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Database: PDB
Entry: 4HT2
LinkDB: 4HT2
Original site: 4HT2 
HEADER    LYASE/LYASE INHIBITOR                   31-OCT-12   4HT2              
TITLE     CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE ISOZYME XII WITH THE    
TITLE    2 INHIBITOR.                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 12;                                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: HUMAN CARBONIC ANHYDRASE XII;                              
COMPND   5 SYNONYM: CARBONATE DEHYDRATASE XII, CARBONIC ANHYDRASE XII, CA-XII,  
COMPND   6 TUMOR ANTIGEN HOM-RCC-3.1.3;                                         
COMPND   7 EC: 4.2.1.1;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CA12;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21A                                    
KEYWDS    DRUG DESIGN, CARBONIC ANHYDRASE, BENZENESULFONAMIDE,METAL-BINDING,    
KEYWDS   2 LYASE-LYASE INHIBITOR COMPLEX, CATALYTIC ACTIVITY, CARBON-OXYGEN     
KEYWDS   3 LYASE ACTIVITY, CARBONATE DEHYDRATASE ACTIVITY, MEMBRANE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.SMIRNOV,E.MANAKOVA,S.GRAZULIS                                       
REVDAT   1   10-APR-13 4HT2    0                                                
JRNL        AUTH   V.DUDUTIENE,A.ZUBRIENE,A.SMIRNOV,J.GYLYTE,D.TIMM,E.MANAKOVA, 
JRNL        AUTH 2 S.GRAZULIS,D.MATULIS                                         
JRNL        TITL   4-SUBSTITUTED-2,3,5,6-TETRAFLUOROBENZENESULFONAMIDES AS      
JRNL        TITL 2 INHIBITORS OF CARBONIC ANHYDRASES I, II, VII, XII, AND XIII. 
JRNL        REF    BIOORG.MED.CHEM.              V.  21  2093 2013              
JRNL        REFN                   ISSN 0968-0896                               
JRNL        PMID   23394791                                                     
JRNL        DOI    10.1016/J.BMC.2013.01.008                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 166177                         
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) : 0.154                           
REMARK   3   R VALUE            (WORKING SET) : 0.150                           
REMARK   3   FREE R VALUE                     : 0.188                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 16455                           
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) : 1.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10865                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.55                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1155                         
REMARK   3   BIN FREE R VALUE                    : 0.2710                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8392                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 165                                     
REMARK   3   SOLVENT ATOMS            : 1504                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.33000                                             
REMARK   3    B22 (A**2) : -0.10000                                             
REMARK   3    B33 (A**2) : 0.27000                                              
REMARK   3    B12 (A**2) : 0.05000                                              
REMARK   3    B13 (A**2) : 0.02000                                              
REMARK   3    B23 (A**2) : 0.49000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.071         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.075         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9207 ; 0.031 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12582 ; 2.462 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1120 ; 7.373 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   457 ;37.671 ;24.683       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1431 ;13.132 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;18.181 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1299 ; 0.200 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7325 ; 0.016 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4473 ; 0.228 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6186 ; 0.311 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1176 ; 0.167 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    13 ; 0.037 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   165 ; 0.260 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):   126 ; 0.175 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5480 ; 1.432 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8927 ; 2.214 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3727 ; 3.129 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3655 ; 4.448 ; 4.500       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4HT2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-NOV-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB075885.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X13                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8123                             
REMARK 200  MONOCHROMATOR                  : SI (111), HORIZONTALLY FOCUSSING   
REMARK 200  OPTICS                         : MIRROR BENT, VERTICALLY FOCUSSING  
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 166179                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.164                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.03900                            
REMARK 200  R SYM                      (I) : 0.03900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.21900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1JD0                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M AMMONIUM CITRATE WITH PH 5.0 AND    
REMARK 280  16% OF PEG4000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 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: 3                                                       
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: C                                     
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: 4                                                       
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: 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     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASN D   134     O    HOH D   779              1.78            
REMARK 500   O    ASP B   253     O    HOH B   653              1.82            
REMARK 500   OD1  ASP B   253     O    HOH B   704              1.84            
REMARK 500   NH2  ARG A   255     O    HOH A   468              1.88            
REMARK 500   N    LYS D     3     O    HOH D   600              2.03            
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    ASP A  99       83.88   -155.56                                   
REMARK 500    GLU A 137       16.80     49.65                                   
REMARK 500    ASP A 235       -3.50     74.53                                   
REMARK 500    ASN A 245       59.43    -96.57                                   
REMARK 500    ASN B 245       56.74    -91.68                                   
REMARK 500    GLU B 254       53.26   -108.14                                   
REMARK 500    LEU C  43       95.90    -67.83                                   
REMARK 500    ASP C  99       80.76   -153.27                                   
REMARK 500    ASN C 245       58.89    -95.88                                   
REMARK 500    ASN D 245       55.77    -91.76                                   
REMARK 500    GLU D 254       -4.01     58.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASP B 235        24.6      L          L   OUTSIDE RANGE           
REMARK 500    ASP B 253        21.4      L          L   OUTSIDE RANGE           
REMARK 500    ARG D 255        23.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C 730        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH C 747        DISTANCE =  5.79 ANGSTROMS                       
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 B 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 V50 B 302   N23                                                    
REMARK 620 2 HIS B  91   NE2 113.1                                              
REMARK 620 3 HIS B  93   NE2 113.5 104.1                                        
REMARK 620 4 HIS B 117   ND1 115.6 111.1  97.8                                  
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 V50 D 302   N23                                                    
REMARK 620 2 HIS D  91   NE2 109.3                                              
REMARK 620 3 HIS D  93   NE2 113.5 102.3                                        
REMARK 620 4 HIS D 117   ND1 119.9 111.0  99.2                                  
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 117   ND1                                                    
REMARK 620 2 HIS C  91   NE2 111.1                                              
REMARK 620 3 V50 C 302   N23 116.2 110.1                                        
REMARK 620 4 HIS C  93   NE2 100.7 104.2 113.7                                  
REMARK 620 N                    1     2     3                                   
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  91   NE2                                                    
REMARK 620 2 HIS A 117   ND1 113.5                                              
REMARK 620 3 V50 A 302   N23 112.5 116.6                                        
REMARK 620 4 HIS A  93   NE2 101.2 101.1 110.1                                  
REMARK 620 5 V50 A 302   S7   96.9 103.3  30.5 140.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE V50 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE V50 B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE V50 C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE V50 D 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 306                 
DBREF  4HT2 A    2   263  UNP    O43570   CAH12_HUMAN     30    291             
DBREF  4HT2 B    2   263  UNP    O43570   CAH12_HUMAN     30    291             
DBREF  4HT2 C    2   263  UNP    O43570   CAH12_HUMAN     30    291             
DBREF  4HT2 D    2   263  UNP    O43570   CAH12_HUMAN     30    291             
SEQADV 4HT2 MET A    1  UNP  O43570              EXPRESSION TAG                 
SEQADV 4HT2 MET B    1  UNP  O43570              EXPRESSION TAG                 
SEQADV 4HT2 MET C    1  UNP  O43570              EXPRESSION TAG                 
SEQADV 4HT2 MET D    1  UNP  O43570              EXPRESSION TAG                 
SEQRES   1 A  263  MET SER LYS TRP THR TYR PHE GLY PRO ASP GLY GLU ASN          
SEQRES   2 A  263  SER TRP SER LYS LYS TYR PRO SER CYS GLY GLY LEU LEU          
SEQRES   3 A  263  GLN SER PRO ILE ASP LEU HIS SER ASP ILE LEU GLN TYR          
SEQRES   4 A  263  ASP ALA SER LEU THR PRO LEU GLU PHE GLN GLY TYR ASN          
SEQRES   5 A  263  LEU SER ALA ASN LYS GLN PHE LEU LEU THR ASN ASN GLY          
SEQRES   6 A  263  HIS SER VAL LYS LEU ASN LEU PRO SER ASP MET HIS ILE          
SEQRES   7 A  263  GLN GLY LEU GLN SER ARG TYR SER ALA THR GLN LEU HIS          
SEQRES   8 A  263  LEU HIS TRP GLY ASN PRO ASN ASP PRO HIS GLY SER GLU          
SEQRES   9 A  263  HIS THR VAL SER GLY GLN HIS PHE ALA ALA GLU LEU HIS          
SEQRES  10 A  263  ILE VAL HIS TYR ASN SER ASP LEU TYR PRO ASP ALA SER          
SEQRES  11 A  263  THR ALA SER ASN LYS SER GLU GLY LEU ALA VAL LEU ALA          
SEQRES  12 A  263  VAL LEU ILE GLU MET GLY SER PHE ASN PRO SER TYR ASP          
SEQRES  13 A  263  LYS ILE PHE SER HIS LEU GLN HIS VAL LYS TYR LYS GLY          
SEQRES  14 A  263  GLN GLU ALA PHE VAL PRO GLY PHE ASN ILE GLU GLU LEU          
SEQRES  15 A  263  LEU PRO GLU ARG THR ALA GLU TYR TYR ARG TYR ARG GLY          
SEQRES  16 A  263  SER LEU THR THR PRO PRO CYS ASN PRO THR VAL LEU TRP          
SEQRES  17 A  263  THR VAL PHE ARG ASN PRO VAL GLN ILE SER GLN GLU GLN          
SEQRES  18 A  263  LEU LEU ALA LEU GLU THR ALA LEU TYR CYS THR HIS MET          
SEQRES  19 A  263  ASP ASP PRO SER PRO ARG GLU MET ILE ASN ASN PHE ARG          
SEQRES  20 A  263  GLN VAL GLN LYS PHE ASP GLU ARG LEU VAL TYR THR SER          
SEQRES  21 A  263  PHE SER GLN                                                  
SEQRES   1 B  263  MET SER LYS TRP THR TYR PHE GLY PRO ASP GLY GLU ASN          
SEQRES   2 B  263  SER TRP SER LYS LYS TYR PRO SER CYS GLY GLY LEU LEU          
SEQRES   3 B  263  GLN SER PRO ILE ASP LEU HIS SER ASP ILE LEU GLN TYR          
SEQRES   4 B  263  ASP ALA SER LEU THR PRO LEU GLU PHE GLN GLY TYR ASN          
SEQRES   5 B  263  LEU SER ALA ASN LYS GLN PHE LEU LEU THR ASN ASN GLY          
SEQRES   6 B  263  HIS SER VAL LYS LEU ASN LEU PRO SER ASP MET HIS ILE          
SEQRES   7 B  263  GLN GLY LEU GLN SER ARG TYR SER ALA THR GLN LEU HIS          
SEQRES   8 B  263  LEU HIS TRP GLY ASN PRO ASN ASP PRO HIS GLY SER GLU          
SEQRES   9 B  263  HIS THR VAL SER GLY GLN HIS PHE ALA ALA GLU LEU HIS          
SEQRES  10 B  263  ILE VAL HIS TYR ASN SER ASP LEU TYR PRO ASP ALA SER          
SEQRES  11 B  263  THR ALA SER ASN LYS SER GLU GLY LEU ALA VAL LEU ALA          
SEQRES  12 B  263  VAL LEU ILE GLU MET GLY SER PHE ASN PRO SER TYR ASP          
SEQRES  13 B  263  LYS ILE PHE SER HIS LEU GLN HIS VAL LYS TYR LYS GLY          
SEQRES  14 B  263  GLN GLU ALA PHE VAL PRO GLY PHE ASN ILE GLU GLU LEU          
SEQRES  15 B  263  LEU PRO GLU ARG THR ALA GLU TYR TYR ARG TYR ARG GLY          
SEQRES  16 B  263  SER LEU THR THR PRO PRO CYS ASN PRO THR VAL LEU TRP          
SEQRES  17 B  263  THR VAL PHE ARG ASN PRO VAL GLN ILE SER GLN GLU GLN          
SEQRES  18 B  263  LEU LEU ALA LEU GLU THR ALA LEU TYR CYS THR HIS MET          
SEQRES  19 B  263  ASP ASP PRO SER PRO ARG GLU MET ILE ASN ASN PHE ARG          
SEQRES  20 B  263  GLN VAL GLN LYS PHE ASP GLU ARG LEU VAL TYR THR SER          
SEQRES  21 B  263  PHE SER GLN                                                  
SEQRES   1 C  263  MET SER LYS TRP THR TYR PHE GLY PRO ASP GLY GLU ASN          
SEQRES   2 C  263  SER TRP SER LYS LYS TYR PRO SER CYS GLY GLY LEU LEU          
SEQRES   3 C  263  GLN SER PRO ILE ASP LEU HIS SER ASP ILE LEU GLN TYR          
SEQRES   4 C  263  ASP ALA SER LEU THR PRO LEU GLU PHE GLN GLY TYR ASN          
SEQRES   5 C  263  LEU SER ALA ASN LYS GLN PHE LEU LEU THR ASN ASN GLY          
SEQRES   6 C  263  HIS SER VAL LYS LEU ASN LEU PRO SER ASP MET HIS ILE          
SEQRES   7 C  263  GLN GLY LEU GLN SER ARG TYR SER ALA THR GLN LEU HIS          
SEQRES   8 C  263  LEU HIS TRP GLY ASN PRO ASN ASP PRO HIS GLY SER GLU          
SEQRES   9 C  263  HIS THR VAL SER GLY GLN HIS PHE ALA ALA GLU LEU HIS          
SEQRES  10 C  263  ILE VAL HIS TYR ASN SER ASP LEU TYR PRO ASP ALA SER          
SEQRES  11 C  263  THR ALA SER ASN LYS SER GLU GLY LEU ALA VAL LEU ALA          
SEQRES  12 C  263  VAL LEU ILE GLU MET GLY SER PHE ASN PRO SER TYR ASP          
SEQRES  13 C  263  LYS ILE PHE SER HIS LEU GLN HIS VAL LYS TYR LYS GLY          
SEQRES  14 C  263  GLN GLU ALA PHE VAL PRO GLY PHE ASN ILE GLU GLU LEU          
SEQRES  15 C  263  LEU PRO GLU ARG THR ALA GLU TYR TYR ARG TYR ARG GLY          
SEQRES  16 C  263  SER LEU THR THR PRO PRO CYS ASN PRO THR VAL LEU TRP          
SEQRES  17 C  263  THR VAL PHE ARG ASN PRO VAL GLN ILE SER GLN GLU GLN          
SEQRES  18 C  263  LEU LEU ALA LEU GLU THR ALA LEU TYR CYS THR HIS MET          
SEQRES  19 C  263  ASP ASP PRO SER PRO ARG GLU MET ILE ASN ASN PHE ARG          
SEQRES  20 C  263  GLN VAL GLN LYS PHE ASP GLU ARG LEU VAL TYR THR SER          
SEQRES  21 C  263  PHE SER GLN                                                  
SEQRES   1 D  263  MET SER LYS TRP THR TYR PHE GLY PRO ASP GLY GLU ASN          
SEQRES   2 D  263  SER TRP SER LYS LYS TYR PRO SER CYS GLY GLY LEU LEU          
SEQRES   3 D  263  GLN SER PRO ILE ASP LEU HIS SER ASP ILE LEU GLN TYR          
SEQRES   4 D  263  ASP ALA SER LEU THR PRO LEU GLU PHE GLN GLY TYR ASN          
SEQRES   5 D  263  LEU SER ALA ASN LYS GLN PHE LEU LEU THR ASN ASN GLY          
SEQRES   6 D  263  HIS SER VAL LYS LEU ASN LEU PRO SER ASP MET HIS ILE          
SEQRES   7 D  263  GLN GLY LEU GLN SER ARG TYR SER ALA THR GLN LEU HIS          
SEQRES   8 D  263  LEU HIS TRP GLY ASN PRO ASN ASP PRO HIS GLY SER GLU          
SEQRES   9 D  263  HIS THR VAL SER GLY GLN HIS PHE ALA ALA GLU LEU HIS          
SEQRES  10 D  263  ILE VAL HIS TYR ASN SER ASP LEU TYR PRO ASP ALA SER          
SEQRES  11 D  263  THR ALA SER ASN LYS SER GLU GLY LEU ALA VAL LEU ALA          
SEQRES  12 D  263  VAL LEU ILE GLU MET GLY SER PHE ASN PRO SER TYR ASP          
SEQRES  13 D  263  LYS ILE PHE SER HIS LEU GLN HIS VAL LYS TYR LYS GLY          
SEQRES  14 D  263  GLN GLU ALA PHE VAL PRO GLY PHE ASN ILE GLU GLU LEU          
SEQRES  15 D  263  LEU PRO GLU ARG THR ALA GLU TYR TYR ARG TYR ARG GLY          
SEQRES  16 D  263  SER LEU THR THR PRO PRO CYS ASN PRO THR VAL LEU TRP          
SEQRES  17 D  263  THR VAL PHE ARG ASN PRO VAL GLN ILE SER GLN GLU GLN          
SEQRES  18 D  263  LEU LEU ALA LEU GLU THR ALA LEU TYR CYS THR HIS MET          
SEQRES  19 D  263  ASP ASP PRO SER PRO ARG GLU MET ILE ASN ASN PHE ARG          
SEQRES  20 D  263  GLN VAL GLN LYS PHE ASP GLU ARG LEU VAL TYR THR SER          
SEQRES  21 D  263  PHE SER GLN                                                  
HET     ZN  A 301       1                                                       
HET    V50  A 302      46                                                       
HET    PEG  A 303       7                                                       
HET    EDO  A 304       8                                                       
HET    EDO  A 305       4                                                       
HET    EDO  A 306       4                                                       
HET     ZN  B 301       1                                                       
HET    V50  B 302      23                                                       
HET    PEG  B 303       7                                                       
HET    EDO  B 304       4                                                       
HET    EDO  B 305       4                                                       
HET    EDO  B 306       4                                                       
HET    EDO  B 307       4                                                       
HET    EDO  B 308       4                                                       
HET     ZN  C 301       1                                                       
HET    V50  C 302      23                                                       
HET    EDO  C 303       4                                                       
HET     ZN  D 301       1                                                       
HET    V50  D 302      23                                                       
HET    PEG  D 303       7                                                       
HET    EDO  D 304       4                                                       
HET    EDO  D 305       8                                                       
HET    EDO  D 306       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     V50 4-[(4,6-DIMETHYLPYRIMIDIN-2-YL)THIO]-2,3,5,6-                    
HETNAM   2 V50  TETRAFLUOROBENZENESULFONAMIDE                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   6  V50    4(C12 H9 F4 N3 O2 S2)                                        
FORMUL   7  PEG    3(C4 H10 O3)                                                 
FORMUL   8  EDO    12(C2 H6 O2)                                                 
FORMUL  28  HOH   *1504(H2 O)                                                   
HELIX    1   1 GLY A   11  ASN A   13  5                                   3    
HELIX    2   2 SER A   14  TYR A   19  1                                   6    
HELIX    3   3 PRO A   20  GLY A   24  5                                   5    
HELIX    4   4 HIS A   33  ASP A   35  5                                   3    
HELIX    5   5 ASP A  128  SER A  133  1                                   6    
HELIX    6   6 ASN A  152  SER A  160  1                                   9    
HELIX    7   7 HIS A  161  VAL A  165  5                                   5    
HELIX    8   8 ASN A  178  LEU A  183  5                                   6    
HELIX    9   9 GLN A  219  ALA A  228  1                                  10    
HELIX   10  10 GLY B   11  ASN B   13  5                                   3    
HELIX   11  11 SER B   14  TYR B   19  1                                   6    
HELIX   12  12 PRO B   20  GLY B   24  5                                   5    
HELIX   13  13 HIS B   33  ASP B   35  5                                   3    
HELIX   14  14 ASP B  128  SER B  133  1                                   6    
HELIX   15  15 ASN B  152  SER B  160  1                                   9    
HELIX   16  16 HIS B  161  VAL B  165  5                                   5    
HELIX   17  17 ASN B  178  LEU B  183  5                                   6    
HELIX   18  18 GLN B  219  ALA B  228  1                                  10    
HELIX   19  19 GLY C   11  ASN C   13  5                                   3    
HELIX   20  20 SER C   14  TYR C   19  1                                   6    
HELIX   21  21 PRO C   20  GLY C   24  5                                   5    
HELIX   22  22 HIS C   33  ASP C   35  5                                   3    
HELIX   23  23 ASP C  128  SER C  133  1                                   6    
HELIX   24  24 ASN C  152  SER C  160  1                                   9    
HELIX   25  25 HIS C  161  VAL C  165  5                                   5    
HELIX   26  26 ASN C  178  LEU C  183  5                                   6    
HELIX   27  27 SER C  218  ALA C  228  1                                  11    
HELIX   28  28 GLY D   11  LYS D   18  5                                   8    
HELIX   29  29 TYR D   19  GLY D   24  5                                   6    
HELIX   30  30 HIS D   33  ASP D   35  5                                   3    
HELIX   31  31 ASP D  128  SER D  133  1                                   6    
HELIX   32  32 TYR D  155  SER D  160  1                                   6    
HELIX   33  33 HIS D  161  VAL D  165  5                                   5    
HELIX   34  34 ASN D  178  LEU D  183  5                                   6    
HELIX   35  35 SER D  218  LEU D  229  1                                  12    
SHEET    1   A 2 ASP A  31  LEU A  32  0                                        
SHEET    2   A 2 THR A 106  VAL A 107  1  O  THR A 106   N  LEU A  32           
SHEET    1   B10 LEU A  37  TYR A  39  0                                        
SHEET    2   B10 VAL A 257  THR A 259  1  O  VAL A 257   N  GLN A  38           
SHEET    3   B10 TYR A 190  GLY A 195 -1  N  ARG A 192   O  TYR A 258           
SHEET    4   B10 VAL A 206  PHE A 211 -1  O  VAL A 206   N  GLY A 195           
SHEET    5   B10 LEU A 139  GLY A 149  1  N  ALA A 143   O  THR A 209           
SHEET    6   B10 ALA A 114  ASN A 122 -1  N  ALA A 114   O  ILE A 146           
SHEET    7   B10 TYR A  85  TRP A  94 -1  N  GLN A  89   O  VAL A 119           
SHEET    8   B10 VAL A  68  ASN A  71 -1  N  LEU A  70   O  LEU A  90           
SHEET    9   B10 GLN A  58  ASN A  63 -1  N  LEU A  60   O  ASN A  71           
SHEET   10   B10 GLU A 171  PRO A 175 -1  O  ALA A 172   N  LEU A  61           
SHEET    1   C 6 GLU A  47  GLN A  49  0                                        
SHEET    2   C 6 HIS A  77  GLN A  79 -1  O  GLN A  79   N  GLU A  47           
SHEET    3   C 6 TYR A  85  TRP A  94 -1  O  TYR A  85   N  ILE A  78           
SHEET    4   C 6 ALA A 114  ASN A 122 -1  O  VAL A 119   N  GLN A  89           
SHEET    5   C 6 LEU A 139  GLY A 149 -1  O  ILE A 146   N  ALA A 114           
SHEET    6   C 6 VAL A 215  SER A 218  1  O  ILE A 217   N  GLY A 149           
SHEET    1   D 2 ASP B  31  LEU B  32  0                                        
SHEET    2   D 2 THR B 106  VAL B 107  1  O  THR B 106   N  LEU B  32           
SHEET    1   E10 LEU B  37  TYR B  39  0                                        
SHEET    2   E10 VAL B 257  THR B 259  1  O  THR B 259   N  GLN B  38           
SHEET    3   E10 TYR B 190  GLY B 195 -1  N  ARG B 192   O  TYR B 258           
SHEET    4   E10 VAL B 206  PHE B 211 -1  O  VAL B 206   N  GLY B 195           
SHEET    5   E10 LEU B 139  GLY B 149  1  N  ALA B 143   O  THR B 209           
SHEET    6   E10 ALA B 114  ASN B 122 -1  N  ILE B 118   O  LEU B 142           
SHEET    7   E10 TYR B  85  TRP B  94 -1  N  GLN B  89   O  VAL B 119           
SHEET    8   E10 VAL B  68  ASN B  71 -1  N  LEU B  70   O  LEU B  90           
SHEET    9   E10 GLN B  58  ASN B  63 -1  N  THR B  62   O  LYS B  69           
SHEET   10   E10 GLU B 171  PRO B 175 -1  O  ALA B 172   N  LEU B  61           
SHEET    1   F 6 GLU B  47  GLN B  49  0                                        
SHEET    2   F 6 HIS B  77  GLN B  79 -1  O  HIS B  77   N  GLN B  49           
SHEET    3   F 6 TYR B  85  TRP B  94 -1  O  TYR B  85   N  ILE B  78           
SHEET    4   F 6 ALA B 114  ASN B 122 -1  O  VAL B 119   N  GLN B  89           
SHEET    5   F 6 LEU B 139  GLY B 149 -1  O  LEU B 142   N  ILE B 118           
SHEET    6   F 6 VAL B 215  SER B 218  1  O  ILE B 217   N  GLY B 149           
SHEET    1   G 2 ASP C  31  LEU C  32  0                                        
SHEET    2   G 2 THR C 106  VAL C 107  1  O  THR C 106   N  LEU C  32           
SHEET    1   H10 LEU C  37  TYR C  39  0                                        
SHEET    2   H10 VAL C 257  THR C 259  1  O  VAL C 257   N  GLN C  38           
SHEET    3   H10 TYR C 190  GLY C 195 -1  N  ARG C 192   O  TYR C 258           
SHEET    4   H10 VAL C 206  PHE C 211 -1  O  VAL C 206   N  GLY C 195           
SHEET    5   H10 LEU C 139  MET C 148  1  N  ALA C 143   O  THR C 209           
SHEET    6   H10 ALA C 114  ASN C 122 -1  N  ALA C 114   O  ILE C 146           
SHEET    7   H10 TYR C  85  TRP C  94 -1  N  GLN C  89   O  VAL C 119           
SHEET    8   H10 VAL C  68  ASN C  71 -1  N  LEU C  70   O  LEU C  90           
SHEET    9   H10 GLN C  58  ASN C  63 -1  N  THR C  62   O  LYS C  69           
SHEET   10   H10 GLU C 171  PRO C 175 -1  O  ALA C 172   N  LEU C  61           
SHEET    1   I 6 GLU C  47  GLN C  49  0                                        
SHEET    2   I 6 HIS C  77  GLN C  79 -1  O  GLN C  79   N  GLU C  47           
SHEET    3   I 6 TYR C  85  TRP C  94 -1  O  TYR C  85   N  ILE C  78           
SHEET    4   I 6 ALA C 114  ASN C 122 -1  O  VAL C 119   N  GLN C  89           
SHEET    5   I 6 LEU C 139  MET C 148 -1  O  ILE C 146   N  ALA C 114           
SHEET    6   I 6 VAL C 215  ILE C 217  1  O  VAL C 215   N  GLU C 147           
SHEET    1   J 2 ASP D  31  LEU D  32  0                                        
SHEET    2   J 2 THR D 106  VAL D 107  1  O  THR D 106   N  LEU D  32           
SHEET    1   K10 LEU D  37  TYR D  39  0                                        
SHEET    2   K10 VAL D 257  THR D 259  1  O  THR D 259   N  GLN D  38           
SHEET    3   K10 TYR D 190  GLY D 195 -1  N  ARG D 192   O  TYR D 258           
SHEET    4   K10 VAL D 206  PHE D 211 -1  O  VAL D 206   N  GLY D 195           
SHEET    5   K10 LEU D 139  MET D 148  1  N  ALA D 143   O  THR D 209           
SHEET    6   K10 ALA D 114  ASN D 122 -1  N  ALA D 114   O  ILE D 146           
SHEET    7   K10 TYR D  85  TRP D  94 -1  N  GLN D  89   O  VAL D 119           
SHEET    8   K10 VAL D  68  ASN D  71 -1  N  LEU D  70   O  LEU D  90           
SHEET    9   K10 GLN D  58  ASN D  63 -1  N  THR D  62   O  LYS D  69           
SHEET   10   K10 GLU D 171  PRO D 175 -1  O  VAL D 174   N  PHE D  59           
SHEET    1   L 6 GLU D  47  GLN D  49  0                                        
SHEET    2   L 6 HIS D  77  GLN D  79 -1  O  HIS D  77   N  GLN D  49           
SHEET    3   L 6 TYR D  85  TRP D  94 -1  O  TYR D  85   N  ILE D  78           
SHEET    4   L 6 ALA D 114  ASN D 122 -1  O  VAL D 119   N  GLN D  89           
SHEET    5   L 6 LEU D 139  MET D 148 -1  O  ILE D 146   N  ALA D 114           
SHEET    6   L 6 VAL D 215  ILE D 217  1  O  VAL D 215   N  GLU D 147           
SSBOND   1 CYS A   22    CYS A  202                          1555   1555  2.06  
SSBOND   2 CYS B   22    CYS B  202                          1555   1555  2.05  
SSBOND   3 CYS C   22    CYS C  202                          1555   1555  2.06  
SSBOND   4 CYS D   22    CYS D  202                          1555   1555  2.06  
LINK        ZN    ZN B 301                 N23 V50 B 302     1555   1555  1.99  
LINK        ZN    ZN D 301                 N23 V50 D 302     1555   1555  2.00  
LINK         ND1 HIS C 117                ZN    ZN C 301     1555   1555  2.02  
LINK         NE2 HIS C  91                ZN    ZN C 301     1555   1555  2.02  
LINK        ZN    ZN C 301                 N23 V50 C 302     1555   1555  2.02  
LINK         NE2 HIS A  91                ZN    ZN A 301     1555   1555  2.02  
LINK         NE2 HIS C  93                ZN    ZN C 301     1555   1555  2.03  
LINK         ND1 HIS A 117                ZN    ZN A 301     1555   1555  2.04  
LINK         NE2 HIS B  91                ZN    ZN B 301     1555   1555  2.04  
LINK         NE2 HIS D  91                ZN    ZN D 301     1555   1555  2.05  
LINK        ZN    ZN A 301                 N23CV50 A 302     1555   1555  2.05  
LINK         NE2 HIS A  93                ZN    ZN A 301     1555   1555  2.06  
LINK         NE2 HIS B  93                ZN    ZN B 301     1555   1555  2.06  
LINK         ND1 HIS B 117                ZN    ZN B 301     1555   1555  2.07  
LINK         NE2 HIS D  93                ZN    ZN D 301     1555   1555  2.07  
LINK         ND1 HIS D 117                ZN    ZN D 301     1555   1555  2.08  
LINK        ZN    ZN A 301                 N23BV50 A 302     1555   1555  2.09  
LINK        ZN    ZN A 301                 S7 CV50 A 302     1555   1555  3.00  
CISPEP   1 SER A   28    PRO A   29          0        -0.41                     
CISPEP   2 PRO A  200    PRO A  201          0         3.99                     
CISPEP   3 SER B   28    PRO B   29          0        -0.15                     
CISPEP   4 PRO B  200    PRO B  201          0         5.09                     
CISPEP   5 SER C   28    PRO C   29          0        -1.47                     
CISPEP   6 PRO C  200    PRO C  201          0         9.59                     
CISPEP   7 SER D   28    PRO D   29          0        -2.65                     
CISPEP   8 PRO D  200    PRO D  201          0         4.07                     
SITE     1 AC1  4 HIS A  91  HIS A  93  HIS A 117  V50 A 302                    
SITE     1 AC2 20 GLN A  89  HIS A  91  HIS A  93  HIS A 117                    
SITE     2 AC2 20 VAL A 119  SER A 130  LEU A 139  VAL A 141                    
SITE     3 AC2 20 LEU A 197  THR A 198  THR A 199  PRO A 200                    
SITE     4 AC2 20 ASN A 203  TRP A 208   ZN A 301  PEG A 303                    
SITE     5 AC2 20 EDO A 304  HOH A 543  HOH A 592  HOH A 604                    
SITE     1 AC3  6 ASN A  64  LYS A  69  GLN A  89  THR A 199                    
SITE     2 AC3  6 V50 A 302  EDO A 304                                          
SITE     1 AC4  9 ASN A  64  SER A  67  GLN A  89  HIS A  91                    
SITE     2 AC4  9 HIS A  93  THR A 199  V50 A 302  PEG A 303                    
SITE     3 AC4  9 HOH A 498                                                     
SITE     1 AC5  6 SER A  42  LEU A  43  THR A  44  GLY A  80                    
SITE     2 AC5  6 TYR A 190  ARG A 192                                          
SITE     1 AC6  3 ASP A  40  TYR A 258  HOH A 488                               
SITE     1 AC7  4 HIS B  91  HIS B  93  HIS B 117  V50 B 302                    
SITE     1 AC8 14 GLN B  89  HIS B  91  HIS B  93  HIS B 117                    
SITE     2 AC8 14 VAL B 119  SER B 133  LEU B 197  THR B 198                    
SITE     3 AC8 14 THR B 199  PRO B 200   ZN B 301  EDO B 304                    
SITE     4 AC8 14 EDO B 305  HOH B 492                                          
SITE     1 AC9  9 HIS B 164  PHE B 173  HOH B 499  HOH B 573                    
SITE     2 AC9  9 HOH B 769  GLN C  58  HIS C 161  PHE C 173                    
SITE     3 AC9  9 PRO C 175                                                     
SITE     1 BC1  8 ASN B  64  HIS B  66  GLN B  89  HIS B  91                    
SITE     2 BC1  8 V50 B 302  EDO B 305  HOH B 450  HOH B 642                    
SITE     1 BC2  6 ASN B  64  LYS B  69  V50 B 302  EDO B 304                    
SITE     2 BC2  6 HOH B 641  HOH B 648                                          
SITE     1 BC3  6 ASN B  71  LEU B  72  THR B  88  HOH B 437                    
SITE     2 BC3  6 HOH B 445  HOH B 456                                          
SITE     1 BC4  4 SER B  83  ASP B 124  MET B 234  ASP B 235                    
SITE     1 BC5  4 LYS B  57  GLN B  58  HOH B 617  HIS C 164                    
SITE     1 BC6  4 HIS C  91  HIS C  93  HIS C 117  V50 C 302                    
SITE     1 BC7 16 GLN C  89  HIS C  91  HIS C  93  HIS C 117                    
SITE     2 BC7 16 VAL C 119  SER C 133  LEU C 139  LEU C 197                    
SITE     3 BC7 16 THR C 198  THR C 199  PRO C 200  PRO C 201                    
SITE     4 BC7 16 TRP C 208   ZN C 301  EDO C 303  HOH C 608                    
SITE     1 BC8  7 ASN C  64  HIS C  66  GLN C  89  HIS C  91                    
SITE     2 BC8  7 V50 C 302  HOH C 609  HOH C 611                               
SITE     1 BC9  4 HIS D  91  HIS D  93  HIS D 117  V50 D 302                    
SITE     1 CC1 14 GLN D  89  HIS D  91  HIS D  93  HIS D 117                    
SITE     2 CC1 14 VAL D 119  SER D 133  LEU D 197  THR D 198                    
SITE     3 CC1 14 THR D 199  PRO D 200   ZN D 301  EDO D 304                    
SITE     4 CC1 14 EDO D 305  HOH D 662                                          
SITE     1 CC2  9 GLN D 163  GLU D 220  ALA D 224  HOH D 531                    
SITE     2 CC2  9 HOH D 551  HOH D 582  HOH D 606  HOH D 626                    
SITE     3 CC2  9 HOH D 786                                                     
SITE     1 CC3  8 ASN D  64  HIS D  66  SER D  67  GLN D  89                    
SITE     2 CC3  8 HIS D  91  V50 D 302  EDO D 305  HOH D 664                    
SITE     1 CC4  7 ASN D  64  LYS D  69  GLN D  89  V50 D 302                    
SITE     2 CC4  7 EDO D 304  HOH D 663  HOH D 665                               
SITE     1 CC5  8 ALA A  55  PRO A 175  HOH A 677  HOH A 728                    
SITE     2 CC5  8 HOH A 729  SER D 160  HIS D 161  HIS D 164                    
CRYST1   46.709   67.261   80.689  81.78  84.01  86.48 P 1           4          
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      0.021409 -0.001317 -0.002085        0.00000                         
SCALE2      0.000000  0.014896 -0.002069        0.00000                         
SCALE3      0.000000  0.000000  0.012581        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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