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Database: PDB
Entry: 1U1Z
LinkDB: 1U1Z
Original site: 1U1Z 
HEADER    LYASE                                   16-JUL-04   1U1Z              
TITLE     THE STRUCTURE OF (3R)-HYDROXYACYL-ACP DEHYDRATASE (FABZ)              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: (3R)-HYDROXYMYRISTOYL-[ACYL CARRIER PROTEIN]               
COMPND   3 DEHYDRATASE;                                                         
COMPND   4 CHAIN: A, B, C, D, E, F;                                             
COMPND   5 SYNONYM: (3R)-HYDROXYMYRISTOYL ACP DEHYDRASE;                        
COMPND   6 EC: 4.2.1.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 GENE: FABZ;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-GOLD;                            
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    DEHYDRATASE; FATTY ACID BIOSYNTHESIS; HOT DOG FOLD, LYASE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.S.KIMBER,F.MARTIN,Y.LU,S.HOUSTON,M.VEDADI,A.DHARAMSI,               
AUTHOR   2 K.M.FIEBIG,M.SCHMID,C.O.ROCK                                         
REVDAT   3   24-FEB-09 1U1Z    1       VERSN                                    
REVDAT   2   25-JAN-05 1U1Z    1       JRNL                                     
REVDAT   1   28-SEP-04 1U1Z    0                                                
JRNL        AUTH   M.S.KIMBER,F.MARTIN,Y.LU,S.HOUSTON,M.VEDADI,                 
JRNL        AUTH 2 A.DHARAMSI,K.M.FIEBIG,M.SCHMID,C.O.ROCK                      
JRNL        TITL   THE STRUCTURE OF (3R)-HYDROXYACYL-ACYL CARRIER               
JRNL        TITL 2 PROTEIN DEHYDRATASE (FABZ) FROM PSEUDOMONAS                  
JRNL        TITL 3 AERUGINOSA                                                   
JRNL        REF    J.BIOL.CHEM.                  V. 279 52593 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15371447                                                     
JRNL        DOI    10.1074/JBC.M408105200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2000.1                                           
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN,MOLECULAR                  
REMARK   3               : SIMULATIONS (BADGER,BERARD,KUMAR,SZALMA,             
REMARK   3               : YIP,DZAKULA)                                         
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.35                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 57672                          
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) : 0.234                           
REMARK   3   R VALUE            (WORKING SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.200                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 5873                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 111343               
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.61                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 8336                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.20                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 960                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7033                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 227                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -13.69000                                            
REMARK   3    B22 (A**2) : -9.49000                                             
REMARK   3    B33 (A**2) : 23.18000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.33                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.47                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.37                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.51                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1U1Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB023145.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 32-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97943                            
REMARK 200  MONOCHROMATOR                  : DIAMOND                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 108745                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.490                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.28200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: CNX 2000.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: FRIEDEL PAIRS WERE USED TO SOLVE THIS STRUCTURE.             
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, PH 5.5, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       46.51550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.62600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.44850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.62600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       46.51550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       50.44850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE SIX CHAINS IN THE ASYMMETRIC UNIT COMPRISE THE           
REMARK 300 BIOLOGICAL HEXAMER                                                   
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16170 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 33600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -112.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     ALA A    82                                                      
REMARK 465     ASP A    83                                                      
REMARK 465     GLY A    84                                                      
REMARK 465     LEU A   146                                                      
REMARK 465     GLY A   147                                                      
REMARK 465     SER A   148                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     GLY B   147                                                      
REMARK 465     SER B   148                                                      
REMARK 465     MET C   -19                                                      
REMARK 465     GLY C   -18                                                      
REMARK 465     SER C   -17                                                      
REMARK 465     SER C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     GLY C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     VAL C    -5                                                      
REMARK 465     PRO C    -4                                                      
REMARK 465     ARG C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     PRO C    81                                                      
REMARK 465     ALA C    82                                                      
REMARK 465     MET D   -19                                                      
REMARK 465     GLY D   -18                                                      
REMARK 465     SER D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     GLY D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     VAL D    -5                                                      
REMARK 465     PRO D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     ALA D    82                                                      
REMARK 465     ASP D    83                                                      
REMARK 465     GLY D   147                                                      
REMARK 465     SER D   148                                                      
REMARK 465     MET E   -19                                                      
REMARK 465     GLY E   -18                                                      
REMARK 465     SER E   -17                                                      
REMARK 465     SER E   -16                                                      
REMARK 465     HIS E   -15                                                      
REMARK 465     HIS E   -14                                                      
REMARK 465     HIS E   -13                                                      
REMARK 465     HIS E   -12                                                      
REMARK 465     HIS E   -11                                                      
REMARK 465     HIS E   -10                                                      
REMARK 465     SER E    -9                                                      
REMARK 465     SER E    -8                                                      
REMARK 465     GLY E    -7                                                      
REMARK 465     LEU E    -6                                                      
REMARK 465     VAL E    -5                                                      
REMARK 465     PRO E    -4                                                      
REMARK 465     ARG E    -3                                                      
REMARK 465     GLY E    -2                                                      
REMARK 465     SER E    -1                                                      
REMARK 465     HIS E     0                                                      
REMARK 465     ASP E    83                                                      
REMARK 465     GLY E   147                                                      
REMARK 465     SER E   148                                                      
REMARK 465     MET F   -19                                                      
REMARK 465     GLY F   -18                                                      
REMARK 465     SER F   -17                                                      
REMARK 465     SER F   -16                                                      
REMARK 465     HIS F   -15                                                      
REMARK 465     HIS F   -14                                                      
REMARK 465     HIS F   -13                                                      
REMARK 465     HIS F   -12                                                      
REMARK 465     HIS F   -11                                                      
REMARK 465     HIS F   -10                                                      
REMARK 465     SER F    -9                                                      
REMARK 465     SER F    -8                                                      
REMARK 465     GLY F    -7                                                      
REMARK 465     LEU F    -6                                                      
REMARK 465     VAL F    -5                                                      
REMARK 465     PRO F    -4                                                      
REMARK 465     ARG F    -3                                                      
REMARK 465     GLY F    -2                                                      
REMARK 465     SER F    -1                                                      
REMARK 465     HIS F     0                                                      
REMARK 465     GLY F   147                                                      
REMARK 465     SER F   148                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A   8        2.80    -68.14                                   
REMARK 500    PRO A  16       43.94    -99.01                                   
REMARK 500    ASN A  42       41.90    -90.45                                   
REMARK 500    HIS A  49       74.53   -154.91                                   
REMARK 500    GLU A  52      -18.40     77.51                                   
REMARK 500    TYR A  87       78.10   -102.44                                   
REMARK 500    PRO B  16       41.61    -99.63                                   
REMARK 500    ASN B  42       44.40    -80.56                                   
REMARK 500    HIS B  53       77.29   -152.12                                   
REMARK 500    PRO B  81     -150.33    -25.31                                   
REMARK 500    ALA B  82       93.67    -24.87                                   
REMARK 500    GLN B  99      143.75    178.40                                   
REMARK 500    ARG B 118      -99.92     66.38                                   
REMARK 500    ASP B 131       -2.00     66.65                                   
REMARK 500    VAL B 134      -40.17   -137.13                                   
REMARK 500    PRO C  16       45.47    -99.24                                   
REMARK 500    ASN C  42       37.35    -82.90                                   
REMARK 500    GLU C  52       -2.33     78.40                                   
REMARK 500    HIS C  53       76.60   -152.88                                   
REMARK 500    THR C  85      145.13    -20.11                                   
REMARK 500    TYR C  88      107.48    -58.23                                   
REMARK 500    PHE C  89      106.69    -56.38                                   
REMARK 500    SER C  92      129.38   -174.25                                   
REMARK 500    ARG C  98      -85.85   -113.97                                   
REMARK 500    VAL C 116      102.71   -160.63                                   
REMARK 500    ASP C 131       -5.30     66.26                                   
REMARK 500    PRO D  16       47.64   -102.16                                   
REMARK 500    ASN D  42       45.75    -92.15                                   
REMARK 500    HIS D  53       77.57   -153.58                                   
REMARK 500    LYS D  80       70.88   -118.11                                   
REMARK 500    LYS D  94       56.71     28.93                                   
REMARK 500    ARG D 118     -114.01     64.51                                   
REMARK 500    ASP D 131       19.44     59.60                                   
REMARK 500    PRO E  16       43.40    -99.50                                   
REMARK 500    ASN E  42       42.07    -80.26                                   
REMARK 500    GLU E  52      -12.76     77.47                                   
REMARK 500    ASP E  78       47.28     34.42                                   
REMARK 500    PRO E  81      172.96    -36.25                                   
REMARK 500    ASP E  93     -106.50   -105.07                                   
REMARK 500    ARG E  98     -112.10   -118.31                                   
REMARK 500    ILE E 114      -88.39   -107.96                                   
REMARK 500    SER E 115     -156.81   -122.35                                   
REMARK 500    VAL E 116       93.31    175.35                                   
REMARK 500    ARG E 118     -105.47     81.94                                   
REMARK 500    ASP E 131      -29.50     76.92                                   
REMARK 500    PRO F  16       46.81   -101.82                                   
REMARK 500    ARG F  22      141.95   -170.65                                   
REMARK 500    ASN F  42       47.75    -83.13                                   
REMARK 500    HIS F  53       70.43   -153.76                                   
REMARK 500    ASP F  78       46.84     14.98                                   
REMARK 500    PRO F  81       50.54    -62.65                                   
REMARK 500    ASP F  83       45.19   -178.88                                   
REMARK 500    SER F  92      135.36   -173.44                                   
REMARK 500    LYS F  94       99.40     32.24                                   
REMARK 500    GLN F  99      144.08    173.83                                   
REMARK 500    ILE F 114      -81.24   -123.24                                   
REMARK 500    SER F 115     -158.49   -121.15                                   
REMARK 500    VAL F 116       78.43    169.66                                   
REMARK 500    ARG F 118     -118.55     83.91                                   
REMARK 500    ASP F 131       -1.89     55.51                                   
REMARK 500    GLU F 143      118.88    -35.64                                   
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 E 170        DISTANCE =  5.15 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 500                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 501                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 502                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 503                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 504                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MKA   RELATED DB: PDB                                   
REMARK 900 RELATED DEHYDRATASE/ISOMERASE                                        
REMARK 900 RELATED ID: 1MKB   RELATED DB: PDB                                   
REMARK 900 RELATED DEHYDRATASE/ISOMERASE                                        
DBREF  1U1Z A    1   146  UNP    Q9HXY7   FABZ_PSEAE       1    146             
DBREF  1U1Z B    1   146  UNP    Q9HXY7   FABZ_PSEAE       1    146             
DBREF  1U1Z C    1   146  UNP    Q9HXY7   FABZ_PSEAE       1    146             
DBREF  1U1Z D    1   146  UNP    Q9HXY7   FABZ_PSEAE       1    146             
DBREF  1U1Z E    1   146  UNP    Q9HXY7   FABZ_PSEAE       1    146             
DBREF  1U1Z F    1   146  UNP    Q9HXY7   FABZ_PSEAE       1    146             
SEQADV 1U1Z MET A  -19  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY A  -18  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER A  -17  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER A  -16  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS A  -15  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS A  -14  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS A  -13  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS A  -12  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS A  -11  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS A  -10  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER A   -9  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER A   -8  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY A   -7  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z LEU A   -6  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z VAL A   -5  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z PRO A   -4  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z ARG A   -3  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY A   -2  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER A   -1  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS A    0  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z MSE A    1  UNP  Q9HXY7    MET     1 MODIFIED RESIDUE               
SEQADV 1U1Z MSE A    2  UNP  Q9HXY7    MET     2 MODIFIED RESIDUE               
SEQADV 1U1Z MSE A   56  UNP  Q9HXY7    MET    56 MODIFIED RESIDUE               
SEQADV 1U1Z MSE A   65  UNP  Q9HXY7    MET    65 MODIFIED RESIDUE               
SEQADV 1U1Z MSE A   76  UNP  Q9HXY7    MET    76 MODIFIED RESIDUE               
SEQADV 1U1Z GLY A  147  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER A  148  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z MET B  -19  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY B  -18  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER B  -17  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER B  -16  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS B  -15  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS B  -14  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS B  -13  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS B  -12  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS B  -11  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS B  -10  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER B   -9  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER B   -8  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY B   -7  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z LEU B   -6  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z VAL B   -5  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z PRO B   -4  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z ARG B   -3  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY B   -2  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER B   -1  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS B    0  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z MSE B    1  UNP  Q9HXY7    MET     1 MODIFIED RESIDUE               
SEQADV 1U1Z MSE B    2  UNP  Q9HXY7    MET     2 MODIFIED RESIDUE               
SEQADV 1U1Z MSE B   56  UNP  Q9HXY7    MET    56 MODIFIED RESIDUE               
SEQADV 1U1Z MSE B   65  UNP  Q9HXY7    MET    65 MODIFIED RESIDUE               
SEQADV 1U1Z MSE B   76  UNP  Q9HXY7    MET    76 MODIFIED RESIDUE               
SEQADV 1U1Z GLY B  147  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER B  148  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z MET C  -19  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY C  -18  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER C  -17  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER C  -16  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS C  -15  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS C  -14  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS C  -13  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS C  -12  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS C  -11  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS C  -10  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER C   -9  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER C   -8  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY C   -7  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z LEU C   -6  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z VAL C   -5  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z PRO C   -4  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z ARG C   -3  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY C   -2  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER C   -1  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS C    0  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z MSE C    1  UNP  Q9HXY7    MET     1 MODIFIED RESIDUE               
SEQADV 1U1Z MSE C    2  UNP  Q9HXY7    MET     2 MODIFIED RESIDUE               
SEQADV 1U1Z MSE C   56  UNP  Q9HXY7    MET    56 MODIFIED RESIDUE               
SEQADV 1U1Z MSE C   65  UNP  Q9HXY7    MET    65 MODIFIED RESIDUE               
SEQADV 1U1Z MSE C   76  UNP  Q9HXY7    MET    76 MODIFIED RESIDUE               
SEQADV 1U1Z GLY C  147  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER C  148  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z MET D  -19  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY D  -18  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER D  -17  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER D  -16  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS D  -15  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS D  -14  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS D  -13  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS D  -12  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS D  -11  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS D  -10  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER D   -9  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER D   -8  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY D   -7  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z LEU D   -6  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z VAL D   -5  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z PRO D   -4  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z ARG D   -3  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY D   -2  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER D   -1  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS D    0  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z MSE D    1  UNP  Q9HXY7    MET     1 MODIFIED RESIDUE               
SEQADV 1U1Z MSE D    2  UNP  Q9HXY7    MET     2 MODIFIED RESIDUE               
SEQADV 1U1Z MSE D   56  UNP  Q9HXY7    MET    56 MODIFIED RESIDUE               
SEQADV 1U1Z MSE D   65  UNP  Q9HXY7    MET    65 MODIFIED RESIDUE               
SEQADV 1U1Z MSE D   76  UNP  Q9HXY7    MET    76 MODIFIED RESIDUE               
SEQADV 1U1Z GLY D  147  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER D  148  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z MET E  -19  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY E  -18  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER E  -17  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER E  -16  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS E  -15  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS E  -14  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS E  -13  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS E  -12  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS E  -11  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS E  -10  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER E   -9  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER E   -8  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY E   -7  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z LEU E   -6  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z VAL E   -5  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z PRO E   -4  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z ARG E   -3  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY E   -2  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER E   -1  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS E    0  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z MSE E    1  UNP  Q9HXY7    MET     1 MODIFIED RESIDUE               
SEQADV 1U1Z MSE E    2  UNP  Q9HXY7    MET     2 MODIFIED RESIDUE               
SEQADV 1U1Z MSE E   56  UNP  Q9HXY7    MET    56 MODIFIED RESIDUE               
SEQADV 1U1Z MSE E   65  UNP  Q9HXY7    MET    65 MODIFIED RESIDUE               
SEQADV 1U1Z MSE E   76  UNP  Q9HXY7    MET    76 MODIFIED RESIDUE               
SEQADV 1U1Z GLY E  147  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER E  148  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z MET F  -19  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY F  -18  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER F  -17  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER F  -16  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS F  -15  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS F  -14  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS F  -13  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS F  -12  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS F  -11  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS F  -10  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER F   -9  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER F   -8  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY F   -7  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z LEU F   -6  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z VAL F   -5  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z PRO F   -4  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z ARG F   -3  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z GLY F   -2  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER F   -1  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z HIS F    0  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z MSE F    1  UNP  Q9HXY7    MET     1 MODIFIED RESIDUE               
SEQADV 1U1Z MSE F    2  UNP  Q9HXY7    MET     2 MODIFIED RESIDUE               
SEQADV 1U1Z MSE F   56  UNP  Q9HXY7    MET    56 MODIFIED RESIDUE               
SEQADV 1U1Z MSE F   65  UNP  Q9HXY7    MET    65 MODIFIED RESIDUE               
SEQADV 1U1Z MSE F   76  UNP  Q9HXY7    MET    76 MODIFIED RESIDUE               
SEQADV 1U1Z GLY F  147  UNP  Q9HXY7              CLONING ARTIFACT               
SEQADV 1U1Z SER F  148  UNP  Q9HXY7              CLONING ARTIFACT               
SEQRES   1 A  168  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  168  LEU VAL PRO ARG GLY SER HIS MSE MSE ASP ILE ASN GLU          
SEQRES   3 A  168  ILE ARG GLU TYR LEU PRO HIS ARG TYR PRO PHE LEU LEU          
SEQRES   4 A  168  VAL ASP ARG VAL VAL GLU LEU ASP ILE GLU GLY LYS ARG          
SEQRES   5 A  168  ILE ARG ALA TYR LYS ASN VAL SER ILE ASN GLU PRO PHE          
SEQRES   6 A  168  PHE ASN GLY HIS PHE PRO GLU HIS PRO ILE MSE PRO GLY          
SEQRES   7 A  168  VAL LEU ILE ILE GLU ALA MSE ALA GLN ALA ALA GLY ILE          
SEQRES   8 A  168  LEU GLY PHE LYS MSE LEU ASP VAL LYS PRO ALA ASP GLY          
SEQRES   9 A  168  THR LEU TYR TYR PHE VAL GLY SER ASP LYS LEU ARG PHE          
SEQRES  10 A  168  ARG GLN PRO VAL LEU PRO GLY ASP GLN LEU GLN LEU HIS          
SEQRES  11 A  168  ALA LYS PHE ILE SER VAL LYS ARG SER ILE TRP LYS PHE          
SEQRES  12 A  168  ASP CYS HIS ALA THR VAL ASP ASP LYS PRO VAL CYS SER          
SEQRES  13 A  168  ALA GLU ILE ILE CYS ALA GLU ARG LYS LEU GLY SER              
SEQRES   1 B  168  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  168  LEU VAL PRO ARG GLY SER HIS MSE MSE ASP ILE ASN GLU          
SEQRES   3 B  168  ILE ARG GLU TYR LEU PRO HIS ARG TYR PRO PHE LEU LEU          
SEQRES   4 B  168  VAL ASP ARG VAL VAL GLU LEU ASP ILE GLU GLY LYS ARG          
SEQRES   5 B  168  ILE ARG ALA TYR LYS ASN VAL SER ILE ASN GLU PRO PHE          
SEQRES   6 B  168  PHE ASN GLY HIS PHE PRO GLU HIS PRO ILE MSE PRO GLY          
SEQRES   7 B  168  VAL LEU ILE ILE GLU ALA MSE ALA GLN ALA ALA GLY ILE          
SEQRES   8 B  168  LEU GLY PHE LYS MSE LEU ASP VAL LYS PRO ALA ASP GLY          
SEQRES   9 B  168  THR LEU TYR TYR PHE VAL GLY SER ASP LYS LEU ARG PHE          
SEQRES  10 B  168  ARG GLN PRO VAL LEU PRO GLY ASP GLN LEU GLN LEU HIS          
SEQRES  11 B  168  ALA LYS PHE ILE SER VAL LYS ARG SER ILE TRP LYS PHE          
SEQRES  12 B  168  ASP CYS HIS ALA THR VAL ASP ASP LYS PRO VAL CYS SER          
SEQRES  13 B  168  ALA GLU ILE ILE CYS ALA GLU ARG LYS LEU GLY SER              
SEQRES   1 C  168  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  168  LEU VAL PRO ARG GLY SER HIS MSE MSE ASP ILE ASN GLU          
SEQRES   3 C  168  ILE ARG GLU TYR LEU PRO HIS ARG TYR PRO PHE LEU LEU          
SEQRES   4 C  168  VAL ASP ARG VAL VAL GLU LEU ASP ILE GLU GLY LYS ARG          
SEQRES   5 C  168  ILE ARG ALA TYR LYS ASN VAL SER ILE ASN GLU PRO PHE          
SEQRES   6 C  168  PHE ASN GLY HIS PHE PRO GLU HIS PRO ILE MSE PRO GLY          
SEQRES   7 C  168  VAL LEU ILE ILE GLU ALA MSE ALA GLN ALA ALA GLY ILE          
SEQRES   8 C  168  LEU GLY PHE LYS MSE LEU ASP VAL LYS PRO ALA ASP GLY          
SEQRES   9 C  168  THR LEU TYR TYR PHE VAL GLY SER ASP LYS LEU ARG PHE          
SEQRES  10 C  168  ARG GLN PRO VAL LEU PRO GLY ASP GLN LEU GLN LEU HIS          
SEQRES  11 C  168  ALA LYS PHE ILE SER VAL LYS ARG SER ILE TRP LYS PHE          
SEQRES  12 C  168  ASP CYS HIS ALA THR VAL ASP ASP LYS PRO VAL CYS SER          
SEQRES  13 C  168  ALA GLU ILE ILE CYS ALA GLU ARG LYS LEU GLY SER              
SEQRES   1 D  168  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  168  LEU VAL PRO ARG GLY SER HIS MSE MSE ASP ILE ASN GLU          
SEQRES   3 D  168  ILE ARG GLU TYR LEU PRO HIS ARG TYR PRO PHE LEU LEU          
SEQRES   4 D  168  VAL ASP ARG VAL VAL GLU LEU ASP ILE GLU GLY LYS ARG          
SEQRES   5 D  168  ILE ARG ALA TYR LYS ASN VAL SER ILE ASN GLU PRO PHE          
SEQRES   6 D  168  PHE ASN GLY HIS PHE PRO GLU HIS PRO ILE MSE PRO GLY          
SEQRES   7 D  168  VAL LEU ILE ILE GLU ALA MSE ALA GLN ALA ALA GLY ILE          
SEQRES   8 D  168  LEU GLY PHE LYS MSE LEU ASP VAL LYS PRO ALA ASP GLY          
SEQRES   9 D  168  THR LEU TYR TYR PHE VAL GLY SER ASP LYS LEU ARG PHE          
SEQRES  10 D  168  ARG GLN PRO VAL LEU PRO GLY ASP GLN LEU GLN LEU HIS          
SEQRES  11 D  168  ALA LYS PHE ILE SER VAL LYS ARG SER ILE TRP LYS PHE          
SEQRES  12 D  168  ASP CYS HIS ALA THR VAL ASP ASP LYS PRO VAL CYS SER          
SEQRES  13 D  168  ALA GLU ILE ILE CYS ALA GLU ARG LYS LEU GLY SER              
SEQRES   1 E  168  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 E  168  LEU VAL PRO ARG GLY SER HIS MSE MSE ASP ILE ASN GLU          
SEQRES   3 E  168  ILE ARG GLU TYR LEU PRO HIS ARG TYR PRO PHE LEU LEU          
SEQRES   4 E  168  VAL ASP ARG VAL VAL GLU LEU ASP ILE GLU GLY LYS ARG          
SEQRES   5 E  168  ILE ARG ALA TYR LYS ASN VAL SER ILE ASN GLU PRO PHE          
SEQRES   6 E  168  PHE ASN GLY HIS PHE PRO GLU HIS PRO ILE MSE PRO GLY          
SEQRES   7 E  168  VAL LEU ILE ILE GLU ALA MSE ALA GLN ALA ALA GLY ILE          
SEQRES   8 E  168  LEU GLY PHE LYS MSE LEU ASP VAL LYS PRO ALA ASP GLY          
SEQRES   9 E  168  THR LEU TYR TYR PHE VAL GLY SER ASP LYS LEU ARG PHE          
SEQRES  10 E  168  ARG GLN PRO VAL LEU PRO GLY ASP GLN LEU GLN LEU HIS          
SEQRES  11 E  168  ALA LYS PHE ILE SER VAL LYS ARG SER ILE TRP LYS PHE          
SEQRES  12 E  168  ASP CYS HIS ALA THR VAL ASP ASP LYS PRO VAL CYS SER          
SEQRES  13 E  168  ALA GLU ILE ILE CYS ALA GLU ARG LYS LEU GLY SER              
SEQRES   1 F  168  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 F  168  LEU VAL PRO ARG GLY SER HIS MSE MSE ASP ILE ASN GLU          
SEQRES   3 F  168  ILE ARG GLU TYR LEU PRO HIS ARG TYR PRO PHE LEU LEU          
SEQRES   4 F  168  VAL ASP ARG VAL VAL GLU LEU ASP ILE GLU GLY LYS ARG          
SEQRES   5 F  168  ILE ARG ALA TYR LYS ASN VAL SER ILE ASN GLU PRO PHE          
SEQRES   6 F  168  PHE ASN GLY HIS PHE PRO GLU HIS PRO ILE MSE PRO GLY          
SEQRES   7 F  168  VAL LEU ILE ILE GLU ALA MSE ALA GLN ALA ALA GLY ILE          
SEQRES   8 F  168  LEU GLY PHE LYS MSE LEU ASP VAL LYS PRO ALA ASP GLY          
SEQRES   9 F  168  THR LEU TYR TYR PHE VAL GLY SER ASP LYS LEU ARG PHE          
SEQRES  10 F  168  ARG GLN PRO VAL LEU PRO GLY ASP GLN LEU GLN LEU HIS          
SEQRES  11 F  168  ALA LYS PHE ILE SER VAL LYS ARG SER ILE TRP LYS PHE          
SEQRES  12 F  168  ASP CYS HIS ALA THR VAL ASP ASP LYS PRO VAL CYS SER          
SEQRES  13 F  168  ALA GLU ILE ILE CYS ALA GLU ARG LYS LEU GLY SER              
MODRES 1U1Z MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE A    2  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE A   56  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE A   65  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE A   76  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE B    2  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE B   56  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE B   65  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE B   76  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE C    1  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE C    2  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE C   56  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE C   65  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE C   76  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE D    1  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE D    2  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE D   56  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE D   65  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE D   76  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE E    1  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE E    2  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE E   56  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE E   65  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE E   76  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE F    1  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE F    2  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE F   56  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE F   65  MET  SELENOMETHIONINE                                   
MODRES 1U1Z MSE F   76  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A   2       8                                                       
HET    MSE  A  56       8                                                       
HET    MSE  A  65       8                                                       
HET    MSE  A  76       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B   2       8                                                       
HET    MSE  B  56       8                                                       
HET    MSE  B  65       8                                                       
HET    MSE  B  76       8                                                       
HET    MSE  C   1       8                                                       
HET    MSE  C   2       8                                                       
HET    MSE  C  56       8                                                       
HET    MSE  C  65       8                                                       
HET    MSE  C  76       8                                                       
HET    MSE  D   1       8                                                       
HET    MSE  D   2       8                                                       
HET    MSE  D  56       8                                                       
HET    MSE  D  65       8                                                       
HET    MSE  D  76       8                                                       
HET    MSE  E   1       8                                                       
HET    MSE  E   2       8                                                       
HET    MSE  E  56       8                                                       
HET    MSE  E  65       8                                                       
HET    MSE  E  76       8                                                       
HET    MSE  F   1       8                                                       
HET    MSE  F   2       8                                                       
HET    MSE  F  56       8                                                       
HET    MSE  F  65       8                                                       
HET    MSE  F  76       8                                                       
HET    SO4  D 500       5                                                       
HET    SO4  D 501       5                                                       
HET    SO4  D 502       5                                                       
HET    SO4  D 503       5                                                       
HET    SO4  D 504       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    30(C5 H11 N O2 SE)                                           
FORMUL   7  SO4    5(O4 S 2-)                                                   
FORMUL  12  HOH   *227(H2 O)                                                    
HELIX    1   1 ASP A    3  ARG A    8  1                                   6    
HELIX    2   2 PHE A   45  HIS A   49  5                                   5    
HELIX    3   3 PRO A   57  ASP A   78  1                                  22    
HELIX    4   4 ASP B    3  LEU B   11  1                                   9    
HELIX    5   5 PHE B   45  HIS B   49  5                                   5    
HELIX    6   6 PRO B   57  LEU B   77  1                                  21    
HELIX    7   7 ASP C    3  LEU C   11  1                                   9    
HELIX    8   8 PHE C   45  HIS C   49  5                                   5    
HELIX    9   9 PRO C   57  LEU C   77  1                                  21    
HELIX   10  10 ASP D    3  LEU D   11  1                                   9    
HELIX   11  11 GLU D   43  HIS D   49  5                                   7    
HELIX   12  12 PRO D   57  LEU D   77  1                                  21    
HELIX   13  13 ASP E    3  LEU E   11  1                                   9    
HELIX   14  14 PHE E   45  HIS E   49  5                                   5    
HELIX   15  15 PRO E   57  LEU E   77  1                                  21    
HELIX   16  16 ASP F    3  LEU F   11  1                                   9    
HELIX   17  17 PRO F   57  LEU F   77  1                                  21    
SHEET    1   A12 ARG A  22  ASP A  27  0                                        
SHEET    2   A12 ARG A  32  ASN A  38 -1  O  ARG A  34   N  GLU A  25           
SHEET    3   A12 GLN A 106  LYS A 117 -1  O  LEU A 109   N  ALA A  35           
SHEET    4   A12 ILE A 120  VAL A 129 -1  O  HIS A 126   N  HIS A 110           
SHEET    5   A12 LYS A 132  ARG A 144 -1  O  ILE A 139   N  PHE A 123           
SHEET    6   A12 LEU A  86  PHE A  97 -1  N  ARG A  96   O  SER A 136           
SHEET    7   A12 THR B  85  PHE B  97 -1  O  LEU B  95   N  SER A  92           
SHEET    8   A12 LYS B 132  LYS B 145 -1  O  ARG B 144   N  LEU B  86           
SHEET    9   A12 ILE B 120  VAL B 129 -1  N  TRP B 121   O  CYS B 141           
SHEET   10   A12 GLN B 106  LYS B 117 -1  N  HIS B 110   O  HIS B 126           
SHEET   11   A12 ARG B  32  ASN B  38 -1  N  ALA B  35   O  LEU B 109           
SHEET   12   A12 ARG B  22  ASP B  27 -1  N  GLU B  25   O  ARG B  34           
SHEET    1   B12 ARG C  22  ASP C  27  0                                        
SHEET    2   B12 ARG C  32  ASN C  38 -1  O  ARG C  34   N  GLU C  25           
SHEET    3   B12 GLN C 106  VAL C 116 -1  O  LEU C 109   N  ALA C  35           
SHEET    4   B12 ILE C 120  VAL C 129 -1  O  THR C 128   N  GLN C 108           
SHEET    5   B12 LYS C 132  GLU C 143 -1  O  CYS C 135   N  ALA C 127           
SHEET    6   B12 TYR C  87  PHE C  97 -1  N  VAL C  90   O  ILE C 140           
SHEET    7   B12 THR D  85  PHE D  97 -1  O  SER D  92   N  LEU C  95           
SHEET    8   B12 LYS D 132  LYS D 145 -1  O  ARG D 144   N  LEU D  86           
SHEET    9   B12 ILE D 120  VAL D 129 -1  N  TRP D 121   O  CYS D 141           
SHEET   10   B12 GLN D 106  LYS D 117 -1  N  LYS D 112   O  ASP D 124           
SHEET   11   B12 ARG D  32  ASN D  38 -1  N  ALA D  35   O  LEU D 109           
SHEET   12   B12 ARG D  22  ASP D  27 -1  N  ARG D  22   O  TYR D  36           
SHEET    1   C12 ARG E  22  ASP E  27  0                                        
SHEET    2   C12 ARG E  32  ASN E  38 -1  O  ARG E  34   N  GLU E  25           
SHEET    3   C12 GLN E 106  PHE E 113 -1  O  LEU E 109   N  ALA E  35           
SHEET    4   C12 ILE E 120  VAL E 129 -1  O  THR E 128   N  GLN E 108           
SHEET    5   C12 LYS E 132  LYS E 145 -1  O  ILE E 139   N  PHE E 123           
SHEET    6   C12 THR E  85  PHE E  97 -1  N  LEU E  86   O  ARG E 144           
SHEET    7   C12 THR F  85  PHE F  97 -1  O  LEU F  95   N  SER E  92           
SHEET    8   C12 LYS F 132  LYS F 145 -1  O  ARG F 144   N  LEU F  86           
SHEET    9   C12 ILE F 120  VAL F 129 -1  N  ALA F 127   O  CYS F 135           
SHEET   10   C12 GLN F 106  LYS F 117 -1  N  LYS F 112   O  ASP F 124           
SHEET   11   C12 ARG F  32  ASN F  38 -1  N  ALA F  35   O  LEU F 109           
SHEET   12   C12 ARG F  22  ASP F  27 -1  N  GLU F  25   O  ARG F  34           
LINK         C   MSE A   1                 N   MSE A   2     1555   1555  1.33  
LINK         C   MSE A   2                 N   ASP A   3     1555   1555  1.33  
LINK         C   ILE A  55                 N   MSE A  56     1555   1555  1.33  
LINK         C   MSE A  56                 N   PRO A  57     1555   1555  1.34  
LINK         C   ALA A  64                 N   MSE A  65     1555   1555  1.33  
LINK         C   MSE A  65                 N   ALA A  66     1555   1555  1.32  
LINK         C   LYS A  75                 N   MSE A  76     1555   1555  1.33  
LINK         C   MSE A  76                 N   LEU A  77     1555   1555  1.33  
LINK         C   MSE B   1                 N   MSE B   2     1555   1555  1.33  
LINK         C   MSE B   2                 N   ASP B   3     1555   1555  1.33  
LINK         C   ILE B  55                 N   MSE B  56     1555   1555  1.33  
LINK         C   MSE B  56                 N   PRO B  57     1555   1555  1.34  
LINK         C   ALA B  64                 N   MSE B  65     1555   1555  1.33  
LINK         C   MSE B  65                 N   ALA B  66     1555   1555  1.33  
LINK         C   LYS B  75                 N   MSE B  76     1555   1555  1.33  
LINK         C   MSE B  76                 N   LEU B  77     1555   1555  1.33  
LINK         C   MSE C   1                 N   MSE C   2     1555   1555  1.33  
LINK         C   MSE C   2                 N   ASP C   3     1555   1555  1.33  
LINK         C   ILE C  55                 N   MSE C  56     1555   1555  1.33  
LINK         C   MSE C  56                 N   PRO C  57     1555   1555  1.34  
LINK         C   ALA C  64                 N   MSE C  65     1555   1555  1.33  
LINK         C   MSE C  65                 N   ALA C  66     1555   1555  1.33  
LINK         C   LYS C  75                 N   MSE C  76     1555   1555  1.33  
LINK         C   MSE C  76                 N   LEU C  77     1555   1555  1.33  
LINK         C   MSE D   1                 N   MSE D   2     1555   1555  1.33  
LINK         C   MSE D   2                 N   ASP D   3     1555   1555  1.33  
LINK         C   ILE D  55                 N   MSE D  56     1555   1555  1.33  
LINK         C   MSE D  56                 N   PRO D  57     1555   1555  1.34  
LINK         C   ALA D  64                 N   MSE D  65     1555   1555  1.33  
LINK         C   MSE D  65                 N   ALA D  66     1555   1555  1.33  
LINK         C   LYS D  75                 N   MSE D  76     1555   1555  1.33  
LINK         C   MSE D  76                 N   LEU D  77     1555   1555  1.33  
LINK         C   MSE E   1                 N   MSE E   2     1555   1555  1.33  
LINK         C   MSE E   2                 N   ASP E   3     1555   1555  1.33  
LINK         C   ILE E  55                 N   MSE E  56     1555   1555  1.33  
LINK         C   MSE E  56                 N   PRO E  57     1555   1555  1.34  
LINK         C   ALA E  64                 N   MSE E  65     1555   1555  1.33  
LINK         C   MSE E  65                 N   ALA E  66     1555   1555  1.33  
LINK         C   LYS E  75                 N   MSE E  76     1555   1555  1.33  
LINK         C   MSE E  76                 N   LEU E  77     1555   1555  1.33  
LINK         C   MSE F   1                 N   MSE F   2     1555   1555  1.33  
LINK         C   MSE F   2                 N   ASP F   3     1555   1555  1.33  
LINK         C   ILE F  55                 N   MSE F  56     1555   1555  1.33  
LINK         C   MSE F  56                 N   PRO F  57     1555   1555  1.34  
LINK         C   ALA F  64                 N   MSE F  65     1555   1555  1.33  
LINK         C   MSE F  65                 N   ALA F  66     1555   1555  1.33  
LINK         C   LYS F  75                 N   MSE F  76     1555   1555  1.33  
LINK         C   MSE F  76                 N   LEU F  77     1555   1555  1.33  
CISPEP   1 TYR A   15    PRO A   16          0         0.25                     
CISPEP   2 HIS A   49    PHE A   50          0         0.20                     
CISPEP   3 TYR B   15    PRO B   16          0         0.05                     
CISPEP   4 HIS B   49    PHE B   50          0         0.00                     
CISPEP   5 TYR C   15    PRO C   16          0         0.18                     
CISPEP   6 HIS C   49    PHE C   50          0        -0.14                     
CISPEP   7 TYR D   15    PRO D   16          0        -0.03                     
CISPEP   8 HIS D   49    PHE D   50          0        -0.16                     
CISPEP   9 TYR E   15    PRO E   16          0        -0.17                     
CISPEP  10 HIS E   49    PHE E   50          0        -0.52                     
CISPEP  11 TYR F   15    PRO F   16          0         0.04                     
CISPEP  12 HIS F   49    PHE F   50          0        -1.63                     
SITE     1 AC1  2 ARG D  34  HOH D 525                                          
SITE     1 AC2  3 LYS B 117  ARG B 118  SER B 119                               
SITE     1 AC3  4 LYS B 117  ARG B 118  GLY D  84  LYS D 145                    
SITE     1 AC4  3 ARG D 118  SER D 119  ARG D 144                               
SITE     1 AC5  4 ASP B  83  LYS B 145  LYS D 117  ARG D 118                    
CRYST1   93.031  100.897  177.252  90.00  90.00  90.00 P 21 21 21   24          
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      0.010749  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009911  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005642        0.00000                         
HETATM    1  N   MSE A   1       7.123  36.563 144.947  1.00 62.00           N  
HETATM    2  CA  MSE A   1       8.227  36.141 144.037  1.00 62.56           C  
HETATM    3  C   MSE A   1       7.700  35.716 142.666  1.00 59.10           C  
HETATM    4  O   MSE A   1       6.602  35.169 142.558  1.00 59.44           O  
HETATM    5  CB  MSE A   1       8.992  34.975 144.653  1.00 69.18           C  
HETATM    6  CG  MSE A   1      10.168  34.512 143.812  1.00 78.19           C  
HETATM    7 SE   MSE A   1      10.376  32.577 143.785  1.00 92.84          SE  
HETATM    8  CE  MSE A   1      10.328  32.259 141.867  1.00 86.65           C  
HETATM    9  N   MSE A   2       8.491  35.954 141.624  1.00 54.73           N  
HETATM   10  CA  MSE A   2       8.104  35.593 140.260  1.00 50.38           C  
HETATM   11  C   MSE A   2       9.145  34.711 139.583  1.00 47.12           C  
HETATM   12  O   MSE A   2      10.294  35.124 139.429  1.00 45.96           O  
HETATM   13  CB  MSE A   2       7.932  36.842 139.411  1.00 51.89           C  
HETATM   14  CG  MSE A   2       6.733  37.690 139.734  1.00 54.45           C  
HETATM   15 SE   MSE A   2       6.803  39.278 138.628  1.00 61.14          SE  
HETATM   16  CE  MSE A   2       6.230  38.514 136.941  1.00 56.05           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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