GenomeNet

Database: PDB
Entry: 3O4W
LinkDB: 3O4W
Original site: 3O4W 
HEADER    TRANSFERASE                             27-JUL-10   3O4W              
TITLE     CRYSTAL STRUCTURE OF DIMERIC KLHXK1 IN CRYSTAL FORM IV                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEXOKINASE;                                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.7.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE   3 ORGANISM_COMMON: YEAST;                                              
SOURCE   4 ORGANISM_TAXID: 28985;                                               
SOURCE   5 STRAIN: CBS2359/152;                                                 
SOURCE   6 GENE: KLLA0D11352G, RAG5;                                            
SOURCE   7 EXPRESSION_SYSTEM: KLUYVEROMYCES LACTIS;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 28985;                                      
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: JA6-DELTA-RAG5;                            
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PTS32X;                               
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PTSRAG5                                   
KEYWDS    RNASEH-LIKE FOLD, HEXOKINASE, GLYCOLYSIS, GLUCOSE REPRESSION, ATP     
KEYWDS   2 BINDING, MIG1 BINDING, TRANSFERASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.B.KUETTNER,K.KETTNER,A.KEIM,T.M.KRIEGEL,N.STRATER                   
REVDAT   2   29-DEC-10 3O4W    1       JRNL                                     
REVDAT   1   13-OCT-10 3O4W    0                                                
JRNL        AUTH   E.B.KUETTNER,K.KETTNER,A.KEIM,D.I.SVERGUN,D.VOLKE,D.SINGER,  
JRNL        AUTH 2 R.HOFFMANN,E.C.MULLER,A.OTTO,T.M.KRIEGEL,N.STRATER           
JRNL        TITL   CRYSTAL STRUCTURE OF HEXOKINASE KLHXK1 OF KLUYVEROMYCES      
JRNL        TITL 2 LACTIS: A MOLECULAR BASIS FOR UNDERSTANDING THE CONTROL OF   
JRNL        TITL 3 YEAST HEXOKINASE FUNCTIONS VIA COVALENT MODIFICATION AND     
JRNL        TITL 4 OLIGOMERIZATION.                                             
JRNL        REF    J.BIOL.CHEM.                  V. 285 41019 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20943665                                                     
JRNL        DOI    10.1074/JBC.M110.185850                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.B.KUETTNER,T.M.KRIEGEL,A.KEIM,M.NAUMANN,N.STRATER          
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES OF 
REMARK   1  TITL 2 HEXOKINASE KLHXK1 FROM KLUYVEROMYCES LACTIS                  
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  63   430 2007              
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  PMID   17565189                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 128436                         
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) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1293                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.61                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.65                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10700                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.77                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2160                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 121                          
REMARK   3   BIN FREE R VALUE                    : 0.2940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7526                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 154                                     
REMARK   3   SOLVENT ATOMS            : 819                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.27                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.53000                                              
REMARK   3    B22 (A**2) : 0.05000                                              
REMARK   3    B33 (A**2) : -0.27000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.43000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.096         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.060         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.356         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7854 ; 0.023 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10636 ; 2.094 ; 1.997       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   966 ; 5.978 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   337 ;35.057 ;25.104       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1384 ;13.964 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    35 ;19.111 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1174 ; 0.140 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5789 ; 0.013 ; 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):  4811 ; 1.985 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7793 ; 2.858 ; 4.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3043 ; 4.559 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2843 ; 6.848 ; 9.000       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A    76                          
REMARK   3    RESIDUE RANGE :   A   210        A   456                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.8432   1.0550  21.6068              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0099 T22:   0.0245                                     
REMARK   3      T33:   0.0393 T12:   0.0063                                     
REMARK   3      T13:   0.0011 T23:  -0.0157                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4027 L22:   0.6101                                     
REMARK   3      L33:   1.6190 L12:   0.0112                                     
REMARK   3      L13:   0.1125 L23:  -0.7130                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0176 S12:  -0.0630 S13:  -0.0258                       
REMARK   3      S21:   0.0188 S22:  -0.0175 S23:  -0.0292                       
REMARK   3      S31:   0.0518 S32:   0.0389 S33:   0.0351                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    77        A   209                          
REMARK   3    RESIDUE RANGE :   A   457        A   485                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.1440  -2.8701  -5.4100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0316 T22:   0.0303                                     
REMARK   3      T33:   0.0133 T12:  -0.0043                                     
REMARK   3      T13:  -0.0092 T23:  -0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1147 L22:   1.9782                                     
REMARK   3      L33:   1.0078 L12:   0.7043                                     
REMARK   3      L13:  -0.5326 L23:  -0.0084                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0351 S12:   0.0141 S13:  -0.0540                       
REMARK   3      S21:  -0.0913 S22:  -0.0167 S23:   0.0467                       
REMARK   3      S31:   0.0753 S32:  -0.0235 S33:   0.0518                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B    76                          
REMARK   3    RESIDUE RANGE :   B   210        B   456                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.7127  -1.5220  28.6563              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0069 T22:   0.0203                                     
REMARK   3      T33:   0.0362 T12:   0.0018                                     
REMARK   3      T13:  -0.0047 T23:   0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4512 L22:   0.6491                                     
REMARK   3      L33:   1.8069 L12:  -0.0398                                     
REMARK   3      L13:  -0.1657 L23:   0.8048                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0332 S12:   0.0233 S13:  -0.0350                       
REMARK   3      S21:  -0.0211 S22:  -0.0199 S23:   0.0245                       
REMARK   3      S31:  -0.0144 S32:  -0.0486 S33:   0.0531                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    77        B   209                          
REMARK   3    RESIDUE RANGE :   B   457        B   485                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.9701  -1.9353  55.8456              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0761 T22:   0.0610                                     
REMARK   3      T33:   0.0585 T12:   0.0213                                     
REMARK   3      T13:  -0.0181 T23:  -0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4011 L22:   2.2104                                     
REMARK   3      L33:   2.0804 L12:  -0.5635                                     
REMARK   3      L13:  -0.8404 L23:   0.3910                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1422 S12:  -0.0322 S13:  -0.2381                       
REMARK   3      S21:   0.2046 S22:   0.1073 S23:  -0.2018                       
REMARK   3      S31:   0.2792 S32:   0.1593 S33:   0.0349                       
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. FULL B FACTORS AND ANISO RECORDS WERE COMPUTED BY CCP4   
REMARK   3  PROGRAMM TLSANL.                                                    
REMARK   4                                                                      
REMARK   4 3O4W COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB060668.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.2                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : SI - 111 TRIANGULAR CRYSTAL        
REMARK 200  OPTICS                         : SI, COATED WITH 200 LAYERS OF      
REMARK 200                                   MO/SI                              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 129734                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.610                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.0                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.65                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.50800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
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: PDB ENTRY 3O08                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1MICROL RESERVOIR + 1MICROL PROTEIN,     
REMARK 280  RESERVOIR: 2.5M AMMONIA SULFATE, 0.1M CHES PH 9.5, PROTEIN: 10MG/   
REMARK 280  ML KLHXK1, 10MM TRIS PH 7.4, 1MM EDTA, 1MM DTT, 0.5MM PMSF, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 292K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       45.99500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -221.0 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 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     MET B     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 301   CD    GLU A 301   OE1     0.067                       
REMARK 500    GLU B 301   CD    GLU B 301   OE1     0.067                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  42   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A  93   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 119   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 119   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 281   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ASP A 289   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A 416   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG B  93   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP B 116   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP B 416   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 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    ARG A   3     -128.06     52.31                                   
REMARK 500    ASN A 102       54.01   -140.53                                   
REMARK 500    ASN A 166       51.34    -95.10                                   
REMARK 500    ASP A 178       88.26   -157.63                                   
REMARK 500    ALA A 411      146.26   -170.44                                   
REMARK 500    ARG B   3     -135.43     64.32                                   
REMARK 500    SER B 157       57.93    -93.45                                   
REMARK 500    ASN B 166       54.96    -98.85                                   
REMARK 500    LYS B 175       39.33     87.54                                   
REMARK 500    ASP B 178       69.39   -152.64                                   
REMARK 500    ASP B 241     -165.50   -102.04                                   
REMARK 500    VAL B 278      -31.13   -136.72                                   
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 NHE A 486                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE A 487                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 488                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 489                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 490                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 491                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 492                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 493                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 494                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 495                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 496                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 497                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE B 486                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE B 487                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 488                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 489                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 490                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 491                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 492                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 493                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 494                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 495                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 496                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3O08   RELATED DB: PDB                                   
REMARK 900 CRYSTAL FORM I OF KLHXK1 (DIMER)                                     
REMARK 900 RELATED ID: 3O1B   RELATED DB: PDB                                   
REMARK 900 CRYSTAL FORM II OF KLHXK1 (DIMER)                                    
REMARK 900 RELATED ID: 3O1W   RELATED DB: PDB                                   
REMARK 900 CRYSTAL FORM III OF KLHXK1 (DIMER)                                   
REMARK 900 RELATED ID: 3O6W   RELATED DB: PDB                                   
REMARK 900 CRYSTAL FORM VIII OF KLHXK1 (MONOMER)                                
REMARK 900 RELATED ID: 3O5B   RELATED DB: PDB                                   
REMARK 900 CRYSTAL FORM VII OF KLHXK1 (DIMER) WITH GLUCOSE BOUND                
REMARK 900 RELATED ID: 3O80   RELATED DB: PDB                                   
REMARK 900 CRYSTAL FORM IX OF KLHXK1 (MONOMER)                                  
REMARK 900 RELATED ID: 3O8M   RELATED DB: PDB                                   
REMARK 900 CRYSTAL FORM XI OF KLHXK1 (MONONER) WITH GLUCOSE BOUND               
DBREF  3O4W A    1   485  UNP    P33284   HXK_KLULA        1    485             
DBREF  3O4W B    1   485  UNP    P33284   HXK_KLULA        1    485             
SEQRES   1 A  485  MET VAL ARG LEU GLY PRO LYS LYS PRO PRO ALA ARG LYS          
SEQRES   2 A  485  GLY SER MET ALA ASP VAL PRO ALA ASN LEU MET GLU GLN          
SEQRES   3 A  485  ILE HIS GLY LEU GLU THR LEU PHE THR VAL SER SER GLU          
SEQRES   4 A  485  LYS MET ARG SER ILE VAL LYS HIS PHE ILE SER GLU LEU          
SEQRES   5 A  485  ASP LYS GLY LEU SER LYS LYS GLY GLY ASN ILE PRO MET          
SEQRES   6 A  485  ILE PRO GLY TRP VAL VAL GLU TYR PRO THR GLY LYS GLU          
SEQRES   7 A  485  THR GLY ASP PHE LEU ALA LEU ASP LEU GLY GLY THR ASN          
SEQRES   8 A  485  LEU ARG VAL VAL LEU VAL LYS LEU GLY GLY ASN HIS ASP          
SEQRES   9 A  485  PHE ASP THR THR GLN ASN LYS TYR ARG LEU PRO ASP HIS          
SEQRES  10 A  485  LEU ARG THR GLY THR SER GLU GLN LEU TRP SER PHE ILE          
SEQRES  11 A  485  ALA LYS CYS LEU LYS GLU PHE VAL ASP GLU TRP TYR PRO          
SEQRES  12 A  485  ASP GLY VAL SER GLU PRO LEU PRO LEU GLY PHE THR PHE          
SEQRES  13 A  485  SER TYR PRO ALA SER GLN LYS LYS ILE ASN SER GLY VAL          
SEQRES  14 A  485  LEU GLN ARG TRP THR LYS GLY PHE ASP ILE GLU GLY VAL          
SEQRES  15 A  485  GLU GLY HIS ASP VAL VAL PRO MET LEU GLN GLU GLN ILE          
SEQRES  16 A  485  GLU LYS LEU ASN ILE PRO ILE ASN VAL VAL ALA LEU ILE          
SEQRES  17 A  485  ASN ASP THR THR GLY THR LEU VAL ALA SER LEU TYR THR          
SEQRES  18 A  485  ASP PRO GLN THR LYS MET GLY ILE ILE ILE GLY THR GLY          
SEQRES  19 A  485  VAL ASN GLY ALA TYR TYR ASP VAL VAL SER GLY ILE GLU          
SEQRES  20 A  485  LYS LEU GLU GLY LEU LEU PRO GLU ASP ILE GLY PRO ASP          
SEQRES  21 A  485  SER PRO MET ALA ILE ASN CYS GLU TYR GLY SER PHE ASP          
SEQRES  22 A  485  ASN GLU HIS LEU VAL LEU PRO ARG THR LYS TYR ASP VAL          
SEQRES  23 A  485  ILE ILE ASP GLU GLU SER PRO ARG PRO GLY GLN GLN ALA          
SEQRES  24 A  485  PHE GLU LYS MET THR SER GLY TYR TYR LEU GLY GLU ILE          
SEQRES  25 A  485  MET ARG LEU VAL LEU LEU ASP LEU TYR ASP SER GLY PHE          
SEQRES  26 A  485  ILE PHE LYS ASP GLN ASP ILE SER LYS LEU LYS GLU ALA          
SEQRES  27 A  485  TYR VAL MET ASP THR SER TYR PRO SER LYS ILE GLU ASP          
SEQRES  28 A  485  ASP PRO PHE GLU ASN LEU GLU ASP THR ASP ASP LEU PHE          
SEQRES  29 A  485  LYS THR ASN LEU ASN ILE GLU THR THR VAL VAL GLU ARG          
SEQRES  30 A  485  LYS LEU ILE ARG LYS LEU ALA GLU LEU VAL GLY THR ARG          
SEQRES  31 A  485  ALA ALA ARG LEU THR VAL CYS GLY VAL SER ALA ILE CYS          
SEQRES  32 A  485  ASP LYS ARG GLY TYR LYS THR ALA HIS ILE ALA ALA ASP          
SEQRES  33 A  485  GLY SER VAL PHE ASN ARG TYR PRO GLY TYR LYS GLU LYS          
SEQRES  34 A  485  ALA ALA GLN ALA LEU LYS ASP ILE TYR ASN TRP ASP VAL          
SEQRES  35 A  485  GLU LYS MET GLU ASP HIS PRO ILE GLN LEU VAL ALA ALA          
SEQRES  36 A  485  GLU ASP GLY SER GLY VAL GLY ALA ALA ILE ILE ALA CYS          
SEQRES  37 A  485  LEU THR GLN LYS ARG LEU ALA ALA GLY LYS SER VAL GLY          
SEQRES  38 A  485  ILE LYS GLY GLU                                              
SEQRES   1 B  485  MET VAL ARG LEU GLY PRO LYS LYS PRO PRO ALA ARG LYS          
SEQRES   2 B  485  GLY SER MET ALA ASP VAL PRO ALA ASN LEU MET GLU GLN          
SEQRES   3 B  485  ILE HIS GLY LEU GLU THR LEU PHE THR VAL SER SER GLU          
SEQRES   4 B  485  LYS MET ARG SER ILE VAL LYS HIS PHE ILE SER GLU LEU          
SEQRES   5 B  485  ASP LYS GLY LEU SER LYS LYS GLY GLY ASN ILE PRO MET          
SEQRES   6 B  485  ILE PRO GLY TRP VAL VAL GLU TYR PRO THR GLY LYS GLU          
SEQRES   7 B  485  THR GLY ASP PHE LEU ALA LEU ASP LEU GLY GLY THR ASN          
SEQRES   8 B  485  LEU ARG VAL VAL LEU VAL LYS LEU GLY GLY ASN HIS ASP          
SEQRES   9 B  485  PHE ASP THR THR GLN ASN LYS TYR ARG LEU PRO ASP HIS          
SEQRES  10 B  485  LEU ARG THR GLY THR SER GLU GLN LEU TRP SER PHE ILE          
SEQRES  11 B  485  ALA LYS CYS LEU LYS GLU PHE VAL ASP GLU TRP TYR PRO          
SEQRES  12 B  485  ASP GLY VAL SER GLU PRO LEU PRO LEU GLY PHE THR PHE          
SEQRES  13 B  485  SER TYR PRO ALA SER GLN LYS LYS ILE ASN SER GLY VAL          
SEQRES  14 B  485  LEU GLN ARG TRP THR LYS GLY PHE ASP ILE GLU GLY VAL          
SEQRES  15 B  485  GLU GLY HIS ASP VAL VAL PRO MET LEU GLN GLU GLN ILE          
SEQRES  16 B  485  GLU LYS LEU ASN ILE PRO ILE ASN VAL VAL ALA LEU ILE          
SEQRES  17 B  485  ASN ASP THR THR GLY THR LEU VAL ALA SER LEU TYR THR          
SEQRES  18 B  485  ASP PRO GLN THR LYS MET GLY ILE ILE ILE GLY THR GLY          
SEQRES  19 B  485  VAL ASN GLY ALA TYR TYR ASP VAL VAL SER GLY ILE GLU          
SEQRES  20 B  485  LYS LEU GLU GLY LEU LEU PRO GLU ASP ILE GLY PRO ASP          
SEQRES  21 B  485  SER PRO MET ALA ILE ASN CYS GLU TYR GLY SER PHE ASP          
SEQRES  22 B  485  ASN GLU HIS LEU VAL LEU PRO ARG THR LYS TYR ASP VAL          
SEQRES  23 B  485  ILE ILE ASP GLU GLU SER PRO ARG PRO GLY GLN GLN ALA          
SEQRES  24 B  485  PHE GLU LYS MET THR SER GLY TYR TYR LEU GLY GLU ILE          
SEQRES  25 B  485  MET ARG LEU VAL LEU LEU ASP LEU TYR ASP SER GLY PHE          
SEQRES  26 B  485  ILE PHE LYS ASP GLN ASP ILE SER LYS LEU LYS GLU ALA          
SEQRES  27 B  485  TYR VAL MET ASP THR SER TYR PRO SER LYS ILE GLU ASP          
SEQRES  28 B  485  ASP PRO PHE GLU ASN LEU GLU ASP THR ASP ASP LEU PHE          
SEQRES  29 B  485  LYS THR ASN LEU ASN ILE GLU THR THR VAL VAL GLU ARG          
SEQRES  30 B  485  LYS LEU ILE ARG LYS LEU ALA GLU LEU VAL GLY THR ARG          
SEQRES  31 B  485  ALA ALA ARG LEU THR VAL CYS GLY VAL SER ALA ILE CYS          
SEQRES  32 B  485  ASP LYS ARG GLY TYR LYS THR ALA HIS ILE ALA ALA ASP          
SEQRES  33 B  485  GLY SER VAL PHE ASN ARG TYR PRO GLY TYR LYS GLU LYS          
SEQRES  34 B  485  ALA ALA GLN ALA LEU LYS ASP ILE TYR ASN TRP ASP VAL          
SEQRES  35 B  485  GLU LYS MET GLU ASP HIS PRO ILE GLN LEU VAL ALA ALA          
SEQRES  36 B  485  GLU ASP GLY SER GLY VAL GLY ALA ALA ILE ILE ALA CYS          
SEQRES  37 B  485  LEU THR GLN LYS ARG LEU ALA ALA GLY LYS SER VAL GLY          
SEQRES  38 B  485  ILE LYS GLY GLU                                              
HET    NHE  A 486      13                                                       
HET    NHE  A 487      13                                                       
HET    GOL  A 488       6                                                       
HET    SO4  A 489       5                                                       
HET    SO4  A 490       5                                                       
HET    SO4  A 491       5                                                       
HET    SO4  A 492       5                                                       
HET    SO4  A 493       5                                                       
HET    SO4  A 494       5                                                       
HET    SO4  A 495       5                                                       
HET    SO4  A 496       5                                                       
HET    SO4  A 497       5                                                       
HET    SO4  A 498       5                                                       
HET    NHE  B 486      13                                                       
HET    NHE  B 487      13                                                       
HET    GOL  B 488       6                                                       
HET    SO4  B 489       5                                                       
HET    SO4  B 490       5                                                       
HET    SO4  B 491       5                                                       
HET    SO4  B 492       5                                                       
HET    SO4  B 493       5                                                       
HET    SO4  B 494       5                                                       
HET    SO4  B 495       5                                                       
HET    SO4  B 496       5                                                       
HETNAM     NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID                        
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     NHE N-CYCLOHEXYLTAURINE; CHES                                        
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NHE    4(C8 H17 N O3 S)                                             
FORMUL   5  GOL    2(C3 H8 O3)                                                  
FORMUL   6  SO4    18(O4 S 2-)                                                  
FORMUL  27  HOH   *819(H2 O)                                                    
HELIX    1   1 PRO A   20  THR A   35  1                                  16    
HELIX    2   2 SER A   37  SER A   57  1                                  21    
HELIX    3   3 PRO A  115  THR A  120  5                                   6    
HELIX    4   4 THR A  122  TYR A  142  1                                  21    
HELIX    5   5 ASP A  186  LEU A  198  1                                  13    
HELIX    6   6 ASN A  209  ASP A  222  1                                  14    
HELIX    7   7 SER A  244  GLU A  250  5                                   7    
HELIX    8   8 GLU A  268  PHE A  272  5                                   5    
HELIX    9   9 THR A  282  SER A  292  1                                  11    
HELIX   10  10 GLN A  298  SER A  305  1                                   8    
HELIX   11  11 TYR A  308  SER A  323  1                                  16    
HELIX   12  12 ILE A  332  GLU A  337  5                                   6    
HELIX   13  13 THR A  343  ASP A  352  1                                  10    
HELIX   14  14 LEU A  357  ASN A  369  1                                  13    
HELIX   15  15 THR A  373  GLY A  407  1                                  35    
HELIX   16  16 GLY A  417  TYR A  423  1                                   7    
HELIX   17  17 GLY A  425  ASN A  439  1                                  15    
HELIX   18  18 LYS A  444  HIS A  448  5                                   5    
HELIX   19  19 GLY A  460  GLY A  477  1                                  18    
HELIX   20  20 PRO B   20  THR B   35  1                                  16    
HELIX   21  21 SER B   37  SER B   57  1                                  21    
HELIX   22  22 PRO B  115  ARG B  119  5                                   5    
HELIX   23  23 THR B  122  TYR B  142  1                                  21    
HELIX   24  24 ASP B  186  LEU B  198  1                                  13    
HELIX   25  25 ASN B  209  ASP B  222  1                                  14    
HELIX   26  26 SER B  244  GLU B  250  5                                   7    
HELIX   27  27 GLU B  268  PHE B  272  5                                   5    
HELIX   28  28 THR B  282  GLU B  291  1                                  10    
HELIX   29  29 GLN B  298  SER B  305  1                                   8    
HELIX   30  30 TYR B  308  SER B  323  1                                  16    
HELIX   31  31 ILE B  332  GLU B  337  5                                   6    
HELIX   32  32 THR B  343  ASP B  352  1                                  10    
HELIX   33  33 LEU B  357  ASN B  369  1                                  13    
HELIX   34  34 THR B  373  GLY B  407  1                                  35    
HELIX   35  35 GLY B  417  TYR B  423  1                                   7    
HELIX   36  36 GLY B  425  ASN B  439  1                                  15    
HELIX   37  37 LYS B  444  HIS B  448  5                                   5    
HELIX   38  38 GLY B  460  GLY B  477  1                                  18    
SHEET    1   A 6 ILE A  66  PRO A  67  0                                        
SHEET    2   A 6 PRO A 262  ASN A 266 -1  O  ASN A 266   N  ILE A  66           
SHEET    3   A 6 VAL A 235  VAL A 242 -1  N  TYR A 239   O  ILE A 265           
SHEET    4   A 6 THR A 225  ILE A 231 -1  N  ILE A 230   O  ASN A 236           
SHEET    5   A 6 ALA A 411  ASP A 416  1  O  HIS A 412   N  LYS A 226           
SHEET    6   A 6 ILE A 450  ALA A 454  1  O  VAL A 453   N  ALA A 415           
SHEET    1   B 5 PHE A 105  ARG A 113  0                                        
SHEET    2   B 5 ASN A  91  GLY A 100 -1  N  LEU A  92   O  TYR A 112           
SHEET    3   B 5 THR A  79  LEU A  87 -1  N  PHE A  82   O  VAL A  97           
SHEET    4   B 5 LEU A 150  THR A 155  1  O  THR A 155   N  LEU A  85           
SHEET    5   B 5 ILE A 202  ILE A 208  1  O  ALA A 206   N  PHE A 154           
SHEET    1   C 2 ALA A 160  SER A 161  0                                        
SHEET    2   C 2 VAL A 169  LEU A 170 -1  O  VAL A 169   N  SER A 161           
SHEET    1   D 6 ILE B  66  PRO B  67  0                                        
SHEET    2   D 6 PRO B 262  ASN B 266 -1  O  ASN B 266   N  ILE B  66           
SHEET    3   D 6 VAL B 235  VAL B 242 -1  N  TYR B 239   O  ILE B 265           
SHEET    4   D 6 THR B 225  ILE B 231 -1  N  ILE B 230   O  ASN B 236           
SHEET    5   D 6 ALA B 411  ASP B 416  1  O  ALA B 414   N  ILE B 229           
SHEET    6   D 6 ILE B 450  ALA B 454  1  O  VAL B 453   N  ALA B 415           
SHEET    1   E 5 PHE B 105  ARG B 113  0                                        
SHEET    2   E 5 ASN B  91  GLY B 100 -1  N  LEU B  96   O  THR B 108           
SHEET    3   E 5 THR B  79  LEU B  87 -1  N  PHE B  82   O  VAL B  97           
SHEET    4   E 5 LEU B 150  PHE B 156  1  O  THR B 155   N  LEU B  85           
SHEET    5   E 5 ILE B 202  ILE B 208  1  O  ALA B 206   N  PHE B 154           
SHEET    1   F 2 ALA B 160  SER B 161  0                                        
SHEET    2   F 2 VAL B 169  LEU B 170 -1  O  VAL B 169   N  SER B 161           
SITE     1 AC1  9 TYR A 112  GLU A 136  HOH A 782  ASN B 356                    
SITE     2 AC1  9 VAL B 374  ARG B 377  SO4 B 496  HOH B 732                    
SITE     3 AC1  9 HOH B 889                                                     
SITE     1 AC2  2 HIS A 117  GLN A 125                                          
SITE     1 AC3  8 ASN A 209  ASP A 210  THR A 211  ILE A 230                    
SITE     2 AC3  8 GLY A 234  VAL A 235  ASN A 236  VAL B   2                    
SITE     1 AC4  5 THR A  90  ASN A  91  LYS A 111  ARG A 113                    
SITE     2 AC4  5 HOH A 742                                                     
SITE     1 AC5  8 GLY A 232  THR A 233  GLY A 417  SER A 418                    
SITE     2 AC5  8 HOH A 635  HOH A 749  VAL B   2  ARG B   3                    
SITE     1 AC6  4 GLU A 180  GLY A 181  HOH A 541  HOH A 557                    
SITE     1 AC7  5 SER A 292  ARG A 294  GLN A 298  LYS A 302                    
SITE     2 AC7  5 TYR A 308                                                     
SITE     1 AC8  3 GLN A 432  LYS A 435  HOH A 516                               
SITE     1 AC9  3 LYS A 444  MET A 445  HOH A 593                               
SITE     1 BC1  3 SER A  15  MET A  16  ALA A  17                               
SITE     1 BC2  3 PRO A  20  ALA A  21  HOH A 804                               
SITE     1 BC3  5 GLY A 417  SER A 418  ASN A 421  ARG A 422                    
SITE     2 BC3  5 ARG B   3                                                     
SITE     1 BC4  4 GLU A  39  ARG A  42  LYS A  46  HOH A 663                    
SITE     1 BC5 12 LYS A  40  HIS A 276  LEU A 277  VAL A 278                    
SITE     2 BC5 12 LEU A 279  HOH A 890  THR B  32  LEU B  33                    
SITE     3 BC5 12 LYS B  40  HOH B 533  HOH B 569  HOH B 893                    
SITE     1 BC6  7 ASN A 356  VAL A 374  ARG A 377  TYR B 112                    
SITE     2 BC6  7 CYS B 133  GLU B 136  HOH B 631                               
SITE     1 BC7  8 VAL A   2  ASN B 209  ASP B 210  THR B 211                    
SITE     2 BC7  8 GLY B 234  ASN B 236  HOH B 683  HOH B 775                    
SITE     1 BC8  6 VAL A   2  GLY B 232  THR B 233  GLY B 417                    
SITE     2 BC8  6 SER B 418  HOH B 794                                          
SITE     1 BC9  2 GLN B 432  LYS B 435                                          
SITE     1 CC1  5 SER B 292  ARG B 294  GLN B 298  LYS B 302                    
SITE     2 CC1  5 TYR B 308                                                     
SITE     1 CC2  5 PHE B 420  LYS B 427  VAL B 453  ALA B 454                    
SITE     2 CC2  5 HOH B 518                                                     
SITE     1 CC3  4 THR B  90  ASN B  91  LYS B 111  ARG B 113                    
SITE     1 CC4  8 LYS A 283  HIS B 276  ARG B 281  VAL B 286                    
SITE     2 CC4  8 HOH B 564  HOH B 680  HOH B 793  HOH B 873                    
SITE     1 CC5  3 PRO B  20  ALA B  21  HOH B 531                               
SITE     1 CC6  6 NHE A 486  HOH A 790  THR B 373  VAL B 374                    
SITE     2 CC6  6 HOH B 559  HOH B 732                                          
CRYST1   73.710   91.990   92.580  90.00 110.92  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013567  0.000000  0.005186        0.00000                         
SCALE2      0.000000  0.010871  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011564        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system