ZN B4007                 NE2 HIS B 166     1555   1555  1.90  
LINK        ZN    ZN B4007                 NE2 HIS B 151     1555   1555  2.16  
LINK        ZN    ZN B4007                 ND1 HIS B 179     1555   1555  2.03  
LINK        CA    CA B4008                 O   LEU B 163     1555   1555  2.30  
LINK        CA    CA B4008                 OE2 GLU B 184     1555   1555  2.37  
LINK        CA    CA B4008                 OD2 ASP B 181     1555   1555  2.19  
LINK        CA    CA B4008                 OD1 ASP B 158     1555   1555  2.44  
LINK        CA    CA B4008                 O   GLY B 159     1555   1555  2.36  
LINK        CA    CA B4008                 O   SER B 161     1555   1555  2.36  
LINK        CA    CA B4009                 O   HOH B4017     1555   1555  2.46  
LINK        CA    CA B4009                 O   ASP B 141     1555   1555  2.31  
LINK        CA    CA B4009                 O   HOH B4097     1555   1555  2.54  
LINK        CA    CA B4009                 O   GLY B 175     1555   1555  2.37  
LINK        CA    CA B4009                 OD1 ASP B 177     1555   1555  2.57  
LINK        CA    CA B4009                 O   ASN B 173     1555   1555  2.38  
LINK        CA    CA B4010                 OD2 ASP B 107     1555   1555  2.06  
LINK        CA    CA B4010                 OD1 ASP B 182     1555   1555  2.58  
LINK        CA    CA B4010                 O   HOH B4018     1555   1555  2.45  
LINK        CA    CA B4010                 O   GLU B 184     1555   1555  2.41  
LINK        CA    CA B4010                 O   ASP B 182     1555   1555  2.62  
LINK        ZN    ZN C4011                 NE2 HIS C 201     1555   1555  2.12  
LINK        ZN    ZN C4011                 O   HAE C3001     1555   1555  2.31  
LINK        ZN    ZN C4011                 NE2 HIS C 205     1555   1555  2.19  
LINK        ZN    ZN C4011                 NE2 HIS C 211     1555   1555  2.09  
LINK        ZN    ZN C4012                 NE2 HIS C 151     1555   1555  2.06  
LINK        ZN    ZN C4012                 OD2 ASP C 153     1555   1555  2.04  
LINK        ZN    ZN C4012                 NE2 HIS C 166     1555   1555  2.03  
LINK        ZN    ZN C4012                 ND1 HIS C 179     1555   1555  2.14  
LINK        CA    CA C4013                 OE2 GLU C 184     1555   1555  2.28  
LINK        CA    CA C4013                 O   GLY C 159     1555   1555  2.21  
LINK        CA    CA C4013                 O   LEU C 163     1555   1555  2.41  
LINK        CA    CA C4013                 OD1 ASP C 158     1555   1555  2.32  
LINK        CA    CA C4013                 OD2 ASP C 181     1555   1555  2.35  
LINK        CA    CA C4013                 O   SER C 161     1555   1555  2.32  
LINK        CA    CA C4014                 O   HOH C4147     1555   1555  2.31  
LINK        CA    CA C4014                 OD1 ASP C 177     1555   1555  2.52  
LINK        CA    CA C4014                 O   ASP C 141     1555   1555  2.25  
LINK        CA    CA C4014                 O   ASN C 173     1555   1555  2.38  
LINK        CA    CA C4014                 O   HOH C4020     1555   1555  2.33  
LINK        CA    CA C4014                 O   GLY C 175     1555   1555  2.42  
LINK        CA    CA C4015                 OD1 ASP C 107     1555   1555  3.12  
LINK        CA    CA C4015                 OD2 ASP C 107     1555   1555  2.36  
LINK        CA    CA C4015                 O   HOH C4150     1555   1555  2.41  
LINK        CA    CA C4015                 OD1 ASP C 182     1555   1555  2.90  
LINK        CA    CA C4015                 O   ASP C 182     1555   1555  2.56  
LINK        CA    CA C4015                 O   GLU C 184     1555   1555  2.40  
LINK        ZN    ZN D4016                 NE2 HIS D 201     1555   1555  2.17  
LINK        ZN    ZN D4016                 O2  HAE D3002     1555   1555  2.25  
LINK        ZN    ZN D4016                 NE2 HIS D 205     1555   1555  2.30  
LINK        ZN    ZN D4016                 NE2 HIS D 211     1555   1555  2.06  
LINK        ZN    ZN D4017                 NE2 HIS D 151     1555   1555  2.15  
LINK        ZN    ZN D4017                 OD2 ASP D 153     1555   1555  2.01  
LINK        ZN    ZN D4017                 NE2 HIS D 166     1555   1555  2.05  
LINK        ZN    ZN D4017                 ND1 HIS D 179     1555   1555  2.00  
LINK        CA    CA D4018                 O   GLY D 159     1555   1555  2.35  
LINK        CA    CA D4018                 OE2 GLU D 184     1555   1555  2.31  
LINK        CA    CA D4018                 O   SER D 161     1555   1555  2.31  
LINK        CA    CA D4018                 OD2 ASP D 181     1555   1555  2.33  
LINK        CA    CA D4018                 O   LEU D 163     1555   1555  2.26  
LINK        CA    CA D4018                 OD1 ASP D 158     1555   1555  2.37  
LINK        CA    CA D4019                 OD1 ASP D 177     1555   1555  2.53  
LINK        CA    CA D4019                 O   HOH D4126     1555   1555  2.50  
LINK        CA    CA D4019                 O   GLY D 175     1555   1555  2.27  
LINK        CA    CA D4019                 O   ASP D 141     1555   1555  2.27  
LINK        CA    CA D4019                 O   ASN D 173     1555   1555  2.36  
LINK        CA    CA D4019                 O   HOH D4133     1555   1555  2.41  
LINK        CA    CA D4020                 O   HOH D4150     1555   1555  3.10  
LINK        CA    CA D4020                 OD2 ASP D 107     1555   1555  2.30  
LINK        CA    CA D4020                 OD1 ASP D 182     1555   1555  2.53  
LINK        CA    CA D4020                 O   GLU D 184     1555   1555  2.34  
LINK        CA    CA D4020                 O   ASP D 182     1555   1555  2.67  
LINK        CA    CA D4020                 O   HOH D4139     1555   1555  2.21  
LINK         O2  HAE E3003                ZN    ZN E4021     1555   1555  1.97  
LINK        ZN    ZN E4021                 NE2 HIS E 211     1555   1555  2.40  
LINK        ZN    ZN E4021                 NE2 HIS E 205     1555   1555  1.95  
LINK        ZN    ZN E4021                 O   HAE E3003     1555   1555  2.52  
LINK        ZN    ZN E4021                 NE2 HIS E 201     1555   1555  2.33  
LINK        ZN    ZN E4022                 NE2 HIS E 151     1555   1555  2.03  
LINK        ZN    ZN E4022                 OD2 ASP E 153     1555   1555  1.98  
LINK        ZN    ZN E4022                 ND1 HIS E 179     1555   1555  2.19  
LINK        ZN    ZN E4022                 NE2 HIS E 166     1555   1555  2.13  
LINK        CA    CA E4023                 OD1 ASP E 158     1555   1555  2.37  
LINK        CA    CA E4023                 OE2 GLU E 184     1555   1555  2.28  
LINK        CA    CA E4023                 OD2 ASP E 181     1555   1555  2.29  
LINK        CA    CA E4023                 O   GLY E 159     1555   1555  2.38  
LINK        CA    CA E4023                 O   SER E 161     1555   1555  2.37  
LINK        CA    CA E4023                 O   LEU E 163     1555   1555  2.30  
LINK        CA    CA E4024                 O   ASN E 173     1555   1555  2.54  
LINK        CA    CA E4024                 O   GLY E 175     1555   1555  2.44  
LINK        CA    CA E4024                 OD1 ASP E 177     1555   1555  2.69  
LINK        CA    CA E4024                 O   ASP E 141     1555   1555  2.32  
LINK        CA    CA E4024                 O   HOH E4032     1555   1555  2.31  
LINK        CA    CA E4025                 OD1 ASP E 107     1555   1555  3.31  
LINK        CA    CA E4025                 OD1 ASP E 182     1555   1555  2.36  
LINK        CA    CA E4025                 O   ASP E 182     1555   1555  2.50  
LINK        CA    CA E4025                 O   HOH E4095     1555   1555  2.30  
LINK        CA    CA E4025                 OD2 ASP E 107     1555   1555  2.59  
LINK        CA    CA E4025                 O   GLU E 184     1555   1555  2.55  
LINK         O   HAE F3004                ZN    ZN F4026     1555   1555  1.75  
LINK        ZN    ZN F4026                 NE2 HIS F 201     1555   1555  2.31  
LINK        ZN    ZN F4026                 NE2 HIS F 205     1555   1555  1.82  
LINK        ZN    ZN F4026                 N   HAE F3004     1555   1555  2.73  
LINK        ZN    ZN F4027                 ND1 HIS F 179     1555   1555  2.20  
LINK        ZN    ZN F4027                 NE2 HIS F 151     1555   1555  1.95  
LINK        ZN    ZN F4027                 OD2 ASP F 153     1555   1555  1.82  
LINK        ZN    ZN F4027                 NE2 HIS F 166     1555   1555  2.22  
LINK        CA    CA F4028                 O   LEU F 163     1555   1555  2.35  
LINK        CA    CA F4028                 OD2 ASP F 181     1555   1555  2.40  
LINK        CA    CA F4028                 OE2 GLU F 184     1555   1555  2.32  
LINK        CA    CA F4028                 OD1 ASP F 158     1555   1555  2.53  
LINK        CA    CA F4028                 O   GLY F 159     1555   1555  2.29  
LINK        CA    CA F4028                 O   SER F 161     1555   1555  2.40  
LINK        CA    CA F4029                 O   ASN F 173     1555   1555  2.37  
LINK        CA    CA F4029                 O   GLY F 175     1555   1555  2.55  
LINK        CA    CA F4029                 OD1 ASP F 177     1555   1555  2.59  
LINK        CA    CA F4029                 O   ASP F 141     1555   1555  2.31  
LINK        CA    CA F4029                 O   HOH F4038     1555   1555  2.76  
LINK        CA    CA F4030                 O   ASP F 182     1555   1555  2.66  
LINK        CA    CA F4030                 O   HOH F4125     1555   1555  3.09  
LINK        CA    CA F4030                 O   GLU F 184     1555   1555  2.19  
LINK        CA    CA F4030                 OD2 ASP F 107     1555   1555  2.46  
LINK        CA    CA F4030                 OD1 ASP F 182     1555   1555  2.56  
LINK        ZN    ZN G4031                 O   HOH G4090     1555   1555  2.59  
LINK        ZN    ZN G4031                 NE2 HIS G 205     1555   1555  1.97  
LINK        ZN    ZN G4031                 NE2 HIS G 211     1555   1555  2.11  
LINK        ZN    ZN G4031                 NE2 HIS G 201     1555   1555  2.11  
LINK        ZN    ZN G4032                 ND1 HIS G 179     1555   1555  2.05  
LINK        ZN    ZN G4032                 NE2 HIS G 166     1555   1555  2.29  
LINK        ZN    ZN G4032                 OD1 ASP G 153     1555   1555  2.01  
LINK        ZN    ZN G4032                 NE2 HIS G 151     1555   1555  2.11  
LINK        CA    CA G4033                 O   SER G 161     1555   1555  2.30  
LINK        CA    CA G4033                 OD2 ASP G 181     1555   1555  2.35  
LINK        CA    CA G4033                 OE2 GLU G 184     1555   1555  2.34  
LINK        CA    CA G4033                 OD1 ASP G 158     1555   1555  2.30  
LINK        CA    CA G4033                 O   GLY G 159     1555   1555  2.40  
LINK        CA    CA G4033                 O   LEU G 163     1555   1555  2.24  
LINK        CA    CA G4034                 O   ASN G 173     1555   1555  2.42  
LINK        CA    CA G4034                 OD1 ASP G 177     1555   1555  2.86  
LINK        CA    CA G4034                 O   HOH G4131     1555   1555  2.08  
LINK        CA    CA G4034                 O   ASP G 141     1555   1555  2.37  
LINK        CA    CA G4034                 O   GLY G 175     1555   1555  2.49  
LINK        CA    CA G4035                 OD1 ASP G 182     1555   1555  2.69  
LINK        CA    CA G4035                 OD1 ASP G 107     1555   1555  3.02  
LINK        CA    CA G4035                 O   ASP G 182     1555   1555  2.61  
LINK        CA    CA G4035                 O   GLU G 184     1555   1555  2.43  
LINK        CA    CA G4035                 OD2 ASP G 107     1555   1555  2.45  
LINK        ZN    ZN H4036                 O   HOH H4124     1555   1555  2.60  
LINK        ZN    ZN H4036                 NE2 HIS H 205     1555   1555  2.05  
LINK        ZN    ZN H4036                 NE2 HIS H 211     1555   1555  2.18  
LINK        ZN    ZN H4036                 NE2 HIS H 201     1555   1555  2.11  
LINK        ZN    ZN H4037                 ND1 HIS H 179     1555   1555  2.15  
LINK        ZN    ZN H4037                 OD2 ASP H 153     1555   1555  1.89  
LINK        ZN    ZN H4037                 NE2 HIS H 151     1555   1555  2.27  
LINK        CA    CA H4038                 OE2 GLU H 184     1555   1555  2.15  
LINK        CA    CA H4038                 OD1 ASP H 158     1555   1555  2.32  
LINK        CA    CA H4038                 O   LEU H 163     1555   1555  2.24  
LINK        CA    CA H4038                 OD2 ASP H 181     1555   1555  2.45  
LINK        CA    CA H4038                 O   SER H 161     1555   1555  2.35  
LINK        CA    CA H4038                 O   GLY H 159     1555   1555  2.32  
LINK        CA    CA H4039                 O   HOH H4110     1555   1555  3.25  
LINK        CA    CA H4039                 O   GLY H 175     1555   1555  2.45  
LINK        CA    CA H4039                 O   ASP H 141     1555   1555  2.25  
LINK        CA    CA H4039                 OD1 ASP H 177     1555   1555  2.72  
LINK        CA    CA H4039                 O   ASN H 173     1555   1555  2.45  
LINK        CA    CA H4040                 O   HOH H4133     1555   1555  3.07  
LINK        CA    CA H4040                 OD2 ASP H 107     1555   1555  2.52  
LINK        CA    CA H4040                 OD1 ASP H 182     1555   1555  2.38  
LINK        CA    CA H4040                 O   HOH H4125     1555   1555  2.61  
LINK        CA    CA H4040                 O   GLU H 184     1555   1555  2.34  
LINK        CA    CA H4040                 O   ASP H 182     1555   1555  2.49  
CISPEP   1 LYS D  228    SER D  229          0       -14.69                     
CISPEP   2 GLY E  248    ASP E  249          0         8.06                     
CISPEP   3 THR F  226    GLY F  227          0        23.96                     
CISPEP   4 ARG G   88    THR G   89          0        21.39                     
CISPEP   5 THR G  226    GLY G  227          0        15.11                     
CISPEP   6 GLY G  227    LYS G  228          0        24.19                     
CRYST1  161.836   71.974  138.130  90.00 124.59  90.00 C 1 2 1      32          
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      0.006179  0.000000  0.004261        0.00000                         
SCALE2      0.000000  0.013894  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008794        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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