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Database: PDB
Entry: 3MDZ
LinkDB: 3MDZ
Original site: 3MDZ 
HEADER    LYASE                                   31-MAR-10   3MDZ              
TITLE     CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE VII [ISOFORM 1], CA7    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 7;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES IN UNP 24-281;                                    
COMPND   5 SYNONYM: CA7, CARBONIC ANHYDRASE VII, CA-VII, CARBONATE DEHYDRATASE  
COMPND   6 VII;                                                                 
COMPND   7 EC: 4.2.1.1;                                                         
COMPND   8 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: CA7;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    CARBONIC ANHYDRASE VII, CA7, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS 
KEYWDS   2 CONSORTIUM, SGC, CYTOPLASM, LYASE, METAL-BINDING, ZINC               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.UGOCHUKWU,N.SHAFQAT,E.PILKA,A.CHAIKUAD,T.KROJER,J.MUNIZ,J.KIM,      
AUTHOR   2 J.BRAY,C.BOUNTRA,C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,F.VON DELFT,     
AUTHOR   3 E.P.CARPENTER,W.W.YUE,U.OPPERMANN,STRUCTURAL GENOMICS CONSORTIUM     
AUTHOR   4 (SGC)                                                                
REVDAT   2   08-NOV-17 3MDZ    1       REMARK                                   
REVDAT   1   23-JUN-10 3MDZ    0                                                
JRNL        AUTH   E.UGOCHUKWU,N.SHAFQAT,E.PILKA,A.CHAIKUAD,T.KROJER,J.MUNIZ,   
JRNL        AUTH 2 J.KIM,J.BRAY,C.BOUNTRA,C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,   
JRNL        AUTH 3 F.VON DELFT,E.P.CARPENTER,W.W.YUE,U.OPPERMANN                
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE VII [ISOFORM   
JRNL        TITL 2 1], CA7                                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.32 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.32                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.74                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 11825                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 588                             
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) : 2.32                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.38                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 843                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.44                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3280                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 40                           
REMARK   3   BIN FREE R VALUE                    : 0.4390                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1987                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 48                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.61000                                              
REMARK   3    B22 (A**2) : -1.69000                                             
REMARK   3    B33 (A**2) : -1.92000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.364         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.250         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.205         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.935        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2092 ; 0.015 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1401 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2849 ; 1.570 ; 1.947       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3402 ; 0.898 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   260 ; 7.016 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    85 ;34.647 ;23.059       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   305 ;15.550 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;14.466 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   300 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2331 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   431 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1297 ; 0.650 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   519 ; 0.127 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2087 ; 1.192 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   795 ; 1.891 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   761 ; 2.999 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     5        A    43                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.2024  12.4679  81.3533              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0442 T22:   0.0817                                     
REMARK   3      T33:   0.1331 T12:  -0.0453                                     
REMARK   3      T13:  -0.0244 T23:   0.0024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3750 L22:   7.9527                                     
REMARK   3      L33:   6.3009 L12:  -1.9088                                     
REMARK   3      L13:  -0.1138 L23:  -1.9523                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0067 S12:  -0.2256 S13:   0.2352                       
REMARK   3      S21:   0.1336 S22:  -0.2072 S23:  -0.7980                       
REMARK   3      S31:  -0.3493 S32:   0.5190 S33:   0.2005                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    44        A    80                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.9309  11.4725  75.2292              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2107 T22:   0.5916                                     
REMARK   3      T33:   0.3845 T12:   0.1183                                     
REMARK   3      T13:  -0.0936 T23:  -0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9135 L22:   3.6765                                     
REMARK   3      L33:   7.5775 L12:   0.4747                                     
REMARK   3      L13:   1.6429 L23:  -0.4718                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0209 S12:   0.2750 S13:  -0.0383                       
REMARK   3      S21:  -0.5143 S22:   0.0397 S23:   0.7235                       
REMARK   3      S31:   0.0003 S32:  -1.1713 S33:  -0.0187                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    81        A   152                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2154  13.5166  75.3510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1506 T22:   0.2118                                     
REMARK   3      T33:   0.0509 T12:   0.1107                                     
REMARK   3      T13:  -0.0238 T23:   0.0367                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2011 L22:   7.2765                                     
REMARK   3      L33:   5.1900 L12:   1.8432                                     
REMARK   3      L13:   0.3180 L23:   0.1690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0387 S12:   0.0612 S13:   0.0357                       
REMARK   3      S21:  -0.6727 S22:  -0.0134 S23:   0.2002                       
REMARK   3      S31:  -0.3400 S32:  -0.4805 S33:  -0.0253                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   153        A   229                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.5274  19.7049  79.6816              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3074 T22:   0.3265                                     
REMARK   3      T33:   0.2320 T12:   0.2387                                     
REMARK   3      T13:  -0.0057 T23:   0.0709                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7320 L22:   4.5484                                     
REMARK   3      L33:   5.8005 L12:  -0.1368                                     
REMARK   3      L13:  -0.2357 L23:   0.4751                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0192 S12:  -0.0913 S13:   0.2562                       
REMARK   3      S21:  -0.0788 S22:   0.0910 S23:   0.8157                       
REMARK   3      S31:  -0.9861 S32:  -1.1931 S33:  -0.0718                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   230        A   262                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2418  17.2621  84.8750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1277 T22:   0.0647                                     
REMARK   3      T33:   0.0731 T12:   0.0118                                     
REMARK   3      T13:  -0.0110 T23:  -0.0201                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9909 L22:   4.5487                                     
REMARK   3      L33:   6.7665 L12:  -0.5295                                     
REMARK   3      L13:   0.0511 L23:  -0.5240                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0354 S12:  -0.3330 S13:   0.2032                       
REMARK   3      S21:   0.3570 S22:   0.1309 S23:  -0.0628                       
REMARK   3      S31:  -0.4297 S32:   0.0926 S33:  -0.0955                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3MDZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-APR-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000058426.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12474                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.320                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.740                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : 0.07800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.32                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.70700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.70700                            
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: PHASER                                                
REMARK 200 STARTING MODEL: 3CAJ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NA/K TARTRATE, 1M AMMONIUM          
REMARK 280  SULPHATE, 0.1M TRI NACIT, PH 4.5, VAPOR DIFFUSION, SITTING DROP,    
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.22150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       41.22150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       34.85500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       48.87300            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       34.85500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       48.87300            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       41.22150            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       34.85500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       48.87300            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       41.22150            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       34.85500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       48.87300            
REMARK 290   SMTRY3   8  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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     SER A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     VAL A    -8                                                      
REMARK 465     ASP A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     GLY A    -5                                                      
REMARK 465     THR A    -4                                                      
REMARK 465     GLU A    -3                                                      
REMARK 465     ASN A    -2                                                      
REMARK 465     LEU A    -1                                                      
REMARK 465     TYR A     0                                                      
REMARK 465     PHE A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  54    CG   CD   OE1  OE2                                  
REMARK 470     CYS A  56    SG                                                  
REMARK 470     ASP A  76    CG   OD1  OD2                                       
REMARK 470     ASP A  77    OD1  OD2                                            
REMARK 470     ARG A  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  87    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 102    CD   CE   NZ                                        
REMARK 470     ASP A 104    OD1  OD2                                            
REMARK 470     ASP A 154    CG   OD1  OD2                                       
REMARK 470     GLU A 155    CG   CD   OE1  OE2                                  
REMARK 470     SER A 158    OG                                                  
REMARK 470     LEU A 162    CG   CD1  CD2                                       
REMARK 470     TYR A 167    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     ARG A 170    NE   CZ   NH1  NH2                                  
REMARK 470     GLN A 177    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 184    CG   CD   CE   NZ                                   
REMARK 470     GLU A 236    CD   OE1  OE2                                       
REMARK 470     ASP A 237    CG   OD1  OD2                                       
REMARK 470     GLU A 239    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 240    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  74       47.74   -145.31                                   
REMARK 500    ASP A  77       37.59    -84.89                                   
REMARK 500    MET A 159       36.25    -94.80                                   
REMARK 500    PHE A 178       70.05   -150.58                                   
REMARK 500    PRO A 203      137.27    -39.24                                   
REMARK 500    GLU A 222      -36.21    -39.59                                   
REMARK 500    LYS A 254       50.54     34.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 263  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 EZL A 264   N1                                                     
REMARK 620 2 HIS A  96   NE2 102.9                                              
REMARK 620 3 HIS A 121   ND1 115.0 118.3                                        
REMARK 620 4 HIS A  98   NE2 107.6 111.0 101.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 263                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EZL A 264                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 265                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 266                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 267                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3CAJ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CARBONIC ANHYDRASE II IN COMPLEX      
REMARK 900 WITH ETHOXZOLAMIDE                                                   
DBREF  3MDZ A    5   262  UNP    P43166   CAH7_HUMAN       5    262             
SEQADV 3MDZ MET A  -18  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ HIS A  -17  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ HIS A  -16  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ HIS A  -15  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ HIS A  -14  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ HIS A  -13  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ HIS A  -12  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ SER A  -11  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ SER A  -10  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ GLY A   -9  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ VAL A   -8  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ ASP A   -7  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ LEU A   -6  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ GLY A   -5  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ THR A   -4  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ GLU A   -3  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ ASN A   -2  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ LEU A   -1  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ TYR A    0  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ PHE A    1  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ GLN A    2  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ SER A    3  UNP  P43166              EXPRESSION TAG                 
SEQADV 3MDZ MET A    4  UNP  P43166              EXPRESSION TAG                 
SEQRES   1 A  281  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  281  GLY THR GLU ASN LEU TYR PHE GLN SER MET HIS GLY TRP          
SEQRES   3 A  281  GLY TYR GLY GLN ASP ASP GLY PRO SER HIS TRP HIS LYS          
SEQRES   4 A  281  LEU TYR PRO ILE ALA GLN GLY ASP ARG GLN SER PRO ILE          
SEQRES   5 A  281  ASN ILE ILE SER SER GLN ALA VAL TYR SER PRO SER LEU          
SEQRES   6 A  281  GLN PRO LEU GLU LEU SER TYR GLU ALA CYS MET SER LEU          
SEQRES   7 A  281  SER ILE THR ASN ASN GLY HIS SER VAL GLN VAL ASP PHE          
SEQRES   8 A  281  ASN ASP SER ASP ASP ARG THR VAL VAL THR GLY GLY PRO          
SEQRES   9 A  281  LEU GLU GLY PRO TYR ARG LEU LYS GLN PHE HIS PHE HIS          
SEQRES  10 A  281  TRP GLY LYS LYS HIS ASP VAL GLY SER GLU HIS THR VAL          
SEQRES  11 A  281  ASP GLY LYS SER PHE PRO SER GLU LEU HIS LEU VAL HIS          
SEQRES  12 A  281  TRP ASN ALA LYS LYS TYR SER THR PHE GLY GLU ALA ALA          
SEQRES  13 A  281  SER ALA PRO ASP GLY LEU ALA VAL VAL GLY VAL PHE LEU          
SEQRES  14 A  281  GLU THR GLY ASP GLU HIS PRO SER MET ASN ARG LEU THR          
SEQRES  15 A  281  ASP ALA LEU TYR MET VAL ARG PHE LYS GLY THR LYS ALA          
SEQRES  16 A  281  GLN PHE SER CYS PHE ASN PRO LYS CYS LEU LEU PRO ALA          
SEQRES  17 A  281  SER ARG HIS TYR TRP THR TYR PRO GLY SER LEU THR THR          
SEQRES  18 A  281  PRO PRO LEU SER GLU SER VAL THR TRP ILE VAL LEU ARG          
SEQRES  19 A  281  GLU PRO ILE CYS ILE SER GLU ARG GLN MET GLY LYS PHE          
SEQRES  20 A  281  ARG SER LEU LEU PHE THR SER GLU ASP ASP GLU ARG ILE          
SEQRES  21 A  281  HIS MET VAL ASN ASN PHE ARG PRO PRO GLN PRO LEU LYS          
SEQRES  22 A  281  GLY ARG VAL VAL LYS ALA SER PHE                              
HET     ZN  A 263       1                                                       
HET    EZL  A 264      16                                                       
HET    GOL  A 265       6                                                       
HET    GOL  A 266       6                                                       
HET    GOL  A 267       6                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     EZL 6-ETHOXY-1,3-BENZOTHIAZOLE-2-SULFONAMIDE                         
HETNAM     GOL GLYCEROL                                                         
HETSYN     EZL ETHOXZOLAMIDE                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  EZL    C9 H10 N2 O3 S2                                              
FORMUL   4  GOL    3(C3 H8 O3)                                                  
FORMUL   7  HOH   *48(H2 O)                                                     
HELIX    1   1 GLY A   14  LEU A   21  5                                   8    
HELIX    2   2 TYR A   22  GLY A   27  5                                   6    
HELIX    3   3 THR A  132  ALA A  137  1                                   6    
HELIX    4   4 PRO A  157  MET A  159  5                                   3    
HELIX    5   5 ASN A  160  LEU A  166  1                                   7    
HELIX    6   6 ASN A  182  LEU A  187  5                                   6    
HELIX    7   7 SER A  221  SER A  230  1                                  10    
SHEET    1   A 2 ASN A  34  ILE A  35  0                                        
SHEET    2   A 2 THR A 110  VAL A 111  1  O  THR A 110   N  ILE A  35           
SHEET    1   B10 VAL A  41  TYR A  42  0                                        
SHEET    2   B10 LYS A 259  ALA A 260  1  O  ALA A 260   N  VAL A  41           
SHEET    3   B10 TYR A 193  GLY A 198 -1  N  THR A 195   O  LYS A 259           
SHEET    4   B10 VAL A 209  LEU A 214 -1  O  VAL A 209   N  GLY A 198           
SHEET    5   B10 LEU A 143  THR A 152  1  N  GLY A 147   O  LEU A 214           
SHEET    6   B10 SER A 118  TRP A 125 -1  N  LEU A 122   O  VAL A 146           
SHEET    7   B10 TYR A  90  TRP A  99 -1  N  LYS A  93   O  VAL A 123           
SHEET    8   B10 VAL A  68  PHE A  72 -1  N  PHE A  72   O  LYS A  93           
SHEET    9   B10 SER A  58  ASN A  63 -1  N  LEU A  59   O  ASP A  71           
SHEET   10   B10 LYS A 175  GLN A 177 -1  O  ALA A 176   N  ILE A  61           
SHEET    1   C 6 GLU A  50  SER A  52  0                                        
SHEET    2   C 6 VAL A  80  THR A  82 -1  O  VAL A  80   N  SER A  52           
SHEET    3   C 6 TYR A  90  TRP A  99 -1  O  TYR A  90   N  VAL A  81           
SHEET    4   C 6 SER A 118  TRP A 125 -1  O  VAL A 123   N  LYS A  93           
SHEET    5   C 6 LEU A 143  THR A 152 -1  O  VAL A 146   N  LEU A 122           
SHEET    6   C 6 ILE A 218  ILE A 220  1  O  ILE A 218   N  GLU A 151           
LINK        ZN    ZN A 263                 N1  EZL A 264     1555   1555  1.90  
LINK         NE2 HIS A  96                ZN    ZN A 263     1555   1555  2.01  
LINK         ND1 HIS A 121                ZN    ZN A 263     1555   1555  2.14  
LINK         NE2 HIS A  98                ZN    ZN A 263     1555   1555  2.18  
CISPEP   1 SER A   31    PRO A   32          0         1.28                     
CISPEP   2 PRO A  203    PRO A  204          0        10.58                     
SITE     1 AC1  4 HIS A  96  HIS A  98  HIS A 121  EZL A 264                    
SITE     1 AC2 11 HIS A  96  HIS A  98  HIS A 121  VAL A 123                    
SITE     2 AC2 11 LEU A 200  THR A 201  THR A 202  PRO A 203                    
SITE     3 AC2 11 TRP A 211   ZN A 263  GOL A 267                               
SITE     1 AC3  5 ARG A 223  LYS A 227  PRO A 252  LEU A 253                    
SITE     2 AC3  5 LYS A 254                                                     
SITE     1 AC4  4 TYR A  22  PRO A  23  ILE A  24  PRO A 204                    
SITE     1 AC5  4 GLN A  69  GLN A  94  THR A 132  EZL A 264                    
CRYST1   69.710   97.746   82.443  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014345  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010231  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012130        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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