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Database: PDB
Entry: 3O5B
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HEADER    TRANSFERASE                             28-JUL-10   3O5B              
TITLE     CRYSTAL STRUCTURE OF DIMERIC KLHXK1 IN CRYSTAL FORM VII WITH GLUCOSE  
TITLE    2 BOUND (OPEN 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 3O5B    1       JRNL                                     
REVDAT   1   13-OCT-10 3O5B    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.    1.97 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) : 1.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 77579                          
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) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1153                            
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) : 1.97                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5610                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.15                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2900                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 87                           
REMARK   3   BIN FREE R VALUE                    : 0.2980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7443                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 353                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.95000                                             
REMARK   3    B22 (A**2) : 3.38000                                              
REMARK   3    B33 (A**2) : -2.43000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.161         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.135         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.868        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7648 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10366 ; 1.709 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   961 ; 5.986 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   331 ;38.263 ;25.227       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1350 ;17.820 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;20.401 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1164 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5720 ; 0.008 ; 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):  4756 ; 2.837 ; 4.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7690 ; 3.896 ; 6.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2892 ; 6.629 ; 9.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2673 ; 8.654 ;13.500       
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     1        A    76                          
REMARK   3    RESIDUE RANGE :   A   210        A   456                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.6709 -24.4836 -13.2831              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1444 T22:   0.0362                                     
REMARK   3      T33:   0.1418 T12:  -0.0477                                     
REMARK   3      T13:   0.0259 T23:  -0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5516 L22:   1.3006                                     
REMARK   3      L33:   2.4754 L12:   0.5642                                     
REMARK   3      L13:   0.1353 L23:   0.7029                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1964 S12:   0.2117 S13:  -0.1449                       
REMARK   3      S21:  -0.1765 S22:   0.1128 S23:  -0.0388                       
REMARK   3      S31:   0.3383 S32:  -0.0261 S33:   0.0836                       
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):  25.0323 -15.8539   5.8149              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0777 T22:   0.0306                                     
REMARK   3      T33:   0.1144 T12:   0.0234                                     
REMARK   3      T13:  -0.0025 T23:   0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9365 L22:   1.8767                                     
REMARK   3      L33:   2.6107 L12:  -1.1952                                     
REMARK   3      L13:  -0.6664 L23:  -0.5610                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1387 S12:  -0.1759 S13:  -0.0402                       
REMARK   3      S21:  -0.0032 S22:   0.0169 S23:  -0.1692                       
REMARK   3      S31:   0.1883 S32:   0.2503 S33:   0.1218                       
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     1        B    76                          
REMARK   3    RESIDUE RANGE :   B   210        B   456                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.1853  -8.0920 -35.0681              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0853 T22:   0.1825                                     
REMARK   3      T33:   0.1334 T12:  -0.1111                                     
REMARK   3      T13:   0.0018 T23:   0.0241                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7135 L22:   0.3644                                     
REMARK   3      L33:   6.4876 L12:  -0.5064                                     
REMARK   3      L13:   2.3725 L23:  -0.6239                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2719 S12:   0.3046 S13:   0.0807                       
REMARK   3      S21:   0.0402 S22:  -0.0374 S23:  -0.0206                       
REMARK   3      S31:  -0.3064 S32:   0.6295 S33:   0.3092                       
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):  14.9578 -21.5633 -54.6660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2193 T22:   0.2741                                     
REMARK   3      T33:   0.1636 T12:  -0.1247                                     
REMARK   3      T13:   0.0154 T23:  -0.0456                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5918 L22:   2.8830                                     
REMARK   3      L33:   4.8119 L12:   0.3576                                     
REMARK   3      L13:  -0.7478 L23:  -0.8113                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0754 S12:  -0.0227 S13:  -0.4093                       
REMARK   3      S21:  -0.1213 S22:  -0.0677 S23:   0.0253                       
REMARK   3      S31:   0.8289 S32:  -0.1943 S33:   0.1431                       
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 3O5B 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 RCSB060683.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8148                             
REMARK 200  MONOCHROMATOR                  : SI (111), HORIZONTALLY FOCUSSING   
REMARK 200  OPTICS                         : BENT, VERTICALLY FOCUSSING         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : MAR555 FLAT PANEL                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 78731                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.970                              
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                : 4.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.03500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.49200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.870                              
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   (%): 52.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1MICROL RESERVOIR + 1MICROL PROTEIN,     
REMARK 280  RESERVOIR: 18% PEG6000, 0.9M LICL, 2MM MGCL2, 0.1M BICINE PH 9.0,   
REMARK 280  PROTEIN: 10MG/ML KLHXK1, 10MM TRIS PH 7.4, 1MM EDTA, 1MM DTT,       
REMARK 280  0.5MM PMSF, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       49.07000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.10000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.07000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.10000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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 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     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     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 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 B  39   CG    GLU B  39   CD      0.094                       
REMARK 500    GLU B  39   CD    GLU B  39   OE2     0.072                       
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    ASN A 166       41.03    -93.93                                   
REMARK 500    ASP A 241     -162.64   -103.61                                   
REMARK 500    ARG A 294       76.78   -115.59                                   
REMARK 500    ALA A 411      145.45   -174.18                                   
REMARK 500    VAL A 480       30.44   -140.07                                   
REMARK 500    ASN B 166       46.55    -96.55                                   
REMARK 500    ASP B 178       67.83   -156.81                                   
REMARK 500    LYS B 248       -9.68    -56.67                                   
REMARK 500    HIS B 276       51.82     73.55                                   
REMARK 500    ARG B 294       70.62   -117.16                                   
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 BGC A 486                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 487                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 488                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC B 486                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 487                 
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: 3O6W   RELATED DB: PDB                                   
REMARK 900 RYSTAL FORM VIII OF KLHXK1 (MONOMER)                                 
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  3O5B A    1   485  UNP    P33284   HXK_KLULA        1    485             
DBREF  3O5B 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    BGC  A 486      12                                                       
HET    SO4  A 487       5                                                       
HET    SO4  A 488       5                                                       
HET    BGC  B 486      12                                                       
HET    SO4  B 487       5                                                       
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  BGC    2(C6 H12 O6)                                                 
FORMUL   4  SO4    3(O4 S 2-)                                                   
FORMUL   8  HOH   *353(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 THR A  343  ASP A  352  1                                  10    
HELIX   13  13 LEU A  357  ASN A  369  1                                  13    
HELIX   14  14 THR A  373  GLY A  407  1                                  35    
HELIX   15  15 GLY A  417  TYR A  423  1                                   7    
HELIX   16  16 GLY A  425  ASN A  439  1                                  15    
HELIX   17  17 LYS A  444  HIS A  448  5                                   5    
HELIX   18  18 GLY A  460  GLY A  477  1                                  18    
HELIX   19  19 PRO B   20  THR B   35  1                                  16    
HELIX   20  20 SER B   37  SER B   57  1                                  21    
HELIX   21  21 PRO B  115  GLY B  121  5                                   7    
HELIX   22  22 THR B  122  TYR B  142  1                                  21    
HELIX   23  23 ASP B  186  LYS B  197  1                                  12    
HELIX   24  24 ASN B  209  ASP B  222  1                                  14    
HELIX   25  25 SER B  244  GLU B  250  5                                   7    
HELIX   26  26 GLU B  268  PHE B  272  5                                   5    
HELIX   27  27 THR B  282  SER B  292  1                                  11    
HELIX   28  28 GLN B  298  SER B  305  1                                   8    
HELIX   29  29 TYR B  308  SER B  323  1                                  16    
HELIX   30  30 ILE B  332  GLU B  337  5                                   6    
HELIX   31  31 THR B  343  ASP B  352  1                                  10    
HELIX   32  32 LEU B  357  ASN B  369  1                                  13    
HELIX   33  33 THR B  373  GLY B  407  1                                  35    
HELIX   34  34 GLY B  417  TYR B  423  1                                   7    
HELIX   35  35 GLY B  425  ASN B  439  1                                  15    
HELIX   36  36 LYS B  444  HIS B  448  5                                   5    
HELIX   37  37 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  ASP A 241   O  MET A 263           
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  ALA A 414   N  ILE A 229           
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  96   O  THR A 108           
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  PHE A 156  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  GLN B 451   N  ILE B 413           
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  ASN B 203   N  LEU B 152           
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 11 ASN A 209  ASP A 210  THR A 211  ILE A 230                    
SITE     2 AC1 11 GLY A 234  VAL A 235  ASN A 236  GLU A 268                    
SITE     3 AC1 11 GLU A 301  SO4 A 487  SO4 A 488                               
SITE     1 AC2  6 GLY A 232  THR A 233  GLY A 417  SER A 418                    
SITE     2 AC2  6 BGC A 486  SO4 A 488                                          
SITE     1 AC3  4 THR A 233  GLY A 234  BGC A 486  SO4 A 487                    
SITE     1 AC4  9 ASN B 209  ASP B 210  THR B 211  GLY B 234                    
SITE     2 AC4  9 VAL B 235  ASN B 236  GLU B 268  GLU B 301                    
SITE     3 AC4  9 SO4 B 487                                                     
SITE     1 AC5  4 THR B 233  GLY B 417  SER B 418  BGC B 486                    
CRYST1   98.140  122.200   92.300  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010190  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008183  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010834        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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