GenomeNet

Database: PDB
Entry: 4KUV
LinkDB: 4KUV
Original site: 4KUV 
HEADER    LYASE/LYASE INHIBITOR                   22-MAY-13   4KUV              
TITLE     CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH THE  
TITLE    2 5-(3-(4-CHLOROPHENYLSULFONYL)UREIDO)PYRIDINE-2-SULFONAMIDE INHIBITOR 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE II, CARBONIC ANHYDRASE C, CAC,        
COMPND   5 CARBONIC ANHYDRASE II, CA-II;                                        
COMPND   6 EC: 4.2.1.1;                                                         
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: CA2;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    LYASE, LYASE-LYASE INHIBITOR COMPLEX                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.FERRARONI                                                           
REVDAT   1   25-JUN-14 4KUV    0                                                
JRNL        AUTH   M.FERRARONI,C.T.SUPURAN,F.CARTA,M.BOZDAG,A.SCOZZAFAVA        
JRNL        TITL   NEW CLASSES OF CARBONIC ANHYDRASE INHIBITORS                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 49214                          
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) : 0.150                           
REMARK   3   R VALUE            (WORKING SET) : 0.149                           
REMARK   3   FREE R VALUE                     : 0.170                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2515                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.39                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2187                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 58.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1840                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 110                          
REMARK   3   BIN FREE R VALUE                    : 0.1880                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2031                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 261                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.54                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.86                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.12000                                              
REMARK   3    B22 (A**2) : -0.16000                                             
REMARK   3    B33 (A**2) : 0.03000                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.02000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.054         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.054         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.028         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.649         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2205 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2041 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3014 ; 1.507 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4739 ; 0.792 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   280 ; 6.347 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   106 ;37.554 ;25.094       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   364 ;12.232 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;23.316 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   315 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2527 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   516 ; 0.002 ; 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):  1048 ; 0.806 ; 0.946       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1047 ; 0.792 ; 0.944       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1313 ; 1.349 ; 1.418       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 4KUV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB079823.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALBA                               
REMARK 200  BEAMLINE                       : XALOC                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.980                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55094                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 71.382                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 71.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.4200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.19                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 13.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.260                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 3P58                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M SODIUM CITRATE, TRIS 50 MM, PH     
REMARK 280  8.0, VAPOR DIFFUSION, TEMPERATURE 296K                              
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       20.67950            
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 300 REMARK: MONOMER                                                      
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 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     LYS A   9    CG   CD   CE   NZ                                   
REMARK 470     LYS A  45    CE   NZ                                             
REMARK 470     LYS A 133    CE   NZ                                             
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   OE2  GLU A   214     O    HOH A   544              2.03            
REMARK 500   ND1  HIS A    64     O3   GOL A   303              2.08            
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    ARG A  27       55.72   -142.04                                   
REMARK 500    ALA A  65     -167.72   -162.60                                   
REMARK 500    LYS A 111       -1.71     72.43                                   
REMARK 500    PHE A 176       64.93   -151.77                                   
REMARK 500    ASN A 244       48.00    -94.99                                   
REMARK 500    LYS A 252     -136.56     52.96                                   
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 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MB6 A 302   O2                                                     
REMARK 620 2 HIS A  94   NE2 111.1                                              
REMARK 620 3 HIS A  96   NE2 113.8 104.4                                        
REMARK 620 4 HIS A 119   ND1 114.5 113.1  99.0                                  
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 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MB6 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 304                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4KUW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KUY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KV0   RELATED DB: PDB                                   
DBREF  4KUV A    5   261  UNP    P00918   CAH2_HUMAN       5    260             
SEQRES   1 A  256  TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU HIS TRP HIS          
SEQRES   2 A  256  LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG GLN SER PRO          
SEQRES   3 A  256  VAL ASP ILE ASP THR HIS THR ALA LYS TYR ASP PRO SER          
SEQRES   4 A  256  LEU LYS PRO LEU SER VAL SER TYR ASP GLN ALA THR SER          
SEQRES   5 A  256  LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE ASN VAL GLU          
SEQRES   6 A  256  PHE ASP ASP SER GLN ASP LYS ALA VAL LEU LYS GLY GLY          
SEQRES   7 A  256  PRO LEU ASP GLY THR TYR ARG LEU ILE GLN PHE HIS PHE          
SEQRES   8 A  256  HIS TRP GLY SER LEU ASP GLY GLN GLY SER GLU HIS THR          
SEQRES   9 A  256  VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU HIS LEU VAL          
SEQRES  10 A  256  HIS TRP ASN THR LYS TYR GLY ASP PHE GLY LYS ALA VAL          
SEQRES  11 A  256  GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY ILE PHE LEU          
SEQRES  12 A  256  LYS VAL GLY SER ALA LYS PRO GLY LEU GLN LYS VAL VAL          
SEQRES  13 A  256  ASP VAL LEU ASP SER ILE LYS THR LYS GLY LYS SER ALA          
SEQRES  14 A  256  ASP PHE THR ASN PHE ASP PRO ARG GLY LEU LEU PRO GLU          
SEQRES  15 A  256  SER LEU ASP TYR TRP THR TYR PRO GLY SER LEU THR THR          
SEQRES  16 A  256  PRO PRO LEU LEU GLU CYS VAL THR TRP ILE VAL LEU LYS          
SEQRES  17 A  256  GLU PRO ILE SER VAL SER SER GLU GLN VAL LEU LYS PHE          
SEQRES  18 A  256  ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU PRO GLU GLU          
SEQRES  19 A  256  LEU MET VAL ASP ASN TRP ARG PRO ALA GLN PRO LEU LYS          
SEQRES  20 A  256  ASN ARG GLN ILE LYS ALA SER PHE LYS                          
HET     ZN  A 301       1                                                       
HET    MB6  A 302      24                                                       
HET    GOL  A 303       6                                                       
HET    BME  A 304       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     MB6 5-({[(4-CHLOROPHENYL)SULFONYL]CARBAMOYL}AMINO)PYRIDINE-          
HETNAM   2 MB6  2-SULFONAMIDE                                                   
HETNAM     GOL GLYCEROL                                                         
HETNAM     BME BETA-MERCAPTOETHANOL                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  MB6    C12 H11 CL N4 O5 S2                                          
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   5  BME    C2 H6 O S                                                    
FORMUL   6  HOH   *261(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   B10 LYS A  39  TYR A  40  0                                        
SHEET    2   B10 LYS A 257  ALA A 258  1  O  ALA A 258   N  LYS A  39           
SHEET    3   B10 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257           
SHEET    4   B10 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196           
SHEET    5   B10 LEU A 141  VAL A 150  1  N  GLY A 145   O  ILE A 210           
SHEET    6   B10 ALA A 116  ASN A 124 -1  N  LEU A 118   O  ILE A 146           
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  HIS A  94   O  HIS A 119           
SHEET    8   B10 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93           
SHEET    9   B10 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69           
SHEET   10   B10 SER A 173  ASP A 175 -1  O  ALA A 174   N  ILE A  59           
SHEET    1   C 6 LEU A  47  SER A  50  0                                        
SHEET    2   C 6 VAL A  78  GLY A  81 -1  O  VAL A  78   N  SER A  50           
SHEET    3   C 6 TYR A  88  TRP A  97 -1  O  TYR A  88   N  LEU A  79           
SHEET    4   C 6 ALA A 116  ASN A 124 -1  O  HIS A 119   N  HIS A  94           
SHEET    5   C 6 LEU A 141  VAL A 150 -1  O  ILE A 146   N  LEU A 118           
SHEET    6   C 6 ILE A 216  VAL A 218  1  O  ILE A 216   N  PHE A 147           
LINK        ZN    ZN A 301                 O2  MB6 A 302     1555   1555  2.00  
LINK         NE2 HIS A  94                ZN    ZN A 301     1555   1555  2.05  
LINK         NE2 HIS A  96                ZN    ZN A 301     1555   1555  2.05  
LINK         ND1 HIS A 119                ZN    ZN A 301     1555   1555  2.06  
CISPEP   1 SER A   29    PRO A   30          0        -2.52                     
CISPEP   2 PRO A  201    PRO A  202          0        13.16                     
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  MB6 A 302                    
SITE     1 AC2 14 HIS A  94  HIS A  96  HIS A 119  VAL A 135                    
SITE     2 AC2 14 LEU A 198  THR A 199  THR A 200  TRP A 209                    
SITE     3 AC2 14  ZN A 301  GOL A 303  HOH A 464  HOH A 481                    
SITE     4 AC2 14 HOH A 511  HOH A 594                                          
SITE     1 AC3 10 ASN A  62  HIS A  64  ALA A  65  ASN A  67                    
SITE     2 AC3 10 GLN A  92  HIS A  94  MB6 A 302  HOH A 424                    
SITE     3 AC3 10 HOH A 481  HOH A 580                                          
SITE     1 AC4  7 TYR A   7  ASP A 243  TRP A 245  PRO A 247                    
SITE     2 AC4  7 HOH A 492  HOH A 583  HOH A 653                               
CRYST1   42.323   41.359   72.194  90.00 104.30  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      0.023628  0.000000  0.006023        0.00000                         
SCALE2      0.000000  0.024179  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014295        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system