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Database: PDB
Entry: 6G9U
LinkDB: 6G9U
Original site: 6G9U 
HEADER    LYASE                                   11-APR-18   6G9U              
TITLE     THREE DIMENSIONAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE IX IN COMPLEX 
TITLE    2 WITH SULFONAMIDE                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 9;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE IX,CARBONIC ANHYDRASE IX,CAIX,MEMBRANE
COMPND   5 ANTIGEN MN,P54/58N,RENAL CELL CARCINOMA-ASSOCIATED ANTIGEN G250,RCC- 
COMPND   6 ASSOCIATED ANTIGEN G250,PMW1;                                        
COMPND   7 EC: 4.2.1.1;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 OTHER_DETAILS: A, B, C, D CHAINS ARE IDENTICAL.                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CA9, G250, MN;                                                 
SOURCE   6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922                                        
KEYWDS    LYASE                                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LEITANS,K.TARS                                                      
REVDAT   1   04-JUL-18 6G9U    0                                                
JRNL        AUTH   J.KAZOKAITE,R.NIEMANS,V.DUDUTIENE,H.M.BECKER,J.LEITANS,      
JRNL        AUTH 2 A.ZUBRIENE,L.BARANAUSKIENE,G.GONDI,R.ZEIDLER,J.MATULIENE,    
JRNL        AUTH 3 K.TARS,A.YAROMINA,P.LAMBIN,L.J.DUBOIS,D.MATULIS              
JRNL        TITL   NOVEL FLUORINATED CARBONIC ANHYDRASE IX INHIBITORS REDUCE    
JRNL        TITL 2 HYPOXIA-INDUCED ACIDIFICATION AND CLONOGENIC SURVIVAL OF     
JRNL        TITL 3 CANCER CELLS.                                                
JRNL        REF    ONCOTARGET                    V.   9 26800 2018              
JRNL        REFN                   ESSN 1949-2553                               
JRNL        PMID   29928486                                                     
JRNL        DOI    10.18632/ONCOTARGET.25508                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 76.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 139211                         
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) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7170                            
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) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.80                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9657                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.04                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2780                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 513                          
REMARK   3   BIN FREE R VALUE                    : 0.2690                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7388                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 140                                     
REMARK   3   SOLVENT ATOMS            : 879                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.28                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.43000                                              
REMARK   3    B22 (A**2) : 0.43000                                              
REMARK   3    B33 (A**2) : -1.40000                                             
REMARK   3    B12 (A**2) : 0.22000                                              
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): 0.085         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.083         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.065         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.144         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.962                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7733 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  7064 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10533 ; 1.401 ; 1.994       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 16381 ; 0.916 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   946 ; 5.708 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   344 ;35.989 ;23.256       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1143 ;11.795 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    64 ;15.385 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1150 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8556 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1560 ; 0.004 ; 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):  3832 ; 1.879 ; 3.058       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3831 ; 1.877 ; 3.058       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4755 ; 2.938 ; 4.569       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  4756 ; 2.938 ; 4.569       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3901 ; 2.450 ; 3.352       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3902 ; 2.450 ; 3.352       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  5776 ; 3.961 ; 4.924       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  8453 ; 6.083 ;37.774       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  8181 ; 5.887 ;36.720       
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 : NULL                                                 
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 6G9U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-APR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009635.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JAN-18                          
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               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91840                            
REMARK 200  MONOCHROMATOR                  : KMC-1                              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 146413                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 76.190                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.05500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
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: NULL                                                  
REMARK 200 STARTING MODEL: 5FL4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M DI-AMMONIUM HYDROGEN PHOSPHATE,    
REMARK 280  0.1 M SODIUM ACETATE PH 4.5, PROTEIN 10 MG/ML, 5-10 MM INHIBITOR    
REMARK 280  (STOCK SOLUTION WAS 100 MM INHIBITOR DISSOLVED IN 100% DIMETHYL     
REMARK 280  SULFOXIDE), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       76.19000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       43.98832            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       57.28000            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       76.19000            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       43.98832            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       57.28000            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       76.19000            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       43.98832            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       57.28000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       87.97663            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      114.56000            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       87.97663            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      114.56000            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       87.97663            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      114.56000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     GLY A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     TRP A     8                                                      
REMARK 465     ARG A     9                                                      
REMARK 465     TYR A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     ASP A    13                                                      
REMARK 465     PRO A    14                                                      
REMARK 465     PRO A    15                                                      
REMARK 465     TRP A    16                                                      
REMARK 465     PRO A    17                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     GLN B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     TRP B     8                                                      
REMARK 465     ARG B     9                                                      
REMARK 465     TYR B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     ASP B    13                                                      
REMARK 465     PRO B    14                                                      
REMARK 465     PRO B    15                                                      
REMARK 465     TRP B    16                                                      
REMARK 465     PRO B    17                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     PRO C     3                                                      
REMARK 465     ASP C     4                                                      
REMARK 465     GLN C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     HIS C     7                                                      
REMARK 465     TRP C     8                                                      
REMARK 465     ARG C     9                                                      
REMARK 465     TYR C    10                                                      
REMARK 465     GLY C    11                                                      
REMARK 465     GLY C    12                                                      
REMARK 465     ASP C    13                                                      
REMARK 465     PRO C    14                                                      
REMARK 465     PRO C    15                                                      
REMARK 465     TRP C    16                                                      
REMARK 465     PRO C    17                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     PRO D     3                                                      
REMARK 465     ASP D     4                                                      
REMARK 465     GLN D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     HIS D     7                                                      
REMARK 465     TRP D     8                                                      
REMARK 465     ARG D     9                                                      
REMARK 465     TYR D    10                                                      
REMARK 465     GLY D    11                                                      
REMARK 465     GLY D    12                                                      
REMARK 465     ASP D    13                                                      
REMARK 465     PRO D    14                                                      
REMARK 465     PRO D    15                                                      
REMARK 465     TRP D    16                                                      
REMARK 465     PRO D    17                                                      
REMARK 465     ARG D    18                                                      
REMARK 465     VAL D    19                                                      
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     ARG A  18    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 238    CG   OD1  OD2                                       
REMARK 470     ARG B  18    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 238    CG   OD1  OD2                                       
REMARK 470     ARG C  18    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 238    CG   OD1  OD2                                       
REMARK 470     LYS D 221    CG   CD   CE   NZ                                   
REMARK 470     ASP D 238    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PRO A  72   C     GLY A  76   N       0.242                       
REMARK 500    GLY A  82   C     PRO A  84   N       0.243                       
REMARK 500    THR A 125   C     ALA A 127   N       0.281                       
REMARK 500    THR D 125   C     ALA D 127   N       0.265                       
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  86       74.50   -116.48                                   
REMARK 500    ASP A 238       54.88   -106.73                                   
REMARK 500    ASN A 244       57.20    -91.03                                   
REMARK 500    ARG B  86       78.35   -116.70                                   
REMARK 500    ASN B 244       55.91    -90.13                                   
REMARK 500    ARG C  86       75.27   -119.13                                   
REMARK 500    ASP C 238       54.29   -115.87                                   
REMARK 500    ASN C 244       55.51    -94.18                                   
REMARK 500    ARG D  86       79.88   -110.48                                   
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 HIS A  94   NE2                                                    
REMARK 620 2 HIS A  96   NE2 106.4                                              
REMARK 620 3 HIS A 119   ND1 112.3  99.1                                        
REMARK 620 4 ETK A 302   N1  111.9 116.7 109.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  94   NE2                                                    
REMARK 620 2 HIS B  96   NE2 100.9                                              
REMARK 620 3 HIS B 119   ND1 112.8  97.4                                        
REMARK 620 4 ETK B 302   N1  114.9 115.7 113.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  94   NE2                                                    
REMARK 620 2 HIS C  96   NE2 103.2                                              
REMARK 620 3 HIS C 119   ND1 110.8 100.9                                        
REMARK 620 4 ETK C 302   N1  108.5 116.5 116.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  94   NE2                                                    
REMARK 620 2 HIS D  96   NE2 104.7                                              
REMARK 620 3 HIS D 119   ND1 112.9  97.5                                        
REMARK 620 4 ETK D 302   N1  114.8 116.0 109.8                                  
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 ETK A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ETK B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ETK C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ETK D 302                 
DBREF  6G9U A    4   261  UNP    Q16790   CAH9_HUMAN     137    391             
DBREF  6G9U B    4   261  UNP    Q16790   CAH9_HUMAN     137    391             
DBREF  6G9U C    4   261  UNP    Q16790   CAH9_HUMAN     137    391             
DBREF  6G9U D    4   261  UNP    Q16790   CAH9_HUMAN     137    391             
SEQADV 6G9U GLY A    2  UNP  Q16790              EXPRESSION TAG                 
SEQADV 6G9U PRO A    3  UNP  Q16790              EXPRESSION TAG                 
SEQADV 6G9U SER A   41  UNP  Q16790    CYS   174 ENGINEERED MUTATION            
SEQADV 6G9U GLY B    2  UNP  Q16790              EXPRESSION TAG                 
SEQADV 6G9U PRO B    3  UNP  Q16790              EXPRESSION TAG                 
SEQADV 6G9U SER B   41  UNP  Q16790    CYS   174 ENGINEERED MUTATION            
SEQADV 6G9U GLY C    2  UNP  Q16790              EXPRESSION TAG                 
SEQADV 6G9U PRO C    3  UNP  Q16790              EXPRESSION TAG                 
SEQADV 6G9U SER C   41  UNP  Q16790    CYS   174 ENGINEERED MUTATION            
SEQADV 6G9U GLY D    2  UNP  Q16790              EXPRESSION TAG                 
SEQADV 6G9U PRO D    3  UNP  Q16790              EXPRESSION TAG                 
SEQADV 6G9U SER D   41  UNP  Q16790    CYS   174 ENGINEERED MUTATION            
SEQRES   1 A  257  GLY PRO ASP GLN SER HIS TRP ARG TYR GLY GLY ASP PRO          
SEQRES   2 A  257  PRO TRP PRO ARG VAL SER PRO ALA CYS ALA GLY ARG PHE          
SEQRES   3 A  257  GLN SER PRO VAL ASP ILE ARG PRO GLN LEU ALA ALA PHE          
SEQRES   4 A  257  SER PRO ALA LEU ARG PRO LEU GLU LEU LEU GLY PHE GLN          
SEQRES   5 A  257  LEU PRO PRO LEU PRO GLU LEU ARG LEU ARG ASN ASN GLY          
SEQRES   6 A  257  HIS SER VAL GLN LEU THR LEU PRO PRO GLY LEU GLU MET          
SEQRES   7 A  257  ALA LEU GLY PRO GLY ARG GLU TYR ARG ALA LEU GLN LEU          
SEQRES   8 A  257  HIS LEU HIS TRP GLY ALA ALA GLY ARG PRO GLY SER GLU          
SEQRES   9 A  257  HIS THR VAL GLU GLY HIS ARG PHE PRO ALA GLU ILE HIS          
SEQRES  10 A  257  VAL VAL HIS LEU SER THR ALA PHE ALA ARG VAL ASP GLU          
SEQRES  11 A  257  ALA LEU GLY ARG PRO GLY GLY LEU ALA VAL LEU ALA ALA          
SEQRES  12 A  257  PHE LEU GLU GLU GLY PRO GLU GLU ASN SER ALA TYR GLU          
SEQRES  13 A  257  GLN LEU LEU SER ARG LEU GLU GLU ILE ALA GLU GLU GLY          
SEQRES  14 A  257  SER GLU THR GLN VAL PRO GLY LEU ASP ILE SER ALA LEU          
SEQRES  15 A  257  LEU PRO SER ASP PHE SER ARG TYR PHE GLN TYR GLU GLY          
SEQRES  16 A  257  SER LEU THR THR PRO PRO CYS ALA GLN GLY VAL ILE TRP          
SEQRES  17 A  257  THR VAL PHE ASN GLN THR VAL MET LEU SER ALA LYS GLN          
SEQRES  18 A  257  LEU HIS THR LEU SER ASP THR LEU TRP GLY PRO GLY ASP          
SEQRES  19 A  257  SER ARG LEU GLN LEU ASN PHE ARG ALA THR GLN PRO LEU          
SEQRES  20 A  257  ASN GLY ARG VAL ILE GLU ALA SER PHE PRO                      
SEQRES   1 B  257  GLY PRO ASP GLN SER HIS TRP ARG TYR GLY GLY ASP PRO          
SEQRES   2 B  257  PRO TRP PRO ARG VAL SER PRO ALA CYS ALA GLY ARG PHE          
SEQRES   3 B  257  GLN SER PRO VAL ASP ILE ARG PRO GLN LEU ALA ALA PHE          
SEQRES   4 B  257  SER PRO ALA LEU ARG PRO LEU GLU LEU LEU GLY PHE GLN          
SEQRES   5 B  257  LEU PRO PRO LEU PRO GLU LEU ARG LEU ARG ASN ASN GLY          
SEQRES   6 B  257  HIS SER VAL GLN LEU THR LEU PRO PRO GLY LEU GLU MET          
SEQRES   7 B  257  ALA LEU GLY PRO GLY ARG GLU TYR ARG ALA LEU GLN LEU          
SEQRES   8 B  257  HIS LEU HIS TRP GLY ALA ALA GLY ARG PRO GLY SER GLU          
SEQRES   9 B  257  HIS THR VAL GLU GLY HIS ARG PHE PRO ALA GLU ILE HIS          
SEQRES  10 B  257  VAL VAL HIS LEU SER THR ALA PHE ALA ARG VAL ASP GLU          
SEQRES  11 B  257  ALA LEU GLY ARG PRO GLY GLY LEU ALA VAL LEU ALA ALA          
SEQRES  12 B  257  PHE LEU GLU GLU GLY PRO GLU GLU ASN SER ALA TYR GLU          
SEQRES  13 B  257  GLN LEU LEU SER ARG LEU GLU GLU ILE ALA GLU GLU GLY          
SEQRES  14 B  257  SER GLU THR GLN VAL PRO GLY LEU ASP ILE SER ALA LEU          
SEQRES  15 B  257  LEU PRO SER ASP PHE SER ARG TYR PHE GLN TYR GLU GLY          
SEQRES  16 B  257  SER LEU THR THR PRO PRO CYS ALA GLN GLY VAL ILE TRP          
SEQRES  17 B  257  THR VAL PHE ASN GLN THR VAL MET LEU SER ALA LYS GLN          
SEQRES  18 B  257  LEU HIS THR LEU SER ASP THR LEU TRP GLY PRO GLY ASP          
SEQRES  19 B  257  SER ARG LEU GLN LEU ASN PHE ARG ALA THR GLN PRO LEU          
SEQRES  20 B  257  ASN GLY ARG VAL ILE GLU ALA SER PHE PRO                      
SEQRES   1 C  257  GLY PRO ASP GLN SER HIS TRP ARG TYR GLY GLY ASP PRO          
SEQRES   2 C  257  PRO TRP PRO ARG VAL SER PRO ALA CYS ALA GLY ARG PHE          
SEQRES   3 C  257  GLN SER PRO VAL ASP ILE ARG PRO GLN LEU ALA ALA PHE          
SEQRES   4 C  257  SER PRO ALA LEU ARG PRO LEU GLU LEU LEU GLY PHE GLN          
SEQRES   5 C  257  LEU PRO PRO LEU PRO GLU LEU ARG LEU ARG ASN ASN GLY          
SEQRES   6 C  257  HIS SER VAL GLN LEU THR LEU PRO PRO GLY LEU GLU MET          
SEQRES   7 C  257  ALA LEU GLY PRO GLY ARG GLU TYR ARG ALA LEU GLN LEU          
SEQRES   8 C  257  HIS LEU HIS TRP GLY ALA ALA GLY ARG PRO GLY SER GLU          
SEQRES   9 C  257  HIS THR VAL GLU GLY HIS ARG PHE PRO ALA GLU ILE HIS          
SEQRES  10 C  257  VAL VAL HIS LEU SER THR ALA PHE ALA ARG VAL ASP GLU          
SEQRES  11 C  257  ALA LEU GLY ARG PRO GLY GLY LEU ALA VAL LEU ALA ALA          
SEQRES  12 C  257  PHE LEU GLU GLU GLY PRO GLU GLU ASN SER ALA TYR GLU          
SEQRES  13 C  257  GLN LEU LEU SER ARG LEU GLU GLU ILE ALA GLU GLU GLY          
SEQRES  14 C  257  SER GLU THR GLN VAL PRO GLY LEU ASP ILE SER ALA LEU          
SEQRES  15 C  257  LEU PRO SER ASP PHE SER ARG TYR PHE GLN TYR GLU GLY          
SEQRES  16 C  257  SER LEU THR THR PRO PRO CYS ALA GLN GLY VAL ILE TRP          
SEQRES  17 C  257  THR VAL PHE ASN GLN THR VAL MET LEU SER ALA LYS GLN          
SEQRES  18 C  257  LEU HIS THR LEU SER ASP THR LEU TRP GLY PRO GLY ASP          
SEQRES  19 C  257  SER ARG LEU GLN LEU ASN PHE ARG ALA THR GLN PRO LEU          
SEQRES  20 C  257  ASN GLY ARG VAL ILE GLU ALA SER PHE PRO                      
SEQRES   1 D  257  GLY PRO ASP GLN SER HIS TRP ARG TYR GLY GLY ASP PRO          
SEQRES   2 D  257  PRO TRP PRO ARG VAL SER PRO ALA CYS ALA GLY ARG PHE          
SEQRES   3 D  257  GLN SER PRO VAL ASP ILE ARG PRO GLN LEU ALA ALA PHE          
SEQRES   4 D  257  SER PRO ALA LEU ARG PRO LEU GLU LEU LEU GLY PHE GLN          
SEQRES   5 D  257  LEU PRO PRO LEU PRO GLU LEU ARG LEU ARG ASN ASN GLY          
SEQRES   6 D  257  HIS SER VAL GLN LEU THR LEU PRO PRO GLY LEU GLU MET          
SEQRES   7 D  257  ALA LEU GLY PRO GLY ARG GLU TYR ARG ALA LEU GLN LEU          
SEQRES   8 D  257  HIS LEU HIS TRP GLY ALA ALA GLY ARG PRO GLY SER GLU          
SEQRES   9 D  257  HIS THR VAL GLU GLY HIS ARG PHE PRO ALA GLU ILE HIS          
SEQRES  10 D  257  VAL VAL HIS LEU SER THR ALA PHE ALA ARG VAL ASP GLU          
SEQRES  11 D  257  ALA LEU GLY ARG PRO GLY GLY LEU ALA VAL LEU ALA ALA          
SEQRES  12 D  257  PHE LEU GLU GLU GLY PRO GLU GLU ASN SER ALA TYR GLU          
SEQRES  13 D  257  GLN LEU LEU SER ARG LEU GLU GLU ILE ALA GLU GLU GLY          
SEQRES  14 D  257  SER GLU THR GLN VAL PRO GLY LEU ASP ILE SER ALA LEU          
SEQRES  15 D  257  LEU PRO SER ASP PHE SER ARG TYR PHE GLN TYR GLU GLY          
SEQRES  16 D  257  SER LEU THR THR PRO PRO CYS ALA GLN GLY VAL ILE TRP          
SEQRES  17 D  257  THR VAL PHE ASN GLN THR VAL MET LEU SER ALA LYS GLN          
SEQRES  18 D  257  LEU HIS THR LEU SER ASP THR LEU TRP GLY PRO GLY ASP          
SEQRES  19 D  257  SER ARG LEU GLN LEU ASN PHE ARG ALA THR GLN PRO LEU          
SEQRES  20 D  257  ASN GLY ARG VAL ILE GLU ALA SER PHE PRO                      
HET     ZN  A 301       1                                                       
HET    ETK  A 302      34                                                       
HET     ZN  B 301       1                                                       
HET    ETK  B 302      34                                                       
HET     ZN  C 301       1                                                       
HET    ETK  C 302      34                                                       
HET     ZN  D 301       1                                                       
HET    ETK  D 302      34                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     ETK 4-[2-[3-(CYCLOOCTYLAMINO)-2,5,6-TRIS(FLUORANYL)-4-               
HETNAM   2 ETK  SULFAMOYL-PHENYL]SULFANYLETHYL]BENZOIC ACID                     
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   6  ETK    4(C23 H27 F3 N2 O4 S2)                                       
FORMUL  13  HOH   *879(H2 O)                                                    
HELIX    1 AA1 SER A   20  GLY A   25  5                                   6    
HELIX    2 AA2 ARG A   34  ALA A   38  5                                   5    
HELIX    3 AA3 ARG A  130  LEU A  135  1                                   6    
HELIX    4 AA4 ASN A  154  SER A  162  1                                   9    
HELIX    5 AA5 ARG A  163  ALA A  168  5                                   6    
HELIX    6 AA6 ASP A  180  LEU A  185  5                                   6    
HELIX    7 AA7 SER A  219  THR A  228  1                                  11    
HELIX    8 AA8 SER B   20  GLY B   25  5                                   6    
HELIX    9 AA9 ARG B   34  ALA B   38  5                                   5    
HELIX   10 AB1 ARG B  130  LEU B  135  1                                   6    
HELIX   11 AB2 ASN B  154  SER B  162  1                                   9    
HELIX   12 AB3 ARG B  163  ALA B  168  5                                   6    
HELIX   13 AB4 ASP B  180  LEU B  185  5                                   6    
HELIX   14 AB5 SER B  219  THR B  228  1                                  11    
HELIX   15 AB6 SER C   20  GLY C   25  5                                   6    
HELIX   16 AB7 ARG C   34  ALA C   38  5                                   5    
HELIX   17 AB8 ARG C  130  LEU C  135  1                                   6    
HELIX   18 AB9 ASN C  154  SER C  162  1                                   9    
HELIX   19 AC1 ARG C  163  ALA C  168  5                                   6    
HELIX   20 AC2 ASP C  180  LEU C  185  5                                   6    
HELIX   21 AC3 SER C  219  THR C  228  1                                  11    
HELIX   22 AC4 SER D   20  GLY D   25  5                                   6    
HELIX   23 AC5 ARG D   34  ALA D   38  5                                   5    
HELIX   24 AC6 ARG D  130  LEU D  135  1                                   6    
HELIX   25 AC7 ASN D  154  SER D  162  1                                   9    
HELIX   26 AC8 ARG D  163  ALA D  168  5                                   6    
HELIX   27 AC9 ASP D  180  LEU D  185  5                                   6    
HELIX   28 AD1 SER D  219  THR D  228  1                                  11    
SHEET    1 AA1 2 ASP A  32  ILE A  33  0                                        
SHEET    2 AA1 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33           
SHEET    1 AA210 ALA A  39  PHE A  40  0                                        
SHEET    2 AA210 GLU A 257  ALA A 258  1  O  ALA A 258   N  ALA A  39           
SHEET    3 AA210 TYR A 191  SER A 197 -1  N  GLN A 193   O  GLU A 257           
SHEET    4 AA210 GLN A 205  PHE A 212 -1  O  VAL A 207   N  GLY A 196           
SHEET    5 AA210 LEU A 141  GLU A 150  1  N  ALA A 145   O  THR A 210           
SHEET    6 AA210 ALA A 116  SER A 124 -1  N  ALA A 116   O  LEU A 148           
SHEET    7 AA210 ARG A  86  TRP A  97 -1  N  LEU A  91   O  VAL A 121           
SHEET    8 AA210 VAL A  66  THR A  69 -1  N  LEU A  68   O  LEU A  93           
SHEET    9 AA210 LEU A  57  ASN A  61 -1  N  ARG A  60   O  GLN A  67           
SHEET   10 AA210 GLU A 173  VAL A 176 -1  O  VAL A 176   N  LEU A  57           
SHEET    1 AA3 6 GLU A  48  LEU A  50  0                                        
SHEET    2 AA3 6 GLU A  78  GLY A  82 -1  O  GLU A  78   N  LEU A  50           
SHEET    3 AA3 6 ARG A  86  TRP A  97 -1  O  TYR A  88   N  MET A  79           
SHEET    4 AA3 6 ALA A 116  SER A 124 -1  O  VAL A 121   N  LEU A  91           
SHEET    5 AA3 6 LEU A 141  GLU A 150 -1  O  LEU A 148   N  ALA A 116           
SHEET    6 AA3 6 VAL A 216  LEU A 218  1  O  LEU A 218   N  GLU A 149           
SHEET    1 AA4 2 ASP B  32  ILE B  33  0                                        
SHEET    2 AA4 2 THR B 108  VAL B 109  1  O  THR B 108   N  ILE B  33           
SHEET    1 AA510 ALA B  39  PHE B  40  0                                        
SHEET    2 AA510 GLU B 257  ALA B 258  1  O  ALA B 258   N  ALA B  39           
SHEET    3 AA510 TYR B 191  SER B 197 -1  N  GLN B 193   O  GLU B 257           
SHEET    4 AA510 GLN B 205  PHE B 212 -1  O  VAL B 207   N  GLY B 196           
SHEET    5 AA510 LEU B 141  GLU B 150  1  N  ALA B 145   O  THR B 210           
SHEET    6 AA510 ALA B 116  SER B 124 -1  N  ALA B 116   O  LEU B 148           
SHEET    7 AA510 ARG B  86  TRP B  97 -1  N  LEU B  91   O  VAL B 121           
SHEET    8 AA510 VAL B  66  THR B  69 -1  N  LEU B  68   O  LEU B  93           
SHEET    9 AA510 LEU B  57  ASN B  61 -1  N  ARG B  60   O  GLN B  67           
SHEET   10 AA510 GLU B 173  VAL B 176 -1  O  VAL B 176   N  LEU B  57           
SHEET    1 AA6 6 GLU B  48  LEU B  50  0                                        
SHEET    2 AA6 6 GLU B  78  GLY B  82 -1  O  GLU B  78   N  LEU B  50           
SHEET    3 AA6 6 ARG B  86  TRP B  97 -1  O  TYR B  88   N  MET B  79           
SHEET    4 AA6 6 ALA B 116  SER B 124 -1  O  VAL B 121   N  LEU B  91           
SHEET    5 AA6 6 LEU B 141  GLU B 150 -1  O  LEU B 148   N  ALA B 116           
SHEET    6 AA6 6 VAL B 216  LEU B 218  1  O  VAL B 216   N  GLU B 149           
SHEET    1 AA7 2 ASP C  32  ILE C  33  0                                        
SHEET    2 AA7 2 THR C 108  VAL C 109  1  O  THR C 108   N  ILE C  33           
SHEET    1 AA810 ALA C  39  PHE C  40  0                                        
SHEET    2 AA810 GLU C 257  ALA C 258  1  O  ALA C 258   N  ALA C  39           
SHEET    3 AA810 TYR C 191  SER C 197 -1  N  GLN C 193   O  GLU C 257           
SHEET    4 AA810 GLN C 205  PHE C 212 -1  O  VAL C 207   N  GLY C 196           
SHEET    5 AA810 LEU C 141  GLU C 150  1  N  ALA C 145   O  THR C 210           
SHEET    6 AA810 ALA C 116  SER C 124 -1  N  HIS C 122   O  ALA C 142           
SHEET    7 AA810 ARG C  86  TRP C  97 -1  N  LEU C  91   O  VAL C 121           
SHEET    8 AA810 VAL C  66  THR C  69 -1  N  LEU C  68   O  LEU C  93           
SHEET    9 AA810 LEU C  57  ASN C  61 -1  N  ARG C  60   O  GLN C  67           
SHEET   10 AA810 GLU C 173  VAL C 176 -1  O  THR C 174   N  LEU C  59           
SHEET    1 AA9 6 GLU C  48  LEU C  50  0                                        
SHEET    2 AA9 6 GLU C  78  GLY C  82 -1  O  GLU C  78   N  LEU C  50           
SHEET    3 AA9 6 ARG C  86  TRP C  97 -1  O  TYR C  88   N  MET C  79           
SHEET    4 AA9 6 ALA C 116  SER C 124 -1  O  VAL C 121   N  LEU C  91           
SHEET    5 AA9 6 LEU C 141  GLU C 150 -1  O  ALA C 142   N  HIS C 122           
SHEET    6 AA9 6 VAL C 216  LEU C 218  1  O  VAL C 216   N  GLU C 149           
SHEET    1 AB1 2 ASP D  32  ILE D  33  0                                        
SHEET    2 AB1 2 THR D 108  VAL D 109  1  O  THR D 108   N  ILE D  33           
SHEET    1 AB210 ALA D  39  PHE D  40  0                                        
SHEET    2 AB210 GLU D 257  ALA D 258  1  O  ALA D 258   N  ALA D  39           
SHEET    3 AB210 TYR D 191  SER D 197 -1  N  GLN D 193   O  GLU D 257           
SHEET    4 AB210 GLN D 205  PHE D 212 -1  O  VAL D 207   N  GLY D 196           
SHEET    5 AB210 LEU D 141  GLU D 150  1  N  ALA D 145   O  THR D 210           
SHEET    6 AB210 ALA D 116  SER D 124 -1  N  HIS D 122   O  ALA D 142           
SHEET    7 AB210 ARG D  86  TRP D  97 -1  N  LEU D  91   O  VAL D 121           
SHEET    8 AB210 VAL D  66  THR D  69 -1  N  LEU D  68   O  LEU D  93           
SHEET    9 AB210 LEU D  57  ASN D  61 -1  N  ARG D  60   O  GLN D  67           
SHEET   10 AB210 GLU D 173  VAL D 176 -1  O  THR D 174   N  LEU D  59           
SHEET    1 AB3 6 GLU D  48  LEU D  50  0                                        
SHEET    2 AB3 6 GLU D  78  GLY D  82 -1  O  GLU D  78   N  LEU D  50           
SHEET    3 AB3 6 ARG D  86  TRP D  97 -1  O  TYR D  88   N  MET D  79           
SHEET    4 AB3 6 ALA D 116  SER D 124 -1  O  VAL D 121   N  LEU D  91           
SHEET    5 AB3 6 LEU D 141  GLU D 150 -1  O  ALA D 142   N  HIS D 122           
SHEET    6 AB3 6 VAL D 216  LEU D 218  1  O  VAL D 216   N  GLU D 149           
SSBOND   1 CYS A   23    CYS A  203                          1555   1555  2.07  
SSBOND   2 CYS B   23    CYS B  203                          1555   1555  2.08  
SSBOND   3 CYS C   23    CYS C  203                          1555   1555  2.07  
SSBOND   4 CYS D   23    CYS D  203                          1555   1555  2.10  
LINK         NE2 HIS A  94                ZN    ZN A 301     1555   1555  2.05  
LINK         NE2 HIS A  96                ZN    ZN A 301     1555   1555  2.02  
LINK         ND1 HIS A 119                ZN    ZN A 301     1555   1555  2.10  
LINK         NE2 HIS B  94                ZN    ZN B 301     1555   1555  2.02  
LINK         NE2 HIS B  96                ZN    ZN B 301     1555   1555  2.08  
LINK         ND1 HIS B 119                ZN    ZN B 301     1555   1555  2.09  
LINK         NE2 HIS C  94                ZN    ZN C 301     1555   1555  2.11  
LINK         NE2 HIS C  96                ZN    ZN C 301     1555   1555  2.12  
LINK         ND1 HIS C 119                ZN    ZN C 301     1555   1555  1.94  
LINK         NE2 HIS D  94                ZN    ZN D 301     1555   1555  1.88  
LINK         NE2 HIS D  96                ZN    ZN D 301     1555   1555  2.12  
LINK         ND1 HIS D 119                ZN    ZN D 301     1555   1555  2.04  
LINK        ZN    ZN A 301                 N1  ETK A 302     1555   1555  1.97  
LINK        ZN    ZN B 301                 N1  ETK B 302     1555   1555  1.97  
LINK        ZN    ZN C 301                 N1  ETK C 302     1555   1555  1.91  
LINK        ZN    ZN D 301                 N1  ETK D 302     1555   1555  2.09  
CISPEP   1 SER A   29    PRO A   30          0        -4.39                     
CISPEP   2 LEU A   54B   PRO A   55          0         1.03                     
CISPEP   3 PRO A  201    PRO A  202          0        13.77                     
CISPEP   4 SER B   29    PRO B   30          0        -1.87                     
CISPEP   5 LEU B   54B   PRO B   55          0         1.52                     
CISPEP   6 PRO B  201    PRO B  202          0        15.32                     
CISPEP   7 SER C   29    PRO C   30          0        -2.75                     
CISPEP   8 LEU C   54B   PRO C   55          0         0.04                     
CISPEP   9 PRO C  201    PRO C  202          0        12.63                     
CISPEP  10 SER D   29    PRO D   30          0        -1.45                     
CISPEP  11 LEU D   54B   PRO D   55          0         3.32                     
CISPEP  12 PRO D  201    PRO D  202          0        17.16                     
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  ETK A 302                    
SITE     1 AC2 13 ARG A  60  ASN A  62  HIS A  64  GLN A  67                    
SITE     2 AC2 13 GLN A  92  HIS A  94  HIS A  96  HIS A 119                    
SITE     3 AC2 13 LEU A 198  THR A 199  THR A 200   ZN A 301                    
SITE     4 AC2 13 HOH A 405                                                     
SITE     1 AC3  4 HIS B  94  HIS B  96  HIS B 119  ETK B 302                    
SITE     1 AC4 14 ARG B  60  ASN B  62  HIS B  64  GLN B  67                    
SITE     2 AC4 14 GLN B  92  HIS B  94  HIS B  96  GLU B 106                    
SITE     3 AC4 14 HIS B 119  LEU B 198  THR B 199  THR B 200                    
SITE     4 AC4 14  ZN B 301  HOH B 483                                          
SITE     1 AC5  4 HIS C  94  HIS C  96  HIS C 119  ETK C 302                    
SITE     1 AC6 14 ARG C  60  ASN C  62  HIS C  64  GLN C  67                    
SITE     2 AC6 14 GLN C  92  HIS C  94  HIS C  96  HIS C 119                    
SITE     3 AC6 14 LEU C 198  THR C 199  THR C 200   ZN C 301                    
SITE     4 AC6 14 HOH C 418  HOH C 477                                          
SITE     1 AC7  4 HIS D  94  HIS D  96  HIS D 119  ETK D 302                    
SITE     1 AC8 12 ARG D  60  ASN D  62  HIS D  64  GLN D  67                    
SITE     2 AC8 12 GLN D  92  HIS D  94  HIS D  96  HIS D 119                    
SITE     3 AC8 12 LEU D 198  THR D 199  THR D 200   ZN D 301                    
CRYST1  152.380  152.380  171.840  90.00  90.00 120.00 H 3          36          
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      0.006563  0.003789  0.000000        0.00000                         
SCALE2      0.000000  0.007578  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005819        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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