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Database: PDB
Entry: 3O6W
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HEADER    TRANSFERASE                             29-JUL-10   3O6W              
TITLE     CRYSTAL STRUCTURE OF MONOMERIC KLHXK1 IN CRYSTAL FORM VIII (OPEN      
TITLE    2 STATE)                                                               
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 3O6W    1       JRNL                                     
REVDAT   1   13-OCT-10 3O6W    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.    1.48 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) : 1.48                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.12                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 170225                         
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) : 0.167                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.184                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1723                            
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) : 1.48                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.52                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 12500                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 129                          
REMARK   3   BIN FREE R VALUE                    : 0.2980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7269                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 45                                      
REMARK   3   SOLVENT ATOMS            : 630                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.74                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.42000                                             
REMARK   3    B22 (A**2) : 1.08000                                              
REMARK   3    B33 (A**2) : -0.95000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.67000                                             
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): 0.059         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.043         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.597         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.973                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.970                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7513 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10168 ; 1.409 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   933 ; 5.540 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   333 ;35.274 ;25.315       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1341 ;11.524 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;18.247 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1136 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5603 ; 0.007 ; 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):  4633 ; 1.272 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7510 ; 2.120 ; 4.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2880 ; 3.548 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2655 ; 5.859 ; 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):   6.1899   5.3667  17.8310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0198 T22:   0.0021                                     
REMARK   3      T33:   0.0535 T12:   0.0008                                     
REMARK   3      T13:   0.0098 T23:  -0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6001 L22:   0.7259                                     
REMARK   3      L33:   2.1071 L12:   0.0983                                     
REMARK   3      L13:   0.2875 L23:   0.2821                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0438 S12:  -0.0134 S13:  -0.0210                       
REMARK   3      S21:   0.0044 S22:  -0.0207 S23:  -0.0043                       
REMARK   3      S31:  -0.0339 S32:  -0.0294 S33:  -0.0231                       
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):  19.0435 -11.3529  -4.6582              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0764 T22:   0.0738                                     
REMARK   3      T33:   0.0776 T12:   0.0065                                     
REMARK   3      T13:  -0.0053 T23:  -0.0430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1569 L22:   1.6028                                     
REMARK   3      L33:   1.5464 L12:   0.0621                                     
REMARK   3      L13:   0.0844 L23:  -0.0027                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0366 S12:  -0.0193 S13:  -0.1784                       
REMARK   3      S21:   0.0923 S22:  -0.0278 S23:  -0.1913                       
REMARK   3      S31:   0.0997 S32:   0.1640 S33:  -0.0088                       
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):  18.3094 -15.5909 -58.4430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0616 T22:   0.0582                                     
REMARK   3      T33:   0.0685 T12:   0.0037                                     
REMARK   3      T13:  -0.0109 T23:  -0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0914 L22:   1.0276                                     
REMARK   3      L33:   2.4654 L12:   0.1223                                     
REMARK   3      L13:   0.0094 L23:   0.0401                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0145 S12:   0.0954 S13:   0.0262                       
REMARK   3      S21:  -0.2454 S22:   0.0037 S23:   0.0810                       
REMARK   3      S31:   0.0150 S32:   0.1134 S33:  -0.0182                       
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):   0.9439 -10.8974 -33.4426              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0279 T22:   0.0643                                     
REMARK   3      T33:   0.0373 T12:  -0.0260                                     
REMARK   3      T13:   0.0033 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4136 L22:   1.6986                                     
REMARK   3      L33:   0.9790 L12:   0.2250                                     
REMARK   3      L13:  -0.2630 L23:   0.0475                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0127 S12:   0.0763 S13:   0.1481                       
REMARK   3      S21:  -0.0924 S22:   0.0865 S23:   0.1507                       
REMARK   3      S31:  -0.0410 S32:  -0.0120 S33:  -0.0738                       
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 3O6W COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB060740.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.6                                
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) : 0.91841                            
REMARK 200  MONOCHROMATOR                  : SI-111 CRYSTAL                     
REMARK 200  OPTICS                         : 1ST MIRROR: SILICON, ACTIVE        
REMARK 200                                   SURFACE 50 NM RH-COATED; 2ND       
REMARK 200                                   MIRROR: GLAS, ACTIVE SURFACE 50    
REMARK 200                                   NM RH-COATED                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 171952                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.480                              
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     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.03100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.49100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
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   (%): 49.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1MICROL RESERVOIR + 1MICROL PROTEIN,     
REMARK 280  RESERVOIR: 2.4M DI-AMMONIA PHOSPHATE, 0.1M CHES PH 9.6, PROTEIN:    
REMARK 280  10MG/ML KLHXK1, 10MM TRIS PH 7.4, 1MM EDTA, 1MM DTT, 0.5MM PMSF,    
REMARK 280  1MM XYLOSE, 1MM ATP, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  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       46.79500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ARG 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     PRO 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 465     ASP A    18                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     PRO B     9                                                      
REMARK 465     PRO B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     ARG B    12                                                      
REMARK 465     LYS B    13                                                      
REMARK 465     GLY B    14                                                      
REMARK 465     SER B    15                                                      
REMARK 465     MET B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     ASP B    18                                                      
REMARK 465     VAL B    19                                                      
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    ASN A 102       57.82   -140.22                                   
REMARK 500    SER A 157       52.11    -90.62                                   
REMARK 500    ASN A 166       54.30    -91.19                                   
REMARK 500    ASP A 178       69.22   -157.03                                   
REMARK 500    VAL A 278      -33.06   -139.62                                   
REMARK 500    SER B 157       49.74    -91.21                                   
REMARK 500    ASN B 166       54.79    -90.90                                   
REMARK 500    ASP B 178       69.65   -152.20                                   
REMARK 500    ASP B 241     -162.21   -100.24                                   
REMARK 500    VAL B 278      -30.86   -138.42                                   
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 GOL A 486                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 487                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 488                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 486                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 487                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 488                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 489                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 490                 
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: 3O4W   RELATED DB: PDB                                   
REMARK 900 CRYSTAL FORM IV OF KLHXK1 (DIMER)                                    
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  3O6W A    1   485  UNP    P33284   HXK_KLULA        1    485             
DBREF  3O6W 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    GOL  A 486       6                                                       
HET    GOL  A 487       6                                                       
HET    PO4  A 488       5                                                       
HET    GOL  B 486       6                                                       
HET    GOL  B 487       6                                                       
HET    GOL  B 488       6                                                       
HET    PO4  B 489       5                                                       
HET    PO4  B 490       5                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  GOL    5(C3 H8 O3)                                                  
FORMUL   5  PO4    3(O4 P 3-)                                                   
FORMUL  11  HOH   *630(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  GLY A  121  5                                   7    
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  ALA A  476  1                                  17    
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  THR B  120  5                                   6    
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  ALA B  476  1                                  17    
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  ASN A 203   N  LEU A 152           
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  HIS B 412   N  LYS B 226           
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  92   O  TYR B 112           
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  THR B 155  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  7 ASN A 209  ASP A 210  THR A 211  GLY A 234                    
SITE     2 AC1  7 VAL A 235  ASN A 236  HOH A 579                               
SITE     1 AC2  9 PHE A 156  TYR A 158  ALA A 160  GLN A 162                    
SITE     2 AC2  9 HOH A 537  HOH A 575  HOH A 630  HOH A 684                    
SITE     3 AC2  9 HOH A 828                                                     
SITE     1 AC3  4 GLY A 232  THR A 233  GLY A 417  SER A 418                    
SITE     1 AC4  6 ASN B 209  ASP B 210  THR B 211  GLY B 234                    
SITE     2 AC4  6 VAL B 235  ASN B 236                                          
SITE     1 AC5  4 THR A 372  THR A 373  VAL A 374  ARG A 377                    
SITE     1 AC6  3 HIS B 185  ASP B 186  HOH B 551                               
SITE     1 AC7  3 THR B 233  GLY B 417  SER B 418                               
SITE     1 AC8  5 SER B  37  SER B  38  GLU B  39  HOH B 702                    
SITE     2 AC8  5 HOH B 772                                                     
CRYST1   50.540   93.590  114.290  90.00 102.42  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      0.019786  0.000000  0.004358        0.00000                         
SCALE2      0.000000  0.010685  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008959        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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