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Database: PDB
Entry: 5FL5
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Original site: 5FL5 
HEADER    LYASE                                   21-OCT-15   5FL5              
TITLE     THREE DIMENSIONAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE IX IN COMPLEX 
TITLE    2 WITH 5-(1-(4-METHOXYPHENYL)-1H-1,2,3-TRIAZOL-4-YL)THIOPHENE-2-       
TITLE    3 SULFONAMIDE                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBONIC ANHYDRASE IX;                                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 137-391;                                      
COMPND   5 SYNONYM: CARBONATE DEHYDRATASE IX, CARBONIC ANHYDRASE IX, CA-IX, CAI 
COMPND   6 X, MEMBRANE ANTIGEN MN, P54/58N, RENAL CELL CARCINOMA-ASSOCIATED     
COMPND   7 ANTIGEN G250, RCC-ASSOCIATED ANTIGEN G250, PMW1, CARBONIC ANHYDRASE  
COMPND   8 IX;                                                                  
COMPND   9 EC: 4.2.1.1;                                                         
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4922                                        
KEYWDS    LYASE, CARBONIC ANHYDRASE IX, CARBONIC ANHYDRASE 9, CA IX, CA 9       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LEITANS,K.TARS,R.ZALUBOVSKIS                                        
REVDAT   5   06-FEB-19 5FL5    1       REMARK                                   
REVDAT   4   30-JAN-19 5FL5    1       REMARK                                   
REVDAT   3   17-JAN-18 5FL5    1       REMARK                                   
REVDAT   2   09-DEC-15 5FL5    1       JRNL                                     
REVDAT   1   11-NOV-15 5FL5    0                                                
JRNL        AUTH   J.LEITANS,A.KAZAKS,A.BALODE,J.IVANOVA,R.ZALUBOVSKIS,         
JRNL        AUTH 2 C.T.SUPURAN,K.TARS                                           
JRNL        TITL   AN EFFICIENT EXPRESSION AND CRYSTALLIZATION SYSTEM OF THE    
JRNL        TITL 2 CANCER ASOCIATED CARBONIC ANHYDRASE ISOFORM IX.              
JRNL        REF    J.MED.CHEM.                   V.  58  9004 2015              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   26522624                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.5B01343                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 88022                          
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) : 0.160                           
REMARK   3   R VALUE            (WORKING SET) : 0.158                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4640                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6523                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2500                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 343                          
REMARK   3   BIN FREE R VALUE                    : 0.2630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7706                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 235                                     
REMARK   3   SOLVENT ATOMS            : 901                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.26000                                              
REMARK   3    B22 (A**2) : 0.26000                                              
REMARK   3    B33 (A**2) : -0.85000                                             
REMARK   3    B12 (A**2) : 0.13000                                              
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): 0.135         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.129         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.099         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.836         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8155 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  7498 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11154 ; 1.754 ; 1.994       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17220 ; 0.907 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1000 ; 5.920 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   355 ;35.599 ;23.070       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1143 ;12.360 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    65 ;16.513 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1202 ; 0.124 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9181 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1896 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4015 ; 1.460 ; 2.439       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4011 ; 1.459 ; 2.438       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5008 ; 2.385 ; 3.651       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4140 ; 2.511 ; 2.762       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. U VALUES REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 5FL5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1290065357.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : SI CRYSTAL                         
REMARK 200  OPTICS                         : MULTILAYER                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 92662                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.68000                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3IAI                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE, 1.26 M AMMONIUM   
REMARK 280  SULFATE, TRIS- HCL, PH 8.5, PROTEIN 10 MG/ML, 5-10 MM               
REMARK 280  INHIBITOR(STOCK SOLUTION WAS 100 MM INHIBITOR DISSOLVED IN 100%     
REMARK 280  DIMETHYL SULFOXIDE) VAPOR DIFFUSION, SITTING DROP, TEMPERATURE      
REMARK 280  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       56.86333            
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       56.86333            
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       56.86333            
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      113.72667            
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      113.72667            
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      113.72667            
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     GLY A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     GLN B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     PRO C     4                                                      
REMARK 465     ASP C     5                                                      
REMARK 465     GLN C     6                                                      
REMARK 465     SER C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     PRO D     4                                                      
REMARK 465     ASP D     5                                                      
REMARK 465     GLN D     6                                                      
REMARK 465     SER D     7                                                      
REMARK 465     HIS D     8                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 165    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 236    CG   OD1  OD2                                       
REMARK 470     ARG B  10    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  19    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 102    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 165    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 169    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 222    CG   CD   CE   NZ                                   
REMARK 470     ASP B 236    CG   OD1  OD2                                       
REMARK 470     ARG C  10    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C  19    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 165    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 222    CG   CD   CE   NZ                                   
REMARK 470     ASP C 236    CG   OD1  OD2                                       
REMARK 470     ARG D  19    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 152    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 165    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 236    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  2272     O    HOH A  2273              2.01            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH2  ARG A    62     O    LEU C   134     5455     2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
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   ATM2   ATM3                                     
REMARK 500    ARG A  62   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG A  62   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
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 236       39.45    -96.17                                   
REMARK 500    ALA B 100      107.80    -40.96                                   
REMARK 500    ASP B 236       44.40   -109.76                                   
REMARK 500    ALA C 100      117.70    -39.11                                   
REMARK 500    ASP C 236       54.37   -112.93                                   
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 A1260  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 82E A 266   N1                                                     
REMARK 620 2 HIS A  96   NE2 115.5                                              
REMARK 620 3 HIS A  94   NE2 107.3 104.4                                        
REMARK 620 4 HIS A 119   ND1 117.6  97.7 113.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1260  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 82E B 267   N1                                                     
REMARK 620 2 HIS B  94   NE2 111.0                                              
REMARK 620 3 HIS B 119   ND1 117.4 111.7                                        
REMARK 620 4 HIS B  96   NE2 112.9 106.0  96.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1260  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 82E C 265   N1                                                     
REMARK 620 2 82E C 265   S2   30.7                                              
REMARK 620 3 HIS C  94   NE2 111.5  94.1                                        
REMARK 620 4 HIS C 119   ND1 118.0 107.4 114.5                                  
REMARK 620 5 HIS C  96   NE2 108.8 139.4 106.7  95.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D1260  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 82E D 269   N1                                                     
REMARK 620 2 82E D 269   S2   29.4                                              
REMARK 620 3 HIS D  96   NE2 115.4 144.8                                        
REMARK 620 4 HIS D 119   ND1 119.5 104.0  97.4                                  
REMARK 620 5 HIS D  94   NE2 107.7  93.0 105.5 110.3                            
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 1260                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 82E A 266                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1261                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1260                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 82E B 267                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1261                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1260                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 82E C 265                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1261                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1260                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 82E D 269                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 1261                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1262                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1262                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1262                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1262                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1263                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1263                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1264                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1263                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1264                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1265                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1263                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1264                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1266                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1265                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1267                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1268                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1264                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1269                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1266                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B 1267                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 1270                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS D 1265                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5FL4   RELATED DB: PDB                                   
REMARK 900 THREE DIMENSIONAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE IX IN        
REMARK 900 COMPLEX WITH 5-(1-NAPHTHALEN-1-YL-1,2,3- TRIAZOL-4-YL)THIOPHENE-2-   
REMARK 900 SULFONAMIDE                                                          
REMARK 900 RELATED ID: 5FL6   RELATED DB: PDB                                   
REMARK 900 THREE DIMENSIONAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE IX IN        
REMARK 900 COMPLEX WITH 5-(1-(4-METHYLPHENYL)-1H-1,2, 3-TRIAZOL-4-YL)THIOPHENE- 
REMARK 900 2-SULFONAMIDE                                                        
DBREF  5FL5 A    5   259  UNP    Q16790   CAH9_HUMAN     137    391             
DBREF  5FL5 B    5   259  UNP    Q16790   CAH9_HUMAN     137    391             
DBREF  5FL5 C    5   259  UNP    Q16790   CAH9_HUMAN     137    391             
DBREF  5FL5 D    5   259  UNP    Q16790   CAH9_HUMAN     137    391             
SEQADV 5FL5 GLY A    3  UNP  Q16790              EXPRESSION TAG                 
SEQADV 5FL5 PRO A    4  UNP  Q16790              EXPRESSION TAG                 
SEQADV 5FL5 SER A   42  UNP  Q16790    CYS   174 ENGINEERED MUTATION            
SEQADV 5FL5 GLY B    3  UNP  Q16790              EXPRESSION TAG                 
SEQADV 5FL5 PRO B    4  UNP  Q16790              EXPRESSION TAG                 
SEQADV 5FL5 SER B   42  UNP  Q16790    CYS   174 ENGINEERED MUTATION            
SEQADV 5FL5 GLY C    3  UNP  Q16790              EXPRESSION TAG                 
SEQADV 5FL5 PRO C    4  UNP  Q16790              EXPRESSION TAG                 
SEQADV 5FL5 SER C   42  UNP  Q16790    CYS   174 ENGINEERED MUTATION            
SEQADV 5FL5 GLY D    3  UNP  Q16790              EXPRESSION TAG                 
SEQADV 5FL5 PRO D    4  UNP  Q16790              EXPRESSION TAG                 
SEQADV 5FL5 SER D   42  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    82E  A 266      22                                                       
HET     ZN  A1260       1                                                       
HET    GOL  A1261       6                                                       
HET    SO4  A1262       5                                                       
HET    SO4  A1263       5                                                       
HET    SO4  A1264       5                                                       
HET    SO4  A1265       5                                                       
HET    SO4  A1266       5                                                       
HET    SO4  A1267       5                                                       
HET    SO4  A1268       5                                                       
HET    SO4  A1269       5                                                       
HET    TRS  A1270       8                                                       
HET    82E  B 267      22                                                       
HET     ZN  B1260       1                                                       
HET    GOL  B1261       6                                                       
HET    SO4  B1262       5                                                       
HET    SO4  B1263       5                                                       
HET    SO4  B1264       5                                                       
HET    SO4  B1265       5                                                       
HET    SO4  B1266       5                                                       
HET    TRS  B1267       8                                                       
HET    82E  C 265      22                                                       
HET     ZN  C1260       1                                                       
HET    GOL  C1261       6                                                       
HET    SO4  C1262       5                                                       
HET    SO4  C1263       5                                                       
HET    SO4  C1264       5                                                       
HET    82E  D 269      22                                                       
HET     ZN  D1260       1                                                       
HET    GOL  D1261       6                                                       
HET    SO4  D1262       5                                                       
HET    SO4  D1263       5                                                       
HET    SO4  D1264       5                                                       
HET    TRS  D1265       8                                                       
HETNAM     82E 5-[1-(4-METHOXYPHENYL)-1,2,3-TRIAZOL-4-YL]THIOPHENE-2-           
HETNAM   2 82E  SULFONAMIDE                                                     
HETNAM      ZN ZINC ION                                                         
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   5  82E    4(C13 H12 N4 O3 S2)                                          
FORMUL   6   ZN    4(ZN 2+)                                                     
FORMUL   7  GOL    4(C3 H8 O3)                                                  
FORMUL   8  SO4    19(O4 S 2-)                                                  
FORMUL  16  TRS    3(C4 H12 N O3 1+)                                            
FORMUL  39  HOH   *901(H2 O)                                                    
HELIX    1   1 PRO A   16  SER A   21  1                                   6    
HELIX    2   2 PRO A   22  GLY A   26  5                                   5    
HELIX    3   3 ARG A   35  ALA A   39  5                                   5    
HELIX    4   4 ARG A  129  LEU A  134  1                                   6    
HELIX    5   5 ASN A  154  SER A  162  1                                   9    
HELIX    6   6 ARG A  163  ALA A  168  5                                   6    
HELIX    7   7 ILE A  181  LEU A  185  5                                   5    
HELIX    8   8 SER A  220  THR A  230  1                                  11    
HELIX    9   9 PRO B   16  VAL B   20  5                                   5    
HELIX   10  10 SER B   21  GLY B   26  5                                   6    
HELIX   11  11 ARG B   35  ALA B   39  5                                   5    
HELIX   12  12 ARG B  129  LEU B  134  1                                   6    
HELIX   13  13 ASN B  154  SER B  162  1                                   9    
HELIX   14  14 ARG B  163  ALA B  168  5                                   6    
HELIX   15  15 ILE B  181  LEU B  185  5                                   5    
HELIX   16  16 SER B  220  THR B  230  1                                  11    
HELIX   17  17 PRO C   16  SER C   21  1                                   6    
HELIX   18  18 PRO C   22  GLY C   26  5                                   5    
HELIX   19  19 ARG C   35  ALA C   39  5                                   5    
HELIX   20  20 ARG C  129  LEU C  134  1                                   6    
HELIX   21  21 ASN C  154  SER C  162  1                                   9    
HELIX   22  22 ARG C  163  ALA C  168  5                                   6    
HELIX   23  23 ILE C  181  LEU C  185  5                                   5    
HELIX   24  24 SER C  220  THR C  230  1                                  11    
HELIX   25  25 PRO D   16  SER D   21  1                                   6    
HELIX   26  26 PRO D   22  GLY D   26  5                                   5    
HELIX   27  27 ARG D   35  ALA D   39  5                                   5    
HELIX   28  28 ARG D  129  LEU D  134  1                                   6    
HELIX   29  29 ASN D  154  SER D  162  1                                   9    
HELIX   30  30 ARG D  163  ALA D  168  5                                   6    
HELIX   31  31 ILE D  181  LEU D  185  5                                   5    
HELIX   32  32 ALA D  221  THR D  230  1                                  10    
SHEET    1  AA 2 ASP A  33  ILE A  34  0                                        
SHEET    2  AA 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  34           
SHEET    1  AB 6 ALA A  40  PHE A  41  0                                        
SHEET    2  AB 6 GLU A 255  ALA A 256  1  N  ALA A 256   O  ALA A  40           
SHEET    3  AB 6 TYR A 192  SER A 198 -1  O  GLN A 194   N  GLU A 255           
SHEET    4  AB 6 GLN A 206  PHE A 213 -1  N  GLY A 207   O  GLY A 197           
SHEET    5  AB 6 LEU A 140  GLU A 149  1  O  LEU A 140   N  ILE A 209           
SHEET    6  AB 6 VAL A 217  LEU A 219  1  O  VAL A 217   N  GLU A 148           
SHEET    1  AC 9 ALA A  40  PHE A  41  0                                        
SHEET    2  AC 9 GLU A 255  ALA A 256  1  N  ALA A 256   O  ALA A  40           
SHEET    3  AC 9 TYR A 192  SER A 198 -1  O  GLN A 194   N  GLU A 255           
SHEET    4  AC 9 GLN A 206  PHE A 213 -1  N  GLY A 207   O  GLY A 197           
SHEET    5  AC 9 LEU A 140  GLU A 149  1  O  LEU A 140   N  ILE A 209           
SHEET    6  AC 9 ALA A 116  SER A 124 -1  O  ALA A 116   N  LEU A 147           
SHEET    7  AC 9 ARG A  86  TRP A  97 -1  O  ARG A  89   N  LEU A 123           
SHEET    8  AC 9 GLU A  79  GLY A  83 -1  O  MET A  80   N  TYR A  88           
SHEET    9  AC 9 GLU A  49  LEU A  51  1  O  GLU A  49   N  ALA A  81           
SHEET    1  AD10 ALA A  40  PHE A  41  0                                        
SHEET    2  AD10 GLU A 255  ALA A 256  1  N  ALA A 256   O  ALA A  40           
SHEET    3  AD10 TYR A 192  SER A 198 -1  O  GLN A 194   N  GLU A 255           
SHEET    4  AD10 GLN A 206  PHE A 213 -1  N  GLY A 207   O  GLY A 197           
SHEET    5  AD10 LEU A 140  GLU A 149  1  O  LEU A 140   N  ILE A 209           
SHEET    6  AD10 ALA A 116  SER A 124 -1  O  ALA A 116   N  LEU A 147           
SHEET    7  AD10 ARG A  86  TRP A  97 -1  O  ARG A  89   N  LEU A 123           
SHEET    8  AD10 VAL A  70  THR A  73 -1  O  VAL A  70   N  LEU A  95           
SHEET    9  AD10 LEU A  61  ASN A  65 -1  O  ARG A  62   N  THR A  73           
SHEET   10  AD10 GLU A 173  VAL A 176 -1  O  THR A 174   N  LEU A  63           
SHEET    1  AE 2 VAL A 217  LEU A 219  0                                        
SHEET    2  AE 2 LEU A 140  GLU A 149  1  O  PHE A 146   N  VAL A 217           
SHEET    1  BA 2 ASP B  33  ILE B  34  0                                        
SHEET    2  BA 2 THR B 108  VAL B 109  1  O  THR B 108   N  ILE B  34           
SHEET    1  BB 6 ALA B  40  PHE B  41  0                                        
SHEET    2  BB 6 GLU B 255  ALA B 256  1  N  ALA B 256   O  ALA B  40           
SHEET    3  BB 6 TYR B 192  SER B 198 -1  O  GLN B 194   N  GLU B 255           
SHEET    4  BB 6 GLN B 206  PHE B 213 -1  N  GLY B 207   O  GLY B 197           
SHEET    5  BB 6 LEU B 140  GLU B 149  1  O  LEU B 140   N  ILE B 209           
SHEET    6  BB 6 VAL B 217  LEU B 219  1  O  VAL B 217   N  GLU B 148           
SHEET    1  BC 9 ALA B  40  PHE B  41  0                                        
SHEET    2  BC 9 GLU B 255  ALA B 256  1  N  ALA B 256   O  ALA B  40           
SHEET    3  BC 9 TYR B 192  SER B 198 -1  O  GLN B 194   N  GLU B 255           
SHEET    4  BC 9 GLN B 206  PHE B 213 -1  N  GLY B 207   O  GLY B 197           
SHEET    5  BC 9 LEU B 140  GLU B 149  1  O  LEU B 140   N  ILE B 209           
SHEET    6  BC 9 ALA B 116  SER B 124 -1  O  ALA B 116   N  LEU B 147           
SHEET    7  BC 9 ARG B  86  TRP B  97 -1  O  ARG B  89   N  LEU B 123           
SHEET    8  BC 9 GLU B  79  GLY B  83 -1  O  MET B  80   N  TYR B  88           
SHEET    9  BC 9 GLU B  49  LEU B  51  1  O  GLU B  49   N  ALA B  81           
SHEET    1  BD10 ALA B  40  PHE B  41  0                                        
SHEET    2  BD10 GLU B 255  ALA B 256  1  N  ALA B 256   O  ALA B  40           
SHEET    3  BD10 TYR B 192  SER B 198 -1  O  GLN B 194   N  GLU B 255           
SHEET    4  BD10 GLN B 206  PHE B 213 -1  N  GLY B 207   O  GLY B 197           
SHEET    5  BD10 LEU B 140  GLU B 149  1  O  LEU B 140   N  ILE B 209           
SHEET    6  BD10 ALA B 116  SER B 124 -1  O  ALA B 116   N  LEU B 147           
SHEET    7  BD10 ARG B  86  TRP B  97 -1  O  ARG B  89   N  LEU B 123           
SHEET    8  BD10 VAL B  70  THR B  73 -1  O  VAL B  70   N  LEU B  95           
SHEET    9  BD10 LEU B  61  ASN B  65 -1  O  ARG B  62   N  THR B  73           
SHEET   10  BD10 GLU B 173  VAL B 176 -1  O  THR B 174   N  LEU B  63           
SHEET    1  BE 2 VAL B 217  LEU B 219  0                                        
SHEET    2  BE 2 LEU B 140  GLU B 149  1  O  PHE B 146   N  VAL B 217           
SHEET    1  CA 2 ASP C  33  ILE C  34  0                                        
SHEET    2  CA 2 THR C 108  VAL C 109  1  O  THR C 108   N  ILE C  34           
SHEET    1  CB 6 ALA C  40  PHE C  41  0                                        
SHEET    2  CB 6 GLU C 255  ALA C 256  1  N  ALA C 256   O  ALA C  40           
SHEET    3  CB 6 TYR C 192  SER C 198 -1  O  GLN C 194   N  GLU C 255           
SHEET    4  CB 6 GLN C 206  PHE C 213 -1  N  GLY C 207   O  GLY C 197           
SHEET    5  CB 6 LEU C 140  GLU C 149  1  O  LEU C 140   N  ILE C 209           
SHEET    6  CB 6 VAL C 217  LEU C 219  1  O  VAL C 217   N  GLU C 148           
SHEET    1  CC 9 ALA C  40  PHE C  41  0                                        
SHEET    2  CC 9 GLU C 255  ALA C 256  1  N  ALA C 256   O  ALA C  40           
SHEET    3  CC 9 TYR C 192  SER C 198 -1  O  GLN C 194   N  GLU C 255           
SHEET    4  CC 9 GLN C 206  PHE C 213 -1  N  GLY C 207   O  GLY C 197           
SHEET    5  CC 9 LEU C 140  GLU C 149  1  O  LEU C 140   N  ILE C 209           
SHEET    6  CC 9 ALA C 116  SER C 124 -1  O  ALA C 116   N  LEU C 147           
SHEET    7  CC 9 ARG C  86  TRP C  97 -1  O  ARG C  89   N  LEU C 123           
SHEET    8  CC 9 GLU C  79  GLY C  83 -1  O  MET C  80   N  TYR C  88           
SHEET    9  CC 9 GLU C  49  LEU C  51  1  O  GLU C  49   N  ALA C  81           
SHEET    1  CD10 ALA C  40  PHE C  41  0                                        
SHEET    2  CD10 GLU C 255  ALA C 256  1  N  ALA C 256   O  ALA C  40           
SHEET    3  CD10 TYR C 192  SER C 198 -1  O  GLN C 194   N  GLU C 255           
SHEET    4  CD10 GLN C 206  PHE C 213 -1  N  GLY C 207   O  GLY C 197           
SHEET    5  CD10 LEU C 140  GLU C 149  1  O  LEU C 140   N  ILE C 209           
SHEET    6  CD10 ALA C 116  SER C 124 -1  O  ALA C 116   N  LEU C 147           
SHEET    7  CD10 ARG C  86  TRP C  97 -1  O  ARG C  89   N  LEU C 123           
SHEET    8  CD10 VAL C  70  THR C  73 -1  O  VAL C  70   N  LEU C  95           
SHEET    9  CD10 LEU C  61  ASN C  65 -1  O  ARG C  62   N  THR C  73           
SHEET   10  CD10 GLU C 173  VAL C 176 -1  O  THR C 174   N  LEU C  63           
SHEET    1  CE 2 VAL C 217  LEU C 219  0                                        
SHEET    2  CE 2 LEU C 140  GLU C 149  1  O  PHE C 146   N  VAL C 217           
SHEET    1  DA 2 ASP D  33  ILE D  34  0                                        
SHEET    2  DA 2 THR D 108  VAL D 109  1  O  THR D 108   N  ILE D  34           
SHEET    1  DB 6 ALA D  40  PHE D  41  0                                        
SHEET    2  DB 6 GLU D 255  ALA D 256  1  N  ALA D 256   O  ALA D  40           
SHEET    3  DB 6 TYR D 192  SER D 198 -1  O  GLN D 194   N  GLU D 255           
SHEET    4  DB 6 GLN D 206  PHE D 213 -1  N  GLY D 207   O  GLY D 197           
SHEET    5  DB 6 LEU D 140  GLY D 150  1  O  LEU D 140   N  ILE D 209           
SHEET    6  DB 6 VAL D 217  SER D 220  1  O  VAL D 217   N  GLU D 148           
SHEET    1  DC 9 ALA D  40  PHE D  41  0                                        
SHEET    2  DC 9 GLU D 255  ALA D 256  1  N  ALA D 256   O  ALA D  40           
SHEET    3  DC 9 TYR D 192  SER D 198 -1  O  GLN D 194   N  GLU D 255           
SHEET    4  DC 9 GLN D 206  PHE D 213 -1  N  GLY D 207   O  GLY D 197           
SHEET    5  DC 9 LEU D 140  GLY D 150  1  O  LEU D 140   N  ILE D 209           
SHEET    6  DC 9 ALA D 116  SER D 124 -1  O  ALA D 116   N  LEU D 147           
SHEET    7  DC 9 ARG D  86  TRP D  97 -1  O  ARG D  89   N  LEU D 123           
SHEET    8  DC 9 GLU D  79  GLY D  83 -1  O  MET D  80   N  TYR D  88           
SHEET    9  DC 9 GLU D  49  LEU D  51  1  O  GLU D  49   N  ALA D  81           
SHEET    1  DD10 ALA D  40  PHE D  41  0                                        
SHEET    2  DD10 GLU D 255  ALA D 256  1  N  ALA D 256   O  ALA D  40           
SHEET    3  DD10 TYR D 192  SER D 198 -1  O  GLN D 194   N  GLU D 255           
SHEET    4  DD10 GLN D 206  PHE D 213 -1  N  GLY D 207   O  GLY D 197           
SHEET    5  DD10 LEU D 140  GLY D 150  1  O  LEU D 140   N  ILE D 209           
SHEET    6  DD10 ALA D 116  SER D 124 -1  O  ALA D 116   N  LEU D 147           
SHEET    7  DD10 ARG D  86  TRP D  97 -1  O  ARG D  89   N  LEU D 123           
SHEET    8  DD10 VAL D  70  THR D  73 -1  O  VAL D  70   N  LEU D  95           
SHEET    9  DD10 LEU D  61  ASN D  65 -1  O  ARG D  62   N  THR D  73           
SHEET   10  DD10 GLU D 173  VAL D 176 -1  O  THR D 174   N  LEU D  63           
SHEET    1  DE 2 VAL D 217  SER D 220  0                                        
SHEET    2  DE 2 LEU D 140  GLY D 150  1  O  PHE D 146   N  VAL D 217           
SSBOND   1 CYS A   24    CYS A  204                          1555   1555  2.13  
SSBOND   2 CYS B   24    CYS B  204                          1555   1555  2.15  
SSBOND   3 CYS C   24    CYS C  204                          1555   1555  2.14  
SSBOND   4 CYS D   24    CYS D  204                          1555   1555  2.11  
LINK         N1  82E A 266                ZN    ZN A1260     1555   1555  2.00  
LINK        ZN    ZN A1260                 NE2 HIS A  96     1555   1555  2.13  
LINK        ZN    ZN A1260                 NE2 HIS A  94     1555   1555  2.15  
LINK        ZN    ZN A1260                 ND1 HIS A 119     1555   1555  2.15  
LINK         N1  82E B 267                ZN    ZN B1260     1555   1555  2.01  
LINK        ZN    ZN B1260                 NE2 HIS B  94     1555   1555  2.10  
LINK        ZN    ZN B1260                 ND1 HIS B 119     1555   1555  2.21  
LINK        ZN    ZN B1260                 NE2 HIS B  96     1555   1555  2.14  
LINK         N1  82E C 265                ZN    ZN C1260     1555   1555  2.12  
LINK         S2  82E C 265                ZN    ZN C1260     1555   1555  3.00  
LINK        ZN    ZN C1260                 NE2 HIS C  94     1555   1555  2.05  
LINK        ZN    ZN C1260                 ND1 HIS C 119     1555   1555  2.18  
LINK        ZN    ZN C1260                 NE2 HIS C  96     1555   1555  2.21  
LINK         N1  82E D 269                ZN    ZN D1260     1555   1555  1.97  
LINK         S2  82E D 269                ZN    ZN D1260     1555   1555  3.00  
LINK        ZN    ZN D1260                 NE2 HIS D  96     1555   1555  2.12  
LINK        ZN    ZN D1260                 ND1 HIS D 119     1555   1555  2.11  
LINK        ZN    ZN D1260                 NE2 HIS D  94     1555   1555  2.14  
CISPEP   1 ASP A   14    PRO A   15          0         3.40                     
CISPEP   2 SER A   30    PRO A   31          0         0.49                     
CISPEP   3 LEU A   58    PRO A   59          0         1.13                     
CISPEP   4 PRO A  202    PRO A  203          0        12.26                     
CISPEP   5 ASP B   14    PRO B   15          0        -4.97                     
CISPEP   6 SER B   30    PRO B   31          0         2.44                     
CISPEP   7 LEU B   58    PRO B   59          0         5.96                     
CISPEP   8 PRO B  202    PRO B  203          0         8.19                     
CISPEP   9 ASP C   14    PRO C   15          0        -1.38                     
CISPEP  10 SER C   30    PRO C   31          0         2.49                     
CISPEP  11 LEU C   58    PRO C   59          0         6.57                     
CISPEP  12 PRO C  202    PRO C  203          0        13.06                     
CISPEP  13 ASP D   14    PRO D   15          0         5.30                     
CISPEP  14 SER D   30    PRO D   31          0         0.11                     
CISPEP  15 LEU D   58    PRO D   59          0        -0.12                     
CISPEP  16 PRO D  202    PRO D  203          0         7.00                     
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  82E A 266                    
SITE     1 AC2 14 GLN A  92  HIS A  94  HIS A  96  HIS A 119                    
SITE     2 AC2 14 VAL A 130  ASP A 131  LEU A 199  THR A 200                    
SITE     3 AC2 14 THR A 201  TRP A 210   ZN A1260  GOL A1261                    
SITE     4 AC2 14 HOH A2276  ARG D 129                                          
SITE     1 AC3  9 ASN A  66  SER A  69  GLN A  71  GLN A  92                    
SITE     2 AC3  9 HIS A  94  THR A 201  82E A 266  HOH A2006                    
SITE     3 AC3  9 HOH A2097                                                     
SITE     1 AC4  4 HIS B  94  HIS B  96  HIS B 119  82E B 267                    
SITE     1 AC5 12 HIS B  94  HIS B  96  HIS B 119  VAL B 130                    
SITE     2 AC5 12 LEU B 134  LEU B 199  THR B 200  THR B 201                    
SITE     3 AC5 12 TRP B 210   ZN B1260  GOL B1261  HOH B2128                    
SITE     1 AC6 10 ASN B  66  HIS B  68  SER B  69  GLN B  71                    
SITE     2 AC6 10 GLN B  92  HIS B  94  82E B 267  HOH B2006                    
SITE     3 AC6 10 HOH B2097  HOH B2214                                          
SITE     1 AC7  4 HIS C  94  HIS C  96  HIS C 119  82E C 265                    
SITE     1 AC8 12 GLU A 173  THR A 174  HIS C  94  HIS C  96                    
SITE     2 AC8 12 HIS C 119  LEU C 134  LEU C 199  THR C 200                    
SITE     3 AC8 12 THR C 201  TRP C 210   ZN C1260  HOH C2089                    
SITE     1 AC9  9 ASN C  66  HIS C  68  SER C  69  GLN C  71                    
SITE     2 AC9  9 GLN C  92  HIS C  94  HOH C2003  HOH C2062                    
SITE     3 AC9  9 HOH C2151                                                     
SITE     1 BC1  4 HIS D  94  HIS D  96  HIS D 119  82E D 269                    
SITE     1 BC2 11 GLN D  92  HIS D  94  HIS D  96  HIS D 119                    
SITE     2 BC2 11 LEU D 199  THR D 200  THR D 201  TRP D 210                    
SITE     3 BC2 11  ZN D1260  GOL D1261  HOH D2177                               
SITE     1 BC3  9 ASN D  66  SER D  69  GLN D  71  GLN D  92                    
SITE     2 BC3  9 HIS D  94  THR D 201  82E D 269  HOH D2006                    
SITE     3 BC3  9 HOH D2066                                                     
SITE     1 BC4  4 ARG C 244  GLN C 247  HOH C2179  HOH C2180                    
SITE     1 BC5  6 SER B 155  HOH B2175  HOH B2246  ARG D 244                    
SITE     2 BC5  6 GLN D 247  TRS D1265                                          
SITE     1 BC6  6 ARG A 244  GLN A 247  TRS A1270  HOH A2277                    
SITE     2 BC6  6 HOH A2278  SER C 155                                          
SITE     1 BC7  7 SER B 187  ARG D  35  PRO D 248  LEU D 249                    
SITE     2 BC7  7 ASN D 250  HOH D2027  HOH D2171                               
SITE     1 BC8  9 ARG A  35  PRO A 248  LEU A 249  ASN A 250                    
SITE     2 BC8  9 HOH A2041  HOH A2264  HOH A2279  HOH A2280                    
SITE     3 BC8  9 SER C 187                                                     
SITE     1 BC9  6 PRO B  18  ARG B 244  GLN B 247  TRS B1267                    
SITE     2 BC9  6 HOH B2026  HOH B2247                                          
SITE     1 CC1  9 LEU A  51  GLY A  52  PHE A  53  GLN A  54                    
SITE     2 CC1  9 GLN A 215  HOH A2072  HOH A2214  HOH A2245                    
SITE     3 CC1  9 HOH A2281                                                     
SITE     1 CC2  5 GLY D  52  PHE D  53  GLN D  54  HOH D2048                    
SITE     2 CC2  5 HOH D2051                                                     
SITE     1 CC3 10 PRO C  84  GLY C  85  ARG C  86  HOH C2073                    
SITE     2 CC3 10 PHE D  28  GLU D 196  GLN D 206  GLY D 207                    
SITE     3 CC3 10 ARG D 252  HOH D2152                                          
SITE     1 CC4  4 VAL A 109  PHE A 114  ASN A 214  HOH A2242                    
SITE     1 CC5  3 PRO C 248  LEU C 249  ASN C 250                               
SITE     1 CC6  6 GLY B  26  ARG B  27  PHE B  28  GLN B 206                    
SITE     2 CC6  6 HOH B2248  HOH B2249                                          
SITE     1 CC7  6 GLY A  12  LEU A 241  PHE A 243  TRS A1270                    
SITE     2 CC7  6 HOH A2007  HOH A2284                                          
SITE     1 CC8  6 GLY B  12  LEU B 241  PHE B 243  ALA B 245                    
SITE     2 CC8  6 TRS B1267  HOH B2250                                          
SITE     1 CC9  7 ARG A  27  PHE A  28  ASN A 250  HOH A2285                    
SITE     2 CC9  7 HOH A2287  PRO B  84  PHE C 189                               
SITE     1 DC1  5 GLU A  49  LEU A  51  GLU A  79  ARG A 191                    
SITE     2 DC1  5 HOH A2229                                                     
SITE     1 DC2  6 GLY C  98  ALA C  99  ARG C 102  PRO C 115                    
SITE     2 DC2  6 LEU C 224  SER C 228                                          
SITE     1 DC3  7 GLY A  98  ALA A  99  ARG A 102  PRO A 115                    
SITE     2 DC3  7 LEU A 224  SER A 228  HOH A2289                               
SITE     1 DC4  3 VAL B 109  PHE B 114  ASN B 214                               
SITE     1 DC5  9 GLY B  12  PRO B  16  TRP B  17  ARG B 244                    
SITE     2 DC5  9 ALA B 245  SO4 B1263  SO4 B1265  HOH B2003                    
SITE     3 DC5  9 HOH B2250                                                     
SITE     1 DC6 10 TYR A  11  GLY A  12  TRP A  17  ARG A 244                    
SITE     2 DC6 10 ALA A 245  SO4 A1262  SO4 A1266  HOH A2002                    
SITE     3 DC6 10 HOH A2011  HOH A2284                                          
SITE     1 DC7 10 SO4 B1262  TYR D  11  GLY D  12  TRP D  17                    
SITE     2 DC7 10 ARG D 244  ALA D 245  HOH D2004  HOH D2009                    
SITE     3 DC7 10 HOH D2170  HOH D2179                                          
CRYST1  152.380  152.380  170.590  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  0.005862        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system