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Database: PDB
Entry: 4Y4L
LinkDB: 4Y4L
Original site: 4Y4L 
HEADER    BIOSYNTHETIC PROTEIN                    10-FEB-15   4Y4L              
TITLE     CRYSTAL STRUCTURE OF YEAST THI4-C205S                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THIAMINE THIAZOLE SYNTHASE;                                
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: THIAZOLE BIOSYNTHETIC ENZYME;                               
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE   3 S288C);                                                              
SOURCE   4 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   5 ORGANISM_TAXID: 559292;                                              
SOURCE   6 STRAIN: ATCC 204508 / S288C;                                         
SOURCE   7 GENE: THI4, ESP35, MOL1, YGR144W, G6620;                             
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    BIOSYNTHETIC PROTEIN                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.ZHANG,S.E.EALICK                                                    
REVDAT   3   27-SEP-17 4Y4L    1       JRNL   REMARK                            
REVDAT   2   04-MAY-16 4Y4L    1       JRNL                                     
REVDAT   1   09-MAR-16 4Y4L    0                                                
JRNL        AUTH   X.ZHANG,B.E.ESER,P.K.CHANANI,T.P.BEGLEY,S.E.EALICK           
JRNL        TITL   STRUCTURAL BASIS FOR IRON-MEDIATED SULFUR TRANSFER IN        
JRNL        TITL 2 ARCHAEL AND YEAST THIAZOLE SYNTHASES.                        
JRNL        REF    BIOCHEMISTRY                  V.  55  1826 2016              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   26919468                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.6B00030                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.27                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 74670                          
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) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.192                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3955                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5409                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.29                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 274                          
REMARK   3   BIN FREE R VALUE                    : 0.2270                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9080                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 156                                     
REMARK   3   SOLVENT ATOMS            : 333                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.39000                                             
REMARK   3    B22 (A**2) : -0.39000                                             
REMARK   3    B33 (A**2) : 0.78000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.180         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.141         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9502 ; 0.005 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12908 ; 1.113 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1215 ; 5.789 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   377 ;33.570 ;24.430       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1547 ;13.141 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    37 ;14.733 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1474 ; 0.062 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7081 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  5989 ; 0.917 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9618 ; 1.618 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3513 ; 0.861 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3285 ; 1.455 ; 4.500       
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   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4Y4L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206744.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-AUG-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 78765                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 3FPZ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% (W/V) PEG1500, 0.0125 M SUCCINIC     
REMARK 280  ACID, 0.04375M SODIUM DIHYDROGEN PHOSPHATE, AND 0.04375M GLYCINE,   
REMARK 280  PH 8.5, EVAPORATION, TEMPERATURE 295K                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 58700 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 65950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -371.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      382.17900            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      127.39300            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      254.78600            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000     -127.39300            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000      127.39300            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000      254.78600            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 58040 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 66070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -350.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      254.78600            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      127.39300            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000     -127.39300            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000      127.39300            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000      127.39300            
REMARK 350   BIOMT3   4  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     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     THR A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     ALA A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     GLN A    14                                                      
REMARK 465     LEU A    15                                                      
REMARK 465     HIS A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     ASN A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     THR A    20                                                      
REMARK 465     PRO A    21                                                      
REMARK 465     GLN A   203                                                      
REMARK 465     ALA A   326                                                      
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     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     THR B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     ALA B    12                                                      
REMARK 465     SER B    13                                                      
REMARK 465     GLN B    14                                                      
REMARK 465     LEU B    15                                                      
REMARK 465     HIS B    16                                                      
REMARK 465     LEU B    17                                                      
REMARK 465     ASN B    18                                                      
REMARK 465     SER B    19                                                      
REMARK 465     THR B    20                                                      
REMARK 465     PRO B    21                                                      
REMARK 465     THR B   179                                                      
REMARK 465     GLU B   180                                                      
REMARK 465     LYS B   181                                                      
REMARK 465     GLY B   182                                                      
REMARK 465     GLU B   183                                                      
REMARK 465     VAL B   184                                                      
REMARK 465     GLN B   203                                                      
REMARK 465     GLN B   254                                                      
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     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     ALA C     3                                                      
REMARK 465     THR C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     THR C     6                                                      
REMARK 465     ALA C     7                                                      
REMARK 465     THR C     8                                                      
REMARK 465     SER C     9                                                      
REMARK 465     THR C    10                                                      
REMARK 465     SER C    11                                                      
REMARK 465     ALA C    12                                                      
REMARK 465     SER C    13                                                      
REMARK 465     GLN C    14                                                      
REMARK 465     LEU C    15                                                      
REMARK 465     HIS C    16                                                      
REMARK 465     LEU C    17                                                      
REMARK 465     ASN C    18                                                      
REMARK 465     SER C    19                                                      
REMARK 465     THR C    20                                                      
REMARK 465     PRO C    21                                                      
REMARK 465     VAL C    22                                                      
REMARK 465     THR C   179                                                      
REMARK 465     GLU C   180                                                      
REMARK 465     LYS C   181                                                      
REMARK 465     GLN C   203                                                      
REMARK 465     ALA C   326                                                      
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     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     ALA D     3                                                      
REMARK 465     THR D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     THR D     6                                                      
REMARK 465     ALA D     7                                                      
REMARK 465     THR D     8                                                      
REMARK 465     SER D     9                                                      
REMARK 465     THR D    10                                                      
REMARK 465     SER D    11                                                      
REMARK 465     ALA D    12                                                      
REMARK 465     SER D    13                                                      
REMARK 465     GLN D    14                                                      
REMARK 465     LEU D    15                                                      
REMARK 465     HIS D    16                                                      
REMARK 465     LEU D    17                                                      
REMARK 465     ASN D    18                                                      
REMARK 465     SER D    19                                                      
REMARK 465     THR D    20                                                      
REMARK 465     PRO D    21                                                      
REMARK 465     GLN D   203                                                      
REMARK 465     ALA D   326                                                      
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     GLN B 256    CG   CD   OE1  NE2                                  
REMARK 470     GLN C 254    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 257    CG   CD   CE   NZ                                   
REMARK 470     ASN D 255    CG   OD1  ND2                                       
REMARK 470     GLN D 256    CG   CD   OE1  NE2                                  
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   555     O    HOH A   568              1.96            
REMARK 500   O    HOH B   509     O    HOH B   516              2.07            
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    ALA A  73       56.99    -95.71                                   
REMARK 500    PRO A 178      152.89    -49.44                                   
REMARK 500    ALA B  73       58.14    -99.85                                   
REMARK 500    THR B 234       58.27   -140.28                                   
REMARK 500    ALA C  73       57.52    -96.34                                   
REMARK 500    ALA D  73       57.66   -101.60                                   
REMARK 500    PRO D 178      151.99    -48.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 48N A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 48N B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 48N C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 48N D 401                 
DBREF  4Y4L A    1   326  UNP    P32318   THI4_YEAST       1    326             
DBREF  4Y4L B    1   326  UNP    P32318   THI4_YEAST       1    326             
DBREF  4Y4L C    1   326  UNP    P32318   THI4_YEAST       1    326             
DBREF  4Y4L D    1   326  UNP    P32318   THI4_YEAST       1    326             
SEQADV 4Y4L MET A  -19  UNP  P32318              INITIATING METHIONINE          
SEQADV 4Y4L GLY A  -18  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER A  -17  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER A  -16  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS A  -15  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS A  -14  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS A  -13  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS A  -12  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS A  -11  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS A  -10  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER A   -9  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER A   -8  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L GLY A   -7  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L LEU A   -6  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L VAL A   -5  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L PRO A   -4  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L ARG A   -3  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L GLY A   -2  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER A   -1  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS A    0  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER A  205  UNP  P32318    CYS   205 ENGINEERED MUTATION            
SEQADV 4Y4L MET B  -19  UNP  P32318              INITIATING METHIONINE          
SEQADV 4Y4L GLY B  -18  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER B  -17  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER B  -16  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS B  -15  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS B  -14  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS B  -13  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS B  -12  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS B  -11  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS B  -10  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER B   -9  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER B   -8  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L GLY B   -7  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L LEU B   -6  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L VAL B   -5  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L PRO B   -4  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L ARG B   -3  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L GLY B   -2  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER B   -1  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS B    0  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER B  205  UNP  P32318    CYS   205 ENGINEERED MUTATION            
SEQADV 4Y4L MET C  -19  UNP  P32318              INITIATING METHIONINE          
SEQADV 4Y4L GLY C  -18  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER C  -17  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER C  -16  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS C  -15  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS C  -14  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS C  -13  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS C  -12  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS C  -11  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS C  -10  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER C   -9  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER C   -8  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L GLY C   -7  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L LEU C   -6  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L VAL C   -5  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L PRO C   -4  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L ARG C   -3  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L GLY C   -2  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER C   -1  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS C    0  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER C  205  UNP  P32318    CYS   205 ENGINEERED MUTATION            
SEQADV 4Y4L MET D  -19  UNP  P32318              INITIATING METHIONINE          
SEQADV 4Y4L GLY D  -18  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER D  -17  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER D  -16  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS D  -15  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS D  -14  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS D  -13  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS D  -12  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS D  -11  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS D  -10  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER D   -9  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER D   -8  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L GLY D   -7  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L LEU D   -6  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L VAL D   -5  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L PRO D   -4  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L ARG D   -3  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L GLY D   -2  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER D   -1  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L HIS D    0  UNP  P32318              EXPRESSION TAG                 
SEQADV 4Y4L SER D  205  UNP  P32318    CYS   205 ENGINEERED MUTATION            
SEQRES   1 A  346  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  346  LEU VAL PRO ARG GLY SER HIS MET SER ALA THR SER THR          
SEQRES   3 A  346  ALA THR SER THR SER ALA SER GLN LEU HIS LEU ASN SER          
SEQRES   4 A  346  THR PRO VAL THR HIS CYS LEU SER ASP ILE VAL LYS LYS          
SEQRES   5 A  346  GLU ASP TRP SER ASP PHE LYS PHE ALA PRO ILE ARG GLU          
SEQRES   6 A  346  SER THR VAL SER ARG ALA MET THR SER ARG TYR PHE LYS          
SEQRES   7 A  346  ASP LEU ASP LYS PHE ALA VAL SER ASP VAL ILE ILE VAL          
SEQRES   8 A  346  GLY ALA GLY SER SER GLY LEU SER ALA ALA TYR VAL ILE          
SEQRES   9 A  346  ALA LYS ASN ARG PRO ASP LEU LYS VAL CYS ILE ILE GLU          
SEQRES  10 A  346  SER SER VAL ALA PRO GLY GLY GLY SER TRP LEU GLY GLY          
SEQRES  11 A  346  GLN LEU PHE SER ALA MET VAL MET ARG LYS PRO ALA HIS          
SEQRES  12 A  346  LEU PHE LEU GLN GLU LEU GLU ILE PRO TYR GLU ASP GLU          
SEQRES  13 A  346  GLY ASP TYR VAL VAL VAL LYS HIS ALA ALA LEU PHE ILE          
SEQRES  14 A  346  SER THR VAL LEU SER LYS VAL LEU GLN LEU PRO ASN VAL          
SEQRES  15 A  346  LYS LEU PHE ASN ALA THR CYS VAL GLU ASP LEU VAL THR          
SEQRES  16 A  346  ARG PRO PRO THR GLU LYS GLY GLU VAL THR VAL ALA GLY          
SEQRES  17 A  346  VAL VAL THR ASN TRP THR LEU VAL THR GLN ALA HIS GLY          
SEQRES  18 A  346  THR GLN CYS SER MET ASP PRO ASN VAL ILE GLU LEU ALA          
SEQRES  19 A  346  GLY TYR LYS ASN ASP GLY THR ARG ASP LEU SER GLN LYS          
SEQRES  20 A  346  HIS GLY VAL ILE LEU SER THR THR GLY HIS ASP GLY PRO          
SEQRES  21 A  346  PHE GLY ALA PHE CYS ALA LYS ARG ILE VAL ASP ILE ASP          
SEQRES  22 A  346  GLN ASN GLN LYS LEU GLY GLY MET LYS GLY LEU ASP MET          
SEQRES  23 A  346  ASN HIS ALA GLU HIS ASP VAL VAL ILE HIS SER GLY ALA          
SEQRES  24 A  346  TYR ALA GLY VAL ASP ASN MET TYR PHE ALA GLY MET GLU          
SEQRES  25 A  346  VAL ALA GLU LEU ASP GLY LEU ASN ARG MET GLY PRO THR          
SEQRES  26 A  346  PHE GLY ALA MET ALA LEU SER GLY VAL HIS ALA ALA GLU          
SEQRES  27 A  346  GLN ILE LEU LYS HIS PHE ALA ALA                              
SEQRES   1 B  346  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  346  LEU VAL PRO ARG GLY SER HIS MET SER ALA THR SER THR          
SEQRES   3 B  346  ALA THR SER THR SER ALA SER GLN LEU HIS LEU ASN SER          
SEQRES   4 B  346  THR PRO VAL THR HIS CYS LEU SER ASP ILE VAL LYS LYS          
SEQRES   5 B  346  GLU ASP TRP SER ASP PHE LYS PHE ALA PRO ILE ARG GLU          
SEQRES   6 B  346  SER THR VAL SER ARG ALA MET THR SER ARG TYR PHE LYS          
SEQRES   7 B  346  ASP LEU ASP LYS PHE ALA VAL SER ASP VAL ILE ILE VAL          
SEQRES   8 B  346  GLY ALA GLY SER SER GLY LEU SER ALA ALA TYR VAL ILE          
SEQRES   9 B  346  ALA LYS ASN ARG PRO ASP LEU LYS VAL CYS ILE ILE GLU          
SEQRES  10 B  346  SER SER VAL ALA PRO GLY GLY GLY SER TRP LEU GLY GLY          
SEQRES  11 B  346  GLN LEU PHE SER ALA MET VAL MET ARG LYS PRO ALA HIS          
SEQRES  12 B  346  LEU PHE LEU GLN GLU LEU GLU ILE PRO TYR GLU ASP GLU          
SEQRES  13 B  346  GLY ASP TYR VAL VAL VAL LYS HIS ALA ALA LEU PHE ILE          
SEQRES  14 B  346  SER THR VAL LEU SER LYS VAL LEU GLN LEU PRO ASN VAL          
SEQRES  15 B  346  LYS LEU PHE ASN ALA THR CYS VAL GLU ASP LEU VAL THR          
SEQRES  16 B  346  ARG PRO PRO THR GLU LYS GLY GLU VAL THR VAL ALA GLY          
SEQRES  17 B  346  VAL VAL THR ASN TRP THR LEU VAL THR GLN ALA HIS GLY          
SEQRES  18 B  346  THR GLN CYS SER MET ASP PRO ASN VAL ILE GLU LEU ALA          
SEQRES  19 B  346  GLY TYR LYS ASN ASP GLY THR ARG ASP LEU SER GLN LYS          
SEQRES  20 B  346  HIS GLY VAL ILE LEU SER THR THR GLY HIS ASP GLY PRO          
SEQRES  21 B  346  PHE GLY ALA PHE CYS ALA LYS ARG ILE VAL ASP ILE ASP          
SEQRES  22 B  346  GLN ASN GLN LYS LEU GLY GLY MET LYS GLY LEU ASP MET          
SEQRES  23 B  346  ASN HIS ALA GLU HIS ASP VAL VAL ILE HIS SER GLY ALA          
SEQRES  24 B  346  TYR ALA GLY VAL ASP ASN MET TYR PHE ALA GLY MET GLU          
SEQRES  25 B  346  VAL ALA GLU LEU ASP GLY LEU ASN ARG MET GLY PRO THR          
SEQRES  26 B  346  PHE GLY ALA MET ALA LEU SER GLY VAL HIS ALA ALA GLU          
SEQRES  27 B  346  GLN ILE LEU LYS HIS PHE ALA ALA                              
SEQRES   1 C  346  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  346  LEU VAL PRO ARG GLY SER HIS MET SER ALA THR SER THR          
SEQRES   3 C  346  ALA THR SER THR SER ALA SER GLN LEU HIS LEU ASN SER          
SEQRES   4 C  346  THR PRO VAL THR HIS CYS LEU SER ASP ILE VAL LYS LYS          
SEQRES   5 C  346  GLU ASP TRP SER ASP PHE LYS PHE ALA PRO ILE ARG GLU          
SEQRES   6 C  346  SER THR VAL SER ARG ALA MET THR SER ARG TYR PHE LYS          
SEQRES   7 C  346  ASP LEU ASP LYS PHE ALA VAL SER ASP VAL ILE ILE VAL          
SEQRES   8 C  346  GLY ALA GLY SER SER GLY LEU SER ALA ALA TYR VAL ILE          
SEQRES   9 C  346  ALA LYS ASN ARG PRO ASP LEU LYS VAL CYS ILE ILE GLU          
SEQRES  10 C  346  SER SER VAL ALA PRO GLY GLY GLY SER TRP LEU GLY GLY          
SEQRES  11 C  346  GLN LEU PHE SER ALA MET VAL MET ARG LYS PRO ALA HIS          
SEQRES  12 C  346  LEU PHE LEU GLN GLU LEU GLU ILE PRO TYR GLU ASP GLU          
SEQRES  13 C  346  GLY ASP TYR VAL VAL VAL LYS HIS ALA ALA LEU PHE ILE          
SEQRES  14 C  346  SER THR VAL LEU SER LYS VAL LEU GLN LEU PRO ASN VAL          
SEQRES  15 C  346  LYS LEU PHE ASN ALA THR CYS VAL GLU ASP LEU VAL THR          
SEQRES  16 C  346  ARG PRO PRO THR GLU LYS GLY GLU VAL THR VAL ALA GLY          
SEQRES  17 C  346  VAL VAL THR ASN TRP THR LEU VAL THR GLN ALA HIS GLY          
SEQRES  18 C  346  THR GLN CYS SER MET ASP PRO ASN VAL ILE GLU LEU ALA          
SEQRES  19 C  346  GLY TYR LYS ASN ASP GLY THR ARG ASP LEU SER GLN LYS          
SEQRES  20 C  346  HIS GLY VAL ILE LEU SER THR THR GLY HIS ASP GLY PRO          
SEQRES  21 C  346  PHE GLY ALA PHE CYS ALA LYS ARG ILE VAL ASP ILE ASP          
SEQRES  22 C  346  GLN ASN GLN LYS LEU GLY GLY MET LYS GLY LEU ASP MET          
SEQRES  23 C  346  ASN HIS ALA GLU HIS ASP VAL VAL ILE HIS SER GLY ALA          
SEQRES  24 C  346  TYR ALA GLY VAL ASP ASN MET TYR PHE ALA GLY MET GLU          
SEQRES  25 C  346  VAL ALA GLU LEU ASP GLY LEU ASN ARG MET GLY PRO THR          
SEQRES  26 C  346  PHE GLY ALA MET ALA LEU SER GLY VAL HIS ALA ALA GLU          
SEQRES  27 C  346  GLN ILE LEU LYS HIS PHE ALA ALA                              
SEQRES   1 D  346  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  346  LEU VAL PRO ARG GLY SER HIS MET SER ALA THR SER THR          
SEQRES   3 D  346  ALA THR SER THR SER ALA SER GLN LEU HIS LEU ASN SER          
SEQRES   4 D  346  THR PRO VAL THR HIS CYS LEU SER ASP ILE VAL LYS LYS          
SEQRES   5 D  346  GLU ASP TRP SER ASP PHE LYS PHE ALA PRO ILE ARG GLU          
SEQRES   6 D  346  SER THR VAL SER ARG ALA MET THR SER ARG TYR PHE LYS          
SEQRES   7 D  346  ASP LEU ASP LYS PHE ALA VAL SER ASP VAL ILE ILE VAL          
SEQRES   8 D  346  GLY ALA GLY SER SER GLY LEU SER ALA ALA TYR VAL ILE          
SEQRES   9 D  346  ALA LYS ASN ARG PRO ASP LEU LYS VAL CYS ILE ILE GLU          
SEQRES  10 D  346  SER SER VAL ALA PRO GLY GLY GLY SER TRP LEU GLY GLY          
SEQRES  11 D  346  GLN LEU PHE SER ALA MET VAL MET ARG LYS PRO ALA HIS          
SEQRES  12 D  346  LEU PHE LEU GLN GLU LEU GLU ILE PRO TYR GLU ASP GLU          
SEQRES  13 D  346  GLY ASP TYR VAL VAL VAL LYS HIS ALA ALA LEU PHE ILE          
SEQRES  14 D  346  SER THR VAL LEU SER LYS VAL LEU GLN LEU PRO ASN VAL          
SEQRES  15 D  346  LYS LEU PHE ASN ALA THR CYS VAL GLU ASP LEU VAL THR          
SEQRES  16 D  346  ARG PRO PRO THR GLU LYS GLY GLU VAL THR VAL ALA GLY          
SEQRES  17 D  346  VAL VAL THR ASN TRP THR LEU VAL THR GLN ALA HIS GLY          
SEQRES  18 D  346  THR GLN CYS SER MET ASP PRO ASN VAL ILE GLU LEU ALA          
SEQRES  19 D  346  GLY TYR LYS ASN ASP GLY THR ARG ASP LEU SER GLN LYS          
SEQRES  20 D  346  HIS GLY VAL ILE LEU SER THR THR GLY HIS ASP GLY PRO          
SEQRES  21 D  346  PHE GLY ALA PHE CYS ALA LYS ARG ILE VAL ASP ILE ASP          
SEQRES  22 D  346  GLN ASN GLN LYS LEU GLY GLY MET LYS GLY LEU ASP MET          
SEQRES  23 D  346  ASN HIS ALA GLU HIS ASP VAL VAL ILE HIS SER GLY ALA          
SEQRES  24 D  346  TYR ALA GLY VAL ASP ASN MET TYR PHE ALA GLY MET GLU          
SEQRES  25 D  346  VAL ALA GLU LEU ASP GLY LEU ASN ARG MET GLY PRO THR          
SEQRES  26 D  346  PHE GLY ALA MET ALA LEU SER GLY VAL HIS ALA ALA GLU          
SEQRES  27 D  346  GLN ILE LEU LYS HIS PHE ALA ALA                              
HET    48N  A 401      39                                                       
HET    48N  B 401      39                                                       
HET    48N  C 401      39                                                       
HET    48N  D 401      39                                                       
HETNAM     48N (2E)-2-[(2S,4R)-5-[[[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-            
HETNAM   2 48N  YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-OXIDANYL-              
HETNAM   3 48N  PHOSPHORYL]OXY-OXIDANYL-PHOSPHORYL]OXY-4-OXIDANYL-3-            
HETNAM   4 48N  OXIDANYLIDENE-PENTAN-2-YL]IMINOETHANOIC ACID                    
FORMUL   5  48N    4(C17 H24 N6 O14 P2)                                         
FORMUL   9  HOH   *333(H2 O)                                                    
HELIX    1 AA1 ARG A   44  ALA A   64  1                                  21    
HELIX    2 AA2 GLY A   74  ARG A   88  1                                  15    
HELIX    3 AA3 ALA A  122  LEU A  129  1                                   8    
HELIX    4 AA4 HIS A  144  GLN A  158  1                                  15    
HELIX    5 AA5 THR A  194  GLN A  198  1                                   5    
HELIX    6 AA6 ALA A  243  ASP A  253  1                                  11    
HELIX    7 AA7 ASP A  265  SER A  277  1                                  13    
HELIX    8 AA8 GLY A  290  GLY A  298  1                                   9    
HELIX    9 AA9 PHE A  306  ALA A  325  1                                  20    
HELIX   10 AB1 ARG B   44  ALA B   64  1                                  21    
HELIX   11 AB2 GLY B   74  ARG B   88  1                                  15    
HELIX   12 AB3 ALA B  122  LEU B  129  1                                   8    
HELIX   13 AB4 HIS B  144  GLN B  158  1                                  15    
HELIX   14 AB5 THR B  194  GLN B  198  1                                   5    
HELIX   15 AB6 ALA B  243  ASP B  253  1                                  11    
HELIX   16 AB7 ASP B  265  SER B  277  1                                  13    
HELIX   17 AB8 GLY B  290  GLY B  298  1                                   9    
HELIX   18 AB9 PHE B  306  ALA B  326  1                                  21    
HELIX   19 AC1 ARG C   44  ALA C   64  1                                  21    
HELIX   20 AC2 GLY C   74  ARG C   88  1                                  15    
HELIX   21 AC3 ALA C  122  GLU C  130  1                                   9    
HELIX   22 AC4 HIS C  144  GLN C  158  1                                  15    
HELIX   23 AC5 THR C  194  GLN C  198  1                                   5    
HELIX   24 AC6 ALA C  243  ASP C  253  1                                  11    
HELIX   25 AC7 ASP C  265  SER C  277  1                                  13    
HELIX   26 AC8 GLY C  290  GLY C  298  1                                   9    
HELIX   27 AC9 PHE C  306  ALA C  325  1                                  20    
HELIX   28 AD1 ARG D   44  ALA D   64  1                                  21    
HELIX   29 AD2 GLY D   74  ARG D   88  1                                  15    
HELIX   30 AD3 ALA D  122  LEU D  129  1                                   8    
HELIX   31 AD4 HIS D  144  GLN D  158  1                                  15    
HELIX   32 AD5 THR D  194  GLN D  198  1                                   5    
HELIX   33 AD6 ALA D  243  ASP D  253  1                                  11    
HELIX   34 AD7 ASP D  265  SER D  277  1                                  13    
HELIX   35 AD8 GLY D  290  GLY D  298  1                                   9    
HELIX   36 AD9 PHE D  306  ALA D  325  1                                  20    
SHEET    1 AA1 4 VAL A  65  SER A  66  0                                        
SHEET    2 AA1 4 ASN A 209  LEU A 213  1  O  GLU A 212   N  SER A  66           
SHEET    3 AA1 4 THR A 185  TRP A 193 -1  N  THR A 191   O  ASN A 209           
SHEET    4 AA1 4 THR A 168  ARG A 176 -1  N  VAL A 174   O  ALA A 187           
SHEET    1 AA2 6 VAL A 162  ASN A 166  0                                        
SHEET    2 AA2 6 VAL A  93  GLU A  97  1  N  ILE A  95   O  LYS A 163           
SHEET    3 AA2 6 VAL A  68  VAL A  71  1  N  VAL A  68   O  CYS A  94           
SHEET    4 AA2 6 VAL A 230  SER A 233  1  O  LEU A 232   N  ILE A  69           
SHEET    5 AA2 6 MET A 286  PHE A 288  1  O  TYR A 287   N  SER A 233           
SHEET    6 AA2 6 GLY A 278  ALA A 279 -1  N  GLY A 278   O  PHE A 288           
SHEET    1 AA3 3 MET A 116  ARG A 119  0                                        
SHEET    2 AA3 3 TYR A 139  VAL A 142 -1  O  VAL A 140   N  MET A 118           
SHEET    3 AA3 3 GLU A 134  ASP A 135 -1  N  GLU A 134   O  VAL A 141           
SHEET    1 AA4 4 VAL B  65  SER B  66  0                                        
SHEET    2 AA4 4 ASN B 209  LEU B 213  1  O  GLU B 212   N  SER B  66           
SHEET    3 AA4 4 VAL B 186  TRP B 193 -1  N  THR B 191   O  ASN B 209           
SHEET    4 AA4 4 THR B 168  THR B 175 -1  N  GLU B 171   O  VAL B 190           
SHEET    1 AA5 6 VAL B 162  PHE B 165  0                                        
SHEET    2 AA5 6 VAL B  93  ILE B  96  1  N  ILE B  95   O  LYS B 163           
SHEET    3 AA5 6 VAL B  68  VAL B  71  1  N  VAL B  68   O  CYS B  94           
SHEET    4 AA5 6 VAL B 230  SER B 233  1  O  LEU B 232   N  ILE B  69           
SHEET    5 AA5 6 MET B 286  PHE B 288  1  O  TYR B 287   N  SER B 233           
SHEET    6 AA5 6 GLY B 278  ALA B 279 -1  N  GLY B 278   O  PHE B 288           
SHEET    1 AA6 3 MET B 116  ARG B 119  0                                        
SHEET    2 AA6 3 TYR B 139  VAL B 142 -1  O  VAL B 140   N  MET B 118           
SHEET    3 AA6 3 GLU B 134  ASP B 135 -1  N  GLU B 134   O  VAL B 141           
SHEET    1 AA7 4 VAL C  65  SER C  66  0                                        
SHEET    2 AA7 4 ASN C 209  LEU C 213  1  O  GLU C 212   N  SER C  66           
SHEET    3 AA7 4 THR C 185  TRP C 193 -1  N  THR C 191   O  ASN C 209           
SHEET    4 AA7 4 THR C 168  ARG C 176 -1  N  VAL C 174   O  ALA C 187           
SHEET    1 AA8 6 VAL C 162  PHE C 165  0                                        
SHEET    2 AA8 6 VAL C  93  ILE C  96  1  N  ILE C  95   O  LYS C 163           
SHEET    3 AA8 6 VAL C  68  VAL C  71  1  N  VAL C  68   O  CYS C  94           
SHEET    4 AA8 6 VAL C 230  SER C 233  1  O  LEU C 232   N  VAL C  71           
SHEET    5 AA8 6 MET C 286  PHE C 288  1  O  TYR C 287   N  SER C 233           
SHEET    6 AA8 6 GLY C 278  ALA C 279 -1  N  GLY C 278   O  PHE C 288           
SHEET    1 AA9 3 MET C 116  ARG C 119  0                                        
SHEET    2 AA9 3 TYR C 139  VAL C 142 -1  O  VAL C 140   N  MET C 118           
SHEET    3 AA9 3 GLU C 134  ASP C 135 -1  N  GLU C 134   O  VAL C 141           
SHEET    1 AB1 4 VAL D  65  SER D  66  0                                        
SHEET    2 AB1 4 ASN D 209  LEU D 213  1  O  GLU D 212   N  SER D  66           
SHEET    3 AB1 4 THR D 185  TRP D 193 -1  N  THR D 191   O  ASN D 209           
SHEET    4 AB1 4 THR D 168  ARG D 176 -1  N  CYS D 169   O  ASN D 192           
SHEET    1 AB2 6 VAL D 162  ASN D 166  0                                        
SHEET    2 AB2 6 VAL D  93  GLU D  97  1  N  ILE D  95   O  LYS D 163           
SHEET    3 AB2 6 VAL D  68  VAL D  71  1  N  VAL D  68   O  CYS D  94           
SHEET    4 AB2 6 VAL D 230  SER D 233  1  O  LEU D 232   N  ILE D  69           
SHEET    5 AB2 6 MET D 286  PHE D 288  1  O  TYR D 287   N  SER D 233           
SHEET    6 AB2 6 GLY D 278  ALA D 279 -1  N  GLY D 278   O  PHE D 288           
SHEET    1 AB3 3 MET D 116  ARG D 119  0                                        
SHEET    2 AB3 3 TYR D 139  VAL D 142 -1  O  VAL D 140   N  MET D 118           
SHEET    3 AB3 3 GLU D 134  ASP D 135 -1  N  GLU D 134   O  VAL D 141           
CISPEP   1 LYS A  120    PRO A  121          0        12.29                     
CISPEP   2 LYS B  120    PRO B  121          0        11.81                     
CISPEP   3 LYS C  120    PRO C  121          0        11.56                     
CISPEP   4 LYS D  120    PRO D  121          0         9.46                     
SITE     1 AC1 32 GLY A  72  GLY A  74  SER A  75  SER A  76                    
SITE     2 AC1 32 ILE A  96  GLU A  97  SER A  98  SER A  99                    
SITE     3 AC1 32 GLY A 104  GLY A 105  CYS A 169  VAL A 170                    
SITE     4 AC1 32 ASP A 207  PRO A 208  THR A 234  THR A 235                    
SITE     5 AC1 32 GLY A 236  HIS A 237  PHE A 241  GLY A 290                    
SITE     6 AC1 32 MET A 291  ARG A 301  MET A 302  GLY A 303                    
SITE     7 AC1 32 THR A 305  PHE A 306  MET A 309  HOH A 503                    
SITE     8 AC1 32 HOH A 522  HOH A 527  HOH A 530  HOH A 532                    
SITE     1 AC2 35 VAL B  71  GLY B  72  GLY B  74  SER B  75                    
SITE     2 AC2 35 SER B  76  ILE B  96  GLU B  97  SER B  98                    
SITE     3 AC2 35 SER B  99  GLY B 104  GLY B 105  CYS B 169                    
SITE     4 AC2 35 VAL B 170  ASP B 207  PRO B 208  THR B 234                    
SITE     5 AC2 35 THR B 235  GLY B 236  HIS B 237  PHE B 241                    
SITE     6 AC2 35 GLY B 290  MET B 291  ARG B 301  MET B 302                    
SITE     7 AC2 35 GLY B 303  THR B 305  PHE B 306  MET B 309                    
SITE     8 AC2 35 HOH B 502  HOH B 509  HOH B 524  HOH B 525                    
SITE     9 AC2 35 HOH B 532  HOH B 541  HOH B 573                               
SITE     1 AC3 33 GLY C  72  GLY C  74  SER C  75  SER C  76                    
SITE     2 AC3 33 ILE C  96  GLU C  97  SER C  98  SER C  99                    
SITE     3 AC3 33 GLY C 104  GLY C 105  CYS C 169  VAL C 170                    
SITE     4 AC3 33 ASP C 207  PRO C 208  THR C 234  THR C 235                    
SITE     5 AC3 33 GLY C 236  HIS C 237  PHE C 241  PHE C 244                    
SITE     6 AC3 33 GLY C 290  MET C 291  ARG C 301  MET C 302                    
SITE     7 AC3 33 GLY C 303  THR C 305  PHE C 306  MET C 309                    
SITE     8 AC3 33 HOH C 501  HOH C 519  HOH C 522  HOH C 532                    
SITE     9 AC3 33 HOH C 551                                                     
SITE     1 AC4 32 GLY D  72  GLY D  74  SER D  75  SER D  76                    
SITE     2 AC4 32 ILE D  96  GLU D  97  SER D  98  SER D  99                    
SITE     3 AC4 32 GLY D 104  GLY D 105  CYS D 169  VAL D 170                    
SITE     4 AC4 32 ASP D 207  PRO D 208  THR D 234  THR D 235                    
SITE     5 AC4 32 GLY D 236  HIS D 237  PHE D 241  GLY D 290                    
SITE     6 AC4 32 MET D 291  ARG D 301  MET D 302  GLY D 303                    
SITE     7 AC4 32 THR D 305  PHE D 306  MET D 309  HOH D 501                    
SITE     8 AC4 32 HOH D 525  HOH D 527  HOH D 539  HOH D 567                    
CRYST1  127.393  127.393   72.579  90.00  90.00  90.00 P 4          16          
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      0.007850  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007850  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013778        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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