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Database: PDB
Entry: 1I91
LinkDB: 1I91
Original site: 1I91 
HEADER    LYASE                                   16-MAR-01   1I91              
TITLE     CARBONIC ANHYDRASE II COMPLEXED WITH AL-6619 2H-THIENO[3,2-E]-1,2-    
TITLE    2 THIAZINE-6-SULFONAMIDE, 2-(3-HYDROXYPHENYL)-3-(4-MORPHOLINYL)-, 1,1- 
TITLE    3 DIOXIDE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBONIC ANHYDRASE II;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE II;                                   
COMPND   5 EC: 4.2.1.1;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CARBONIC ANHYDRASE II, AL-6619, LYASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.-Y.KIM,J.S.CHANG,J.LIAO,J.A.MAY,D.W.CHRISTIANSON                    
REVDAT   5   04-APR-18 1I91    1       REMARK                                   
REVDAT   4   24-FEB-09 1I91    1       VERSN                                    
REVDAT   3   01-APR-03 1I91    1       JRNL                                     
REVDAT   2   13-MAR-02 1I91    1       JRNL   REMARK                            
REVDAT   1   28-MAR-01 1I91    0                                                
JRNL        AUTH   C.Y.KIM,D.A.WHITTINGTON,J.S.CHANG,J.LIAO,J.A.MAY,            
JRNL        AUTH 2 D.W.CHRISTIANSON                                             
JRNL        TITL   STRUCTURAL ASPECTS OF ISOZYME SELECTIVITY IN THE BINDING OF  
JRNL        TITL 2 INHIBITORS TO CARBONIC ANHYDRASES II AND IV.                 
JRNL        REF    J.MED.CHEM.                   V.  45   888 2002              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   11831900                                                     
JRNL        DOI    10.1021/JM010163D                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 15740                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.151                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 767                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2058                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 107                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.49                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.700                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1I91 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-01.                  
REMARK 100 THE DEPOSITION ID IS D_1000013056.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-SEP-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16912                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.10500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: METHYL MERCURIC ACETATE, TRIS-SULFATE,   
REMARK 280  AMMONIUM SULFATE, PH 8.0, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       20.50000            
REMARK 290   SMTRY3   2  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 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     SER A     2                                                      
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    THR A    35     O    HOH A   369              1.02            
REMARK 500   C    THR A    35     O    HOH A   369              2.18            
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   NH1  ARG A    27     O    HIS A    36     2556     1.38            
REMARK 500   O    VAL A   150     O    HOH A   265     1545     1.59            
REMARK 500   N    GLY A   102     OD2  ASP A   130     1545     1.62            
REMARK 500   OD2  ASP A   110     O    HOH A   350     2546     1.98            
REMARK 500   CA   GLY A   102     OD2  ASP A   130     1545     2.01            
REMARK 500   NH1  ARG A    27     C    HIS A    36     2556     2.09            
REMARK 500   O    LYS A   113     O    HOH A   306     1545     2.10            
REMARK 500   OE1  GLN A   103     NZ   LYS A   133     1545     2.10            
REMARK 500   CA   GLY A   129     O    HOH A   352     1565     2.17            
REMARK 500   CG   LYS A    39     OE1  GLN A   137     2546     2.18            
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    HIS A   4      149.85   -179.79                                   
REMARK 500    ASN A  11       21.80   -145.61                                   
REMARK 500    ALA A  65     -176.67   -176.25                                   
REMARK 500    ASP A  75       60.83    -65.35                                   
REMARK 500    ASN A 244       55.27    -94.01                                   
REMARK 500    LYS A 252     -135.15     56.90                                   
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                              HG A 263  HG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 206   SG                                                     
REMARK 620 2 VAL A 135   O    61.0                                              
REMARK 620 3 GLU A 205   O    94.9 154.5                                        
REMARK 620 4 GLN A 137   O    83.8  96.0  89.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 262  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  96   NE2                                                    
REMARK 620 2 HIS A 119   ND1  97.9                                              
REMARK 620 3 HIS A  94   NE2 117.4 111.1                                        
REMARK 620 4 INQ A 555   N03 116.3 113.7 101.0                                  
REMARK 620 5 INQ A 555   S01 138.7  96.3  92.8  24.4                            
REMARK 620 N                    1     2     3     4                             
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 262                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 263                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INQ A 555                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1I8Z   RELATED DB: PDB                                   
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH AL-6629                         
REMARK 900 RELATED ID: 1I90   RELATED DB: PDB                                   
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH AL-8520                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE RESIDUE NUMBERING IS NOT SEQUENTIAL.                             
REMARK 999 RESIDUE 125 IS COVALENTLY BOUND TO RESIDUE 127.                      
DBREF  1I91 A    2   261  UNP    P00918   CAH2_HUMAN       1    259             
SEQRES   1 A  259  SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU          
SEQRES   2 A  259  HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG          
SEQRES   3 A  259  GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR          
SEQRES   4 A  259  ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN          
SEQRES   5 A  259  ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE          
SEQRES   6 A  259  ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU          
SEQRES   7 A  259  LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN          
SEQRES   8 A  259  PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER          
SEQRES   9 A  259  GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU          
SEQRES  10 A  259  HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY          
SEQRES  11 A  259  LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY          
SEQRES  12 A  259  ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN          
SEQRES  13 A  259  LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY          
SEQRES  14 A  259  LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU          
SEQRES  15 A  259  LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER          
SEQRES  16 A  259  LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE          
SEQRES  17 A  259  VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL          
SEQRES  18 A  259  LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU          
SEQRES  19 A  259  PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN          
SEQRES  20 A  259  PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS              
HET     ZN  A 262       1                                                       
HET     HG  A 263       1                                                       
HET    INQ  A 555      29                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      HG MERCURY (II) ION                                                 
HETNAM     INQ 6-[N-(3-HYDROXY-PHENYL)-3-(MORPHOLIN-4-YLMETHYL)-2H-             
HETNAM   2 INQ  THIENO[3,2-E]-1,2-THIAZINE-1,1,-DIOXIDE]-SULFONAMIDE            
HETSYN     INQ AL-6619, [2H-THIENO[3,2-E]-1,2-THIAZINE-6-SULFONAMIDE,           
HETSYN   2 INQ  2-(3-HYDROXYPHENYL)-3-(4-MORPHOLINYL)-, 1,1-DIOXIDE]            
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   HG    HG 2+                                                        
FORMUL   4  INQ    C17 H19 N3 O6 S3                                             
FORMUL   5  HOH   *107(H2 O)                                                    
HELIX    1   1 HIS A   15  ASP A   19  5                                   5    
HELIX    2   2 PHE A   20  GLY A   25  5                                   6    
HELIX    3   3 LYS A  127  GLY A  129  5                                   3    
HELIX    4   4 ASP A  130  VAL A  135  1                                   6    
HELIX    5   5 LYS A  154  GLY A  156  5                                   3    
HELIX    6   6 LEU A  157  LEU A  164  1                                   8    
HELIX    7   7 ASP A  165  LYS A  168  5                                   4    
HELIX    8   8 ASP A  180  LEU A  185  5                                   6    
HELIX    9   9 SER A  219  ARG A  227  1                                   9    
SHEET    1   A 2 ASP A  32  ILE A  33  0                                        
SHEET    2   A 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33           
SHEET    1   B16 LYS A  39  TYR A  40  0                                        
SHEET    2   B16 LYS A 257  ALA A 258  1  N  ALA A 258   O  LYS A  39           
SHEET    3   B16 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257           
SHEET    4   B16 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196           
SHEET    5   B16 LEU A 141  VAL A 150  1  O  LEU A 141   N  THR A 208           
SHEET    6   B16 ILE A 216  VAL A 218  1  O  ILE A 216   N  LYS A 149           
SHEET    7   B16 LEU A 141  VAL A 150  1  O  PHE A 147   N  ILE A 216           
SHEET    8   B16 ALA A 116  ASN A 124 -1  O  ALA A 116   N  LEU A 148           
SHEET    9   B16 TYR A  88  TRP A  97 -1  N  ARG A  89   O  TRP A 123           
SHEET   10   B16 VAL A  78  GLY A  81 -1  N  LEU A  79   O  TYR A  88           
SHEET   11   B16 LEU A  47  SER A  50 -1  N  SER A  48   O  LYS A  80           
SHEET   12   B16 VAL A  78  GLY A  81 -1  N  VAL A  78   O  SER A  50           
SHEET   13   B16 TYR A  88  TRP A  97 -1  O  TYR A  88   N  LEU A  79           
SHEET   14   B16 PHE A  66  PHE A  70 -1  O  PHE A  66   N  PHE A  95           
SHEET   15   B16 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69           
SHEET   16   B16 SER A 173  ASP A 175 -1  O  ALA A 174   N  ILE A  59           
LINK        HG    HG A 263                 SG  CYS A 206     1555   1555  1.60  
LINK        ZN    ZN A 262                 NE2 HIS A  96     1555   1555  1.79  
LINK        ZN    ZN A 262                 ND1 HIS A 119     1555   1555  1.95  
LINK        ZN    ZN A 262                 NE2 HIS A  94     1555   1555  1.73  
LINK        ZN    ZN A 262                 N03 INQ A 555     1555   1555  1.81  
LINK        HG    HG A 263                 O   VAL A 135     1555   1555  3.35  
LINK        HG    HG A 263                 O   GLU A 205     1555   1555  3.26  
LINK        HG    HG A 263                 O   GLN A 137     1555   1555  3.10  
LINK        ZN    ZN A 262                 S01 INQ A 555     1555   1555  2.92  
CISPEP   1 SER A   29    PRO A   30          0         0.18                     
CISPEP   2 PRO A  201    PRO A  202          0         0.36                     
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  INQ A 555                    
SITE     1 AC2  4 VAL A 135  GLN A 137  GLU A 205  CYS A 206                    
SITE     1 AC3 11 ASN A  67  GLN A  92  HIS A  94  HIS A  96                    
SITE     2 AC3 11 HIS A 119  PHE A 131  LEU A 198  THR A 199                    
SITE     3 AC3 11 THR A 200   ZN A 262  HOH A 303                               
CRYST1   42.400   41.000   72.200  90.00 104.90  90.00 P 1 21 1      2          
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      0.023585  0.000000  0.006275        0.00000                         
SCALE2      0.000000  0.024390  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014332        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system