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Entry: 1IG8
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HEADER    TRANSFERASE                             17-APR-01   1IG8              
TITLE     CRYSTAL STRUCTURE OF YEAST HEXOKINASE PII WITH THE CORRECT            
TITLE    2 AMINO ACID SEQUENCE                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEXOKINASE PII;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HEXOKINASE B;                                               
COMPND   5 EC: 2.7.1.1                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932                                                 
KEYWDS    MIXED ALPHA BETA, TWO DOMAINS, CLEFT, TRANSFERASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.R.KUSER,S.KRAUCHENCO,O.A.ANTUNES,I.POLIKARPOV                       
REVDAT   2   24-FEB-09 1IG8    1       VERSN                                    
REVDAT   1   02-MAY-01 1IG8    0                                                
JRNL        AUTH   P.R.KUSER,S.KRAUCHENCO,O.A.ANTUNES,I.POLIKARPOV              
JRNL        TITL   THE HIGH RESOLUTION CRYSTAL STRUCTURE OF YEAST               
JRNL        TITL 2 HEXOKINASE PII WITH THE CORRECT PRIMARY SEQUENCE             
JRNL        TITL 3 PROVIDES NEW INSIGHTS INTO ITS MECHANISM OF ACTION.          
JRNL        REF    J.BIOL.CHEM.                  V. 275 20814 2000              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   10749890                                                     
JRNL        DOI    10.1074/JBC.M910412199                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.R.KUSER,A.M.GOLUBEV,I.POLIKARPOV                           
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY CRYSTAL ANALYSIS             
REMARK   1  TITL 2 OF YEAST HEXOKINASE PI AND PII                               
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  55  2047 1999              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  DOI    10.1107/S0907444999012263                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 13.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 30146                          
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1368                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3671                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 441                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.13                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.248         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.226         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.153         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.141         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.011 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.033 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.036 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1IG8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB013246.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-SEP-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 277                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : LNLS                               
REMARK 200  BEAMLINE                       : D03B-MX1                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.38                               
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
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   : 60395                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 13.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 2.120                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.82                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42000                            
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: AMORE                                                 
REMARK 200 STARTING MODEL: P152K MUTANT OF YEAST HEXOKINASE                     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.3-3.2M AMMONIUM SULPHATE, PH 7.5,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       8555   Y+1/2,-X+1/2,Z+1/2                                      
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   SMTRY1   5  1.000000  0.000000  0.000000       71.40450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       71.40450            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       29.23100            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       71.40450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       71.40450            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       29.23100            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       71.40450            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       71.40450            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       29.23100            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       71.40450            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       71.40450            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       29.23100            
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 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     PRO A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     ARG A    12                                                      
REMARK 465     LYS A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     MET A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   571     O    HOH A   630     8454     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  86   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A  93   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG A 103   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG A 103   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 199   CD  -  NE  -  CZ  ANGL. DEV. =  18.4 DEGREES          
REMARK 500    ARG A 199   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    ARG A 199   NE  -  CZ  -  NH2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    GLU A 204   CA  -  CB  -  CG  ANGL. DEV. =  16.2 DEGREES          
REMARK 500    VAL A 206   N   -  CA  -  CB  ANGL. DEV. = -14.4 DEGREES          
REMARK 500    GLU A 225   OE1 -  CD  -  OE2 ANGL. DEV. =  10.2 DEGREES          
REMARK 500    VAL A 278   N   -  CA  -  CB  ANGL. DEV. = -13.9 DEGREES          
REMARK 500    GLU A 359   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.7 DEGREES          
REMARK 500    ASP A 362   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG A 378   NE  -  CZ  -  NH2 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG A 382   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG A 383   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    ARG A 383   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    ARG A 423   CD  -  NE  -  CZ  ANGL. DEV. =  23.2 DEGREES          
REMARK 500    ARG A 423   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 474   CD  -  NE  -  CZ  ANGL. DEV. =  18.4 DEGREES          
REMARK 500    ARG A 474   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  19      119.87    -37.14                                   
REMARK 500    THR A 121      158.59    -45.65                                   
REMARK 500    SER A 158       42.75    -91.12                                   
REMARK 500    ASP A 179       78.54   -164.27                                   
REMARK 500    ASP A 242     -155.92    -99.87                                   
REMARK 500    VAL A 279      -40.55   -132.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    THR A 121        -12.63                                           
REMARK 500    THR A 213        -10.31                                           
REMARK 500    VAL A 279         11.56                                           
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 A 934        DISTANCE =  6.59 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 A 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2YHX   RELATED DB: PDB                                   
DBREF  1IG8 A    1   486  UNP    P04807   HXKB_YEAST       1    486             
SEQRES   1 A  486  MET VAL HIS LEU GLY PRO LYS LYS PRO GLN ALA ARG LYS          
SEQRES   2 A  486  GLY SER MET ALA ASP VAL PRO LYS GLU LEU MET GLN GLN          
SEQRES   3 A  486  ILE GLU ASN PHE GLU LYS ILE PHE THR VAL PRO THR GLU          
SEQRES   4 A  486  THR LEU GLN ALA VAL THR LYS HIS PHE ILE SER GLU LEU          
SEQRES   5 A  486  GLU LYS GLY LEU SER LYS LYS GLY GLY ASN ILE PRO MET          
SEQRES   6 A  486  ILE PRO GLY TRP VAL MET ASP PHE PRO THR GLY LYS GLU          
SEQRES   7 A  486  SER GLY ASP PHE LEU ALA ILE ASP LEU GLY GLY THR ASN          
SEQRES   8 A  486  LEU ARG VAL VAL LEU VAL LYS LEU GLY GLY ASP ARG THR          
SEQRES   9 A  486  PHE ASP THR THR GLN SER LYS TYR ARG LEU PRO ASP ALA          
SEQRES  10 A  486  MET ARG THR THR GLN ASN PRO ASP GLU LEU TRP GLU PHE          
SEQRES  11 A  486  ILE ALA ASP SER LEU LYS ALA PHE ILE ASP GLU GLN PHE          
SEQRES  12 A  486  PRO GLN GLY ILE SER GLU PRO ILE PRO LEU GLY PHE THR          
SEQRES  13 A  486  PHE SER PHE PRO ALA SER GLN ASN LYS ILE ASN GLU GLY          
SEQRES  14 A  486  ILE LEU GLN ARG TRP THR LYS GLY PHE ASP ILE PRO ASN          
SEQRES  15 A  486  ILE GLU ASN HIS ASP VAL VAL PRO MET LEU GLN LYS GLN          
SEQRES  16 A  486  ILE THR LYS ARG ASN ILE PRO ILE GLU VAL VAL ALA LEU          
SEQRES  17 A  486  ILE ASN ASP THR THR GLY THR LEU VAL ALA SER TYR TYR          
SEQRES  18 A  486  THR ASP PRO GLU THR LYS MET GLY VAL ILE PHE GLY THR          
SEQRES  19 A  486  GLY VAL ASN GLY ALA TYR TYR ASP VAL CYS SER ASP ILE          
SEQRES  20 A  486  GLU LYS LEU GLN GLY LYS LEU SER ASP ASP ILE PRO PRO          
SEQRES  21 A  486  SER ALA PRO MET ALA ILE ASN CYS GLU TYR GLY SER PHE          
SEQRES  22 A  486  ASP ASN GLU HIS VAL VAL LEU PRO ARG THR LYS TYR ASP          
SEQRES  23 A  486  ILE THR ILE ASP GLU GLU SER PRO ARG PRO GLY GLN GLN          
SEQRES  24 A  486  THR PHE GLU LYS MET SER SER GLY TYR TYR LEU GLY GLU          
SEQRES  25 A  486  ILE LEU ARG LEU ALA LEU MET ASP MET TYR LYS GLN GLY          
SEQRES  26 A  486  PHE ILE PHE LYS ASN GLN ASP LEU SER LYS PHE ASP LYS          
SEQRES  27 A  486  PRO PHE VAL MET ASP THR SER TYR PRO ALA ARG ILE GLU          
SEQRES  28 A  486  GLU ASP PRO PHE GLU ASN LEU GLU ASP THR ASP ASP LEU          
SEQRES  29 A  486  PHE GLN ASN GLU PHE GLY ILE ASN THR THR VAL GLN GLU          
SEQRES  30 A  486  ARG LYS LEU ILE ARG ARG LEU SER GLU LEU ILE GLY ALA          
SEQRES  31 A  486  ARG ALA ALA ARG LEU SER VAL CYS GLY ILE ALA ALA ILE          
SEQRES  32 A  486  CYS GLN LYS ARG GLY TYR LYS THR GLY HIS ILE ALA ALA          
SEQRES  33 A  486  ASP GLY SER VAL TYR ASN ARG TYR PRO GLY PHE LYS GLU          
SEQRES  34 A  486  LYS ALA ALA ASN ALA LEU LYS ASP ILE TYR GLY TRP THR          
SEQRES  35 A  486  GLN THR SER LEU ASP ASP TYR PRO ILE LYS ILE VAL PRO          
SEQRES  36 A  486  ALA GLU ASP GLY SER GLY ALA GLY ALA ALA VAL ILE ALA          
SEQRES  37 A  486  ALA LEU ALA GLN LYS ARG ILE ALA GLU GLY LYS SER VAL          
SEQRES  38 A  486  GLY ILE ILE GLY ALA                                          
HET    SO4  A 501       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  HOH   *441(H2 O)                                                    
HELIX    1   1 PRO A   20  THR A   35  1                                  16    
HELIX    2   2 PRO A   37  SER A   57  1                                  21    
HELIX    3   3 ALA A  117  THR A  121  5                                   5    
HELIX    4   4 ASP A  125  PHE A  143  1                                  19    
HELIX    5   5 ASP A  187  ARG A  199  1                                  13    
HELIX    6   6 ASN A  210  ASP A  223  1                                  14    
HELIX    7   7 SER A  245  GLN A  251  5                                   7    
HELIX    8   8 GLU A  269  PHE A  273  5                                   5    
HELIX    9   9 THR A  283  SER A  293  1                                  11    
HELIX   10  10 GLN A  299  SER A  306  1                                   8    
HELIX   11  11 TYR A  309  GLN A  324  1                                  16    
HELIX   12  12 THR A  344  ASP A  353  1                                  10    
HELIX   13  13 LEU A  358  GLY A  370  1                                  13    
HELIX   14  14 THR A  374  VAL A  397  1                                  24    
HELIX   15  15 VAL A  397  GLY A  408  1                                  12    
HELIX   16  16 GLY A  418  TYR A  424  1                                   7    
HELIX   17  17 GLY A  426  GLY A  440  1                                  15    
HELIX   18  18 SER A  445  TYR A  449  5                                   5    
HELIX   19  19 GLY A  461  GLU A  477  1                                  17    
SHEET    1   A 6 ILE A  66  PRO A  67  0                                        
SHEET    2   A 6 PRO A 263  ASN A 267 -1  N  ASN A 267   O  ILE A  66           
SHEET    3   A 6 VAL A 236  VAL A 243 -1  O  TYR A 240   N  ILE A 266           
SHEET    4   A 6 THR A 226  PHE A 232 -1  N  GLY A 229   O  ALA A 239           
SHEET    5   A 6 GLY A 412  ASP A 417  1  O  HIS A 413   N  LYS A 227           
SHEET    6   A 6 ILE A 451  PRO A 455  1  O  LYS A 452   N  ILE A 414           
SHEET    1   B 5 PHE A 105  ARG A 113  0                                        
SHEET    2   B 5 ASN A  91  GLY A 100 -1  O  LEU A  92   N  TYR A 112           
SHEET    3   B 5 SER A  79  LEU A  87 -1  O  GLY A  80   N  LEU A  99           
SHEET    4   B 5 ILE A 151  THR A 156  1  O  PRO A 152   N  LEU A  83           
SHEET    5   B 5 ILE A 203  ILE A 209  1  O  GLU A 204   N  LEU A 153           
SHEET    1   C 2 ALA A 161  SER A 162  0                                        
SHEET    2   C 2 ILE A 170  LEU A 171 -1  N  ILE A 170   O  SER A 162           
SITE     1 AC1  5 THR A 234  GLY A 418  SER A 419  HOH A 650                    
SITE     2 AC1  5 HOH A 874                                                     
CRYST1  142.809  142.809   58.462  90.00  90.00  90.00 I 4           8          
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      0.007000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017110        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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