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Database: PDB
Entry: 3HM8
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HEADER    TRANSFERASE                             28-MAY-09   3HM8              
TITLE     CRYSTAL STRUCTURE OF THE C-TERMINAL HEXOKINASE DOMAIN OF HUMAN HK3    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEXOKINASE-3;                                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: HEXOKINASE TYPE III, HK III;                                
COMPND   5 EC: 2.7.1.1;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HK3;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A-LIC                                
KEYWDS    GLUCOSE, GLUCOSE-6-PHOSPHATE, NON-PROTEIN KINASE, HEXOKINASE,         
KEYWDS   2 STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, ALLOSTERIC 
KEYWDS   3 ENZYME, ATP-BINDING, GLYCOLYSIS, KINASE, NUCLEOTIDE-BINDING,         
KEYWDS   4 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.NEDYALKOVA,Y.TONG,W.RABEH,W.TEMPEL,R.LANDRY,C.H.ARROWSMITH,         
AUTHOR   2 A.M.EDWARDS,C.BOUNTRA,J.WEIGELT,A.BOCHKAREV,H.PARK,STRUCTURAL        
AUTHOR   3 GENOMICS CONSORTIUM (SGC)                                            
REVDAT   4   29-JUL-20 3HM8    1       COMPND REMARK SEQADV HETNAM              
REVDAT   4 2                   1       SITE                                     
REVDAT   3   01-NOV-17 3HM8    1       REMARK                                   
REVDAT   2   15-JUN-11 3HM8    1       AUTHOR JRNL                              
REVDAT   1   11-AUG-09 3HM8    0                                                
JRNL        AUTH   L.NEDYALKOVA,Y.TONG,W.RABEH,W.TEMPEL,R.LANDRY,               
JRNL        AUTH 2 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,J.WEIGELT,A.BOCHKAREV,  
JRNL        AUTH 3 H.PARK                                                       
JRNL        TITL   CRYSTAL STRUCTURE OF THE C-TERMINAL HEXOKINASE DOMAIN OF     
JRNL        TITL 2 HUMAN HK3                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 52939                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.245                           
REMARK   3   R VALUE            (WORKING SET) : 0.245                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.837                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1502                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3210                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.71                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 0                            
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12521                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 112                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 69.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.54100                                              
REMARK   3    B22 (A**2) : 5.54100                                              
REMARK   3    B33 (A**2) : -11.08200                                            
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): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.384         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 48.382        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12803 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  8173 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17404 ; 1.054 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 19913 ; 0.783 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1749 ; 3.864 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   468 ;33.612 ;24.103       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1929 ;11.488 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    78 ;12.304 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2118 ; 0.059 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 14625 ; 0.001 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2533 ; 0.001 ; 0.020       
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):  8655 ; 0.070 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3620 ; 0.030 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13638 ; 0.137 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4148 ; 0.342 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3766 ; 0.576 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 5                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    479       A     773      1                      
REMARK   3           1     B    479       B     773      1                      
REMARK   3           1     C    479       C     773      1                      
REMARK   3           1     D    479       D     773      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3356 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   3356 ; 0.010 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    C    (A):   3356 ; 0.010 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   3356 ; 0.010 ; 0.050           
REMARK   3   TIGHT THERMAL      1    A (A**2):   3356 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      1    B (A**2):   3356 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      1    C (A**2):   3356 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      1    D (A**2):   3356 ; 0.020 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    774       A     778      4                      
REMARK   3           1     B    774       B     778      4                      
REMARK   3           1     C    774       C     778      4                      
REMARK   3           1     D    774       D     778      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):     20 ; 0.130 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):     20 ; 0.230 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    C    (A):     20 ; 0.220 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    D    (A):     20 ; 0.100 ; 0.500           
REMARK   3   MEDIUM THERMAL     2    A (A**2):     20 ; 0.170 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    B (A**2):     20 ; 0.090 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    C (A**2):     20 ; 0.130 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    D (A**2):     20 ; 0.120 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    779       A     799      1                      
REMARK   3           1     B    779       B     799      1                      
REMARK   3           1     C    779       C     799      1                      
REMARK   3           1     D    779       D     799      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    A    (A):    233 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    B    (A):    233 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    C    (A):    233 ; 0.010 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    D    (A):    233 ; 0.010 ; 0.050           
REMARK   3   TIGHT THERMAL      3    A (A**2):    233 ; 0.030 ; 0.500           
REMARK   3   TIGHT THERMAL      3    B (A**2):    233 ; 0.030 ; 0.500           
REMARK   3   TIGHT THERMAL      3    C (A**2):    233 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      3    D (A**2):    233 ; 0.030 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    800       A     826      4                      
REMARK   3           1     B    800       B     826      4                      
REMARK   3           1     C    800       C     826      4                      
REMARK   3           1     D    800       D     826      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  4    A    (A):    261 ; 0.190 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  4    B    (A):    261 ; 0.390 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  4    C    (A):    261 ; 0.280 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  4    D    (A):    261 ; 0.290 ; 0.500           
REMARK   3   MEDIUM THERMAL     4    A (A**2):    261 ; 0.180 ; 2.000           
REMARK   3   MEDIUM THERMAL     4    B (A**2):    261 ; 0.190 ; 2.000           
REMARK   3   MEDIUM THERMAL     4    C (A**2):    261 ; 0.120 ; 2.000           
REMARK   3   MEDIUM THERMAL     4    D (A**2):    261 ; 0.120 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    827       A    1002      1                      
REMARK   3           1     B    827       B    1002      1                      
REMARK   3           1     C    827       C    1002      1                      
REMARK   3           1     D    827       D    1002      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   5    A    (A):   1041 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   5    B    (A):   1041 ; 0.010 ; 0.050           
REMARK   3   TIGHT POSITIONAL   5    C    (A):   1041 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   5    D    (A):   1041 ; 0.010 ; 0.050           
REMARK   3   TIGHT THERMAL      5    A (A**2):   1041 ; 0.030 ; 0.500           
REMARK   3   TIGHT THERMAL      5    B (A**2):   1041 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      5    C (A**2):   1041 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      5    D (A**2):   1041 ; 0.020 ; 0.500           
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 : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A  1002                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.6237  -0.8335 -27.4201              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1513 T22:   0.0671                                     
REMARK   3      T33:   0.1807 T12:  -0.0589                                     
REMARK   3      T13:   0.0162 T23:   0.0276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5995 L22:   1.6292                                     
REMARK   3      L33:   3.6954 L12:  -0.8355                                     
REMARK   3      L13:  -0.9335 L23:   1.0804                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2508 S12:  -0.1380 S13:   0.0377                       
REMARK   3      S21:   0.0117 S22:  -0.1666 S23:  -0.1735                       
REMARK   3      S31:  -0.3916 S32:   0.1009 S33:  -0.0842                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B  1002                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.9388  43.9402  11.1335              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1795 T22:   0.2517                                     
REMARK   3      T33:   0.3304 T12:  -0.0705                                     
REMARK   3      T13:   0.0439 T23:  -0.0191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2413 L22:   2.5303                                     
REMARK   3      L33:   4.9315 L12:   1.1504                                     
REMARK   3      L13:  -0.3399 L23:  -1.3159                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0765 S12:   0.5738 S13:   0.0271                       
REMARK   3      S21:  -0.0847 S22:  -0.0372 S23:  -0.1213                       
REMARK   3      S31:  -0.4239 S32:   0.2217 S33:  -0.0393                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C  1002                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.3558  -3.1364   9.1463              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1596 T22:   0.3709                                     
REMARK   3      T33:   0.1778 T12:  -0.1777                                     
REMARK   3      T13:   0.0086 T23:  -0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7929 L22:   2.4697                                     
REMARK   3      L33:   5.1049 L12:   0.4273                                     
REMARK   3      L13:   1.6845 L23:  -0.0322                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3385 S12:  -0.3091 S13:  -0.2537                       
REMARK   3      S21:  -0.0035 S22:  -0.1717 S23:   0.2850                       
REMARK   3      S31:   0.1323 S32:  -0.8575 S33:  -0.1668                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D  1002                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.8511  40.0313 -24.4231              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1011 T22:   0.5221                                     
REMARK   3      T33:   0.3787 T12:   0.1921                                     
REMARK   3      T13:   0.0355 T23:   0.0938                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8234 L22:   2.8108                                     
REMARK   3      L33:   4.4730 L12:  -1.0485                                     
REMARK   3      L13:   1.3305 L23:   0.0641                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1518 S12:  -0.0705 S13:  -0.0815                       
REMARK   3      S21:   0.0439 S22:  -0.0226 S23:  -0.2127                       
REMARK   3      S31:   0.1212 S32:   0.5534 S33:  -0.1292                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK BULK SOLVENT                                    
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. THE PROGRAMS CHAINSAW, PRODRG, PHENIX, COOT AND          
REMARK   3  MOLPROBLITY WERE ALSO USED.                                         
REMARK   4                                                                      
REMARK   4 3HM8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000053306.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97857                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53686                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR                           
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2NZT, CHAIN A, RESIDUES 468 THROUGH 913    
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR SOLUTION: 16% PEG 3350, 0.20   
REMARK 280  M AMMONIUM CITRATE, 0.1 M HEPES. 0.005 M GLUCOSE-6-PHOSPHATE,       
REMARK 280  0.005 M ADP-MG, 0.02 M TCEP, 1:100 (W/W) TRYPSIN WAS ADDED TO       
REMARK 280  THE PROTEIN STOCK SOLUTION., PH 7.2, VAPOR DIFFUSION, SITTING       
REMARK 280  DROP, TEMPERATURE 291K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
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      161.66350            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       80.83175            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      242.49525            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 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 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A   478                                                      
REMARK 465     LEU A   920                                                      
REMARK 465     THR A   921                                                      
REMARK 465     ARG A   922                                                      
REMARK 465     GLY B   478                                                      
REMARK 465     LEU B   920                                                      
REMARK 465     THR B   921                                                      
REMARK 465     ARG B   922                                                      
REMARK 465     GLY C   478                                                      
REMARK 465     SER C   479                                                      
REMARK 465     ARG C   775                                                      
REMARK 465     GLY C   776                                                      
REMARK 465     GLN C   777                                                      
REMARK 465     GLN C   778                                                      
REMARK 465     LEU C   920                                                      
REMARK 465     THR C   921                                                      
REMARK 465     ARG C   922                                                      
REMARK 465     GLY D   478                                                      
REMARK 465     ARG D   775                                                      
REMARK 465     GLY D   776                                                      
REMARK 465     GLN D   777                                                      
REMARK 465     GLN D   778                                                      
REMARK 465     LEU D   920                                                      
REMARK 465     THR D   921                                                      
REMARK 465     ARG D   922                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 479    OG                                                  
REMARK 470     ARG A 480    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 481    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 510    NZ                                                  
REMARK 470     ARG A 520    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 531    CG   OD1  OD2                                       
REMARK 470     ARG A 535    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 539    CD1  CD2                                            
REMARK 470     ARG A 549    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 557    OG1  CG2                                            
REMARK 470     SER A 567    OG                                                  
REMARK 470     GLU A 570    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 578    CG   CD   OE1  NE2                                  
REMARK 470     VAL A 589    CG1  CG2                                            
REMARK 470     GLN A 593    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 597    CG   CD1  CD2                                       
REMARK 470     SER A 598    OG                                                  
REMARK 470     GLN A 600    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 630    CG   CD   CE   NZ                                   
REMARK 470     ARG A 650    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 655    CG   CD1  CD2                                       
REMARK 470     VAL A 657    CG1  CG2                                            
REMARK 470     SER A 706    OG                                                  
REMARK 470     MET A 726    CG   SD   CE                                        
REMARK 470     SER A 734    OG                                                  
REMARK 470     ARG A 775    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 777    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 778    CD   OE1  NE2                                       
REMARK 470     ILE A 779    CG1  CG2  CD1                                       
REMARK 470     LYS A 791    CG   CD   CE   NZ                                   
REMARK 470     ILE A 796    CG1  CG2  CD1                                       
REMARK 470     ARG A 804    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 872    CD   CE   NZ                                        
REMARK 470     ARG A 876    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 880    CD1  CD2                                            
REMARK 470     GLU A 887    OE1  OE2                                            
REMARK 470     ARG A 891    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 900    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 916    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 917    CG   CD1  CD2                                       
REMARK 470     GLN A 919    CG   CD   OE1  NE2                                  
REMARK 470     SER B 479    OG                                                  
REMARK 470     ARG B 480    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B 481    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 482    CG   CD1  CD2                                       
REMARK 470     GLU B 485    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 510    NZ                                                  
REMARK 470     ARG B 520    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 531    CG   OD1  OD2                                       
REMARK 470     SER B 533    OG                                                  
REMARK 470     ARG B 535    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 537    CG   OD1  OD2                                       
REMARK 470     LEU B 539    CD1  CD2                                            
REMARK 470     LEU B 552    CG   CD1  CD2                                       
REMARK 470     THR B 557    OG1  CG2                                            
REMARK 470     GLN B 560    CG   CD   OE1  NE2                                  
REMARK 470     SER B 567    OG                                                  
REMARK 470     GLU B 570    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 578    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 579    CG   CD   OE1  NE2                                  
REMARK 470     VAL B 585    CG1  CG2                                            
REMARK 470     VAL B 589    CG1  CG2                                            
REMARK 470     GLN B 593    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 595    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 597    CG   CD1  CD2                                       
REMARK 470     SER B 598    OG                                                  
REMARK 470     GLN B 600    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 602    CG   CD1  CD2                                       
REMARK 470     LEU B 615    CG   CD1  CD2                                       
REMARK 470     LYS B 630    CG   CD   CE   NZ                                   
REMARK 470     ASP B 633    CG   OD1  OD2                                       
REMARK 470     ARG B 644    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 650    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 651    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 654    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 655    CG   CD1  CD2                                       
REMARK 470     VAL B 657    CG1  CG2                                            
REMARK 470     GLU B 674    CG   CD   OE1  OE2                                  
REMARK 470     SER B 706    OG                                                  
REMARK 470     MET B 726    CG   SD   CE                                        
REMARK 470     SER B 734    OG                                                  
REMARK 470     GLN B 737    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 744    CG   CD   CE   NZ                                   
REMARK 470     ARG B 775    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 777    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 778    CG   CD   OE1  NE2                                  
REMARK 470     ILE B 779    CG1  CG2  CD1                                       
REMARK 470     GLN B 780    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 791    CG   CD   CE   NZ                                   
REMARK 470     ILE B 796    CG1  CG2  CD1                                       
REMARK 470     GLU B 797    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 799    CG   OD1  OD2                                       
REMARK 470     ARG B 804    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 805    CG   CD   OE1  NE2                                  
REMARK 470     VAL B 806    CG1  CG2                                            
REMARK 470     GLU B 811    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 830    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 858    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 859    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 872    CD   CE   NZ                                        
REMARK 470     ARG B 876    CD   NE   CZ   NH1  NH2                             
REMARK 470     LEU B 880    CD1  CD2                                            
REMARK 470     ARG B 891    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 900    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 916    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 917    CG   CD1  CD2                                       
REMARK 470     GLN B 919    CG   CD   OE1  NE2                                  
REMARK 470     ARG C 480    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG C 481    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C 482    CG   CD1  CD2                                       
REMARK 470     LYS C 510    NZ                                                  
REMARK 470     GLU C 515    CD   OE1  OE2                                       
REMARK 470     ARG C 520    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 531    CG   OD1  OD2                                       
REMARK 470     SER C 533    OG                                                  
REMARK 470     ARG C 535    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C 539    CD1  CD2                                            
REMARK 470     ARG C 554    CD   NE   CZ   NH1  NH2                             
REMARK 470     THR C 557    OG1  CG2                                            
REMARK 470     SER C 567    OG                                                  
REMARK 470     GLU C 570    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 578    CG   CD   OE1  NE2                                  
REMARK 470     VAL C 589    CG1  CG2                                            
REMARK 470     GLN C 593    CG   CD   OE1  NE2                                  
REMARK 470     LEU C 597    CG   CD1  CD2                                       
REMARK 470     SER C 598    OG                                                  
REMARK 470     GLN C 600    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 630    CG   CD   CE   NZ                                   
REMARK 470     ARG C 650    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 651    CG   CD   OE1  NE2                                  
REMARK 470     LEU C 655    CG   CD1  CD2                                       
REMARK 470     VAL C 657    CG1  CG2                                            
REMARK 470     GLU C 674    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 677    NE   CZ   NH1  NH2                                  
REMARK 470     ASP C 705    OD1  OD2                                            
REMARK 470     SER C 706    OG                                                  
REMARK 470     MET C 726    CG   SD   CE                                        
REMARK 470     ARG C 730    NE   CZ   NH1  NH2                                  
REMARK 470     SER C 734    OG                                                  
REMARK 470     GLN C 737    CG   CD   OE1  NE2                                  
REMARK 470     ILE C 779    CG1  CG2  CD1                                       
REMARK 470     GLN C 780    CG   CD   OE1  NE2                                  
REMARK 470     GLN C 783    CG   CD   OE1  NE2                                  
REMARK 470     ARG C 785    NE   CZ   NH1  NH2                                  
REMARK 470     LYS C 791    CG   CD   CE   NZ                                   
REMARK 470     ILE C 796    CG1  CG2  CD1                                       
REMARK 470     ASP C 799    CG   OD1  OD2                                       
REMARK 470     SER C 800    OG                                                  
REMARK 470     LEU C 801    CG   CD1  CD2                                       
REMARK 470     ARG C 804    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C 810    CG   CD1  CD2                                       
REMARK 470     GLU C 811    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 813    CG   CD1  CD2                                       
REMARK 470     LEU C 815    CG   CD1  CD2                                       
REMARK 470     LEU C 817    CG   CD1  CD2                                       
REMARK 470     MET C 824    CG   SD   CE                                        
REMARK 470     GLU C 853    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 872    CD   CE   NZ                                        
REMARK 470     ARG C 876    CD   NE   CZ   NH1  NH2                             
REMARK 470     LEU C 880    CD1  CD2                                            
REMARK 470     ARG C 891    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 900    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 916    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 919    CG   CD   OE1  NE2                                  
REMARK 470     SER D 479    OG                                                  
REMARK 470     ARG D 480    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 481    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU D 482    CG   CD1  CD2                                       
REMARK 470     GLU D 484    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 485    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 503    CD   OE1  NE2                                       
REMARK 470     LYS D 506    CE   NZ                                             
REMARK 470     LYS D 510    NZ                                                  
REMARK 470     ARG D 520    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 531    CG   OD1  OD2                                       
REMARK 470     ARG D 535    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 537    CG   OD1  OD2                                       
REMARK 470     LEU D 539    CD1  CD2                                            
REMARK 470     ARG D 549    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR D 557    OG1  CG2                                            
REMARK 470     GLU D 564    CG   CD   OE1  OE2                                  
REMARK 470     SER D 567    OG                                                  
REMARK 470     GLU D 570    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 578    CG   CD   OE1  NE2                                  
REMARK 470     GLN D 579    CG   CD   OE1  NE2                                  
REMARK 470     VAL D 589    CG1  CG2                                            
REMARK 470     GLN D 593    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 594    CG   CD   CE   NZ                                   
REMARK 470     LEU D 597    CG   CD1  CD2                                       
REMARK 470     SER D 598    OG                                                  
REMARK 470     GLN D 600    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 630    CG   CD   CE   NZ                                   
REMARK 470     ASP D 633    CG   OD1  OD2                                       
REMARK 470     ARG D 644    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 650    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 654    CG   CD   OE1  OE2                                  
REMARK 470     LEU D 655    CG   CD1  CD2                                       
REMARK 470     VAL D 657    CG1  CG2                                            
REMARK 470     GLU D 674    CG   CD   OE1  OE2                                  
REMARK 470     SER D 706    OG                                                  
REMARK 470     LEU D 724    CG   CD1  CD2                                       
REMARK 470     MET D 726    CG   SD   CE                                        
REMARK 470     ARG D 730    NE   CZ   NH1  NH2                                  
REMARK 470     SER D 734    OG                                                  
REMARK 470     LYS D 744    CD   CE   NZ                                        
REMARK 470     LEU D 767    CG   CD1  CD2                                       
REMARK 470     LEU D 770    CG   CD1  CD2                                       
REMARK 470     VAL D 772    CG1  CG2                                            
REMARK 470     LEU D 773    CG   CD1  CD2                                       
REMARK 470     ILE D 779    CG1  CG2  CD1                                       
REMARK 470     GLN D 780    CG   CD   OE1  NE2                                  
REMARK 470     ARG D 785    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 789    CG   CD   CE   NZ                                   
REMARK 470     LYS D 791    CG   CD   CE   NZ                                   
REMARK 470     ILE D 796    CG1  CG2  CD1                                       
REMARK 470     ARG D 804    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU D 815    CG   CD1  CD2                                       
REMARK 470     LEU D 817    CG   CD1  CD2                                       
REMARK 470     GLU D 853    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 858    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 859    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 872    CD   CE   NZ                                        
REMARK 470     ARG D 876    CD   NE   CZ   NH1  NH2                             
REMARK 470     LEU D 880    CD1  CD2                                            
REMARK 470     ARG D 891    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 900    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 905    CG   CD   CE   NZ                                   
REMARK 470     ARG D 916    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU D 917    CG   CD1  CD2                                       
REMARK 470     GLN D 919    CG   CD   OE1  NE2                                  
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    CYS A 829   CB    CYS A 829   SG     -0.111                       
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    PRO A 530      108.19    -41.10                                   
REMARK 500    THR A 556     -128.32   -137.11                                   
REMARK 500    SER A 598     -106.39     50.08                                   
REMARK 500    LYS A 627     -121.67     58.26                                   
REMARK 500    LYS A 630       29.01   -150.64                                   
REMARK 500    ASN A 656     -141.55    -94.09                                   
REMARK 500    ILE A 751      -48.43   -133.44                                   
REMARK 500    PHE A 774       17.55     56.58                                   
REMARK 500    PRO B 530      108.23    -40.98                                   
REMARK 500    THR B 556     -127.94   -136.43                                   
REMARK 500    SER B 598     -106.84     49.72                                   
REMARK 500    LYS B 627     -121.45     57.44                                   
REMARK 500    LYS B 630       28.66   -150.27                                   
REMARK 500    ASN B 656     -142.10    -94.67                                   
REMARK 500    ILE B 751      -48.06   -134.99                                   
REMARK 500    PHE B 774       79.52     42.11                                   
REMARK 500    PRO C 530      108.45    -40.44                                   
REMARK 500    THR C 556     -127.54   -136.99                                   
REMARK 500    SER C 598     -106.84     50.61                                   
REMARK 500    LYS C 627     -121.60     56.80                                   
REMARK 500    LYS C 630       28.11   -149.59                                   
REMARK 500    ASN C 656     -141.56    -94.77                                   
REMARK 500    ILE C 751      -48.29   -132.51                                   
REMARK 500    PRO D 530      108.33    -41.05                                   
REMARK 500    THR D 556     -128.05   -136.76                                   
REMARK 500    SER D 598     -107.00     50.22                                   
REMARK 500    LYS D 627     -122.11     57.15                                   
REMARK 500    LYS D 630       29.20   -150.19                                   
REMARK 500    ASN D 656     -142.00    -94.86                                   
REMARK 500    ILE D 751      -48.73   -132.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3HM8 A  480   922  UNP    P52790   HXK3_HUMAN     480    922             
DBREF  3HM8 B  480   922  UNP    P52790   HXK3_HUMAN     480    922             
DBREF  3HM8 C  480   922  UNP    P52790   HXK3_HUMAN     480    922             
DBREF  3HM8 D  480   922  UNP    P52790   HXK3_HUMAN     480    922             
SEQADV 3HM8 GLY A  478  UNP  P52790              EXPRESSION TAG                 
SEQADV 3HM8 SER A  479  UNP  P52790              EXPRESSION TAG                 
SEQADV 3HM8 GLY B  478  UNP  P52790              EXPRESSION TAG                 
SEQADV 3HM8 SER B  479  UNP  P52790              EXPRESSION TAG                 
SEQADV 3HM8 GLY C  478  UNP  P52790              EXPRESSION TAG                 
SEQADV 3HM8 SER C  479  UNP  P52790              EXPRESSION TAG                 
SEQADV 3HM8 GLY D  478  UNP  P52790              EXPRESSION TAG                 
SEQADV 3HM8 SER D  479  UNP  P52790              EXPRESSION TAG                 
SEQRES   1 A  445  GLY SER ARG ARG LEU LEU GLU GLU THR LEU ALA PRO PHE          
SEQRES   2 A  445  ARG LEU ASN HIS ASP GLN LEU ALA ALA VAL GLN ALA GLN          
SEQRES   3 A  445  MET ARG LYS ALA MET ALA LYS GLY LEU ARG GLY GLU ALA          
SEQRES   4 A  445  SER SER LEU ARG MET LEU PRO THR PHE VAL ARG ALA THR          
SEQRES   5 A  445  PRO ASP GLY SER GLU ARG GLY ASP PHE LEU ALA LEU ASP          
SEQRES   6 A  445  LEU GLY GLY THR ASN PHE ARG VAL LEU LEU VAL ARG VAL          
SEQRES   7 A  445  THR THR GLY VAL GLN ILE THR SER GLU ILE TYR SER ILE          
SEQRES   8 A  445  PRO GLU THR VAL ALA GLN GLY SER GLY GLN GLN LEU PHE          
SEQRES   9 A  445  ASP HIS ILE VAL ASP CYS ILE VAL ASP PHE GLN GLN LYS          
SEQRES  10 A  445  GLN GLY LEU SER GLY GLN SER LEU PRO LEU GLY PHE THR          
SEQRES  11 A  445  PHE SER PHE PRO CYS ARG GLN LEU GLY LEU ASP GLN GLY          
SEQRES  12 A  445  ILE LEU LEU ASN TRP THR LYS GLY PHE LYS ALA SER ASP          
SEQRES  13 A  445  CYS GLU GLY GLN ASP VAL VAL SER LEU LEU ARG GLU ALA          
SEQRES  14 A  445  ILE THR ARG ARG GLN ALA VAL GLU LEU ASN VAL VAL ALA          
SEQRES  15 A  445  ILE VAL ASN ASP THR VAL GLY THR MET MET SER CYS GLY          
SEQRES  16 A  445  TYR GLU ASP PRO ARG CYS GLU ILE GLY LEU ILE VAL GLY          
SEQRES  17 A  445  THR GLY THR ASN ALA CYS TYR MET GLU GLU LEU ARG ASN          
SEQRES  18 A  445  VAL ALA GLY VAL PRO GLY ASP SER GLY ARG MET CYS ILE          
SEQRES  19 A  445  ASN MET GLU TRP GLY ALA PHE GLY ASP ASP GLY SER LEU          
SEQRES  20 A  445  ALA MET LEU SER THR ARG PHE ASP ALA SER VAL ASP GLN          
SEQRES  21 A  445  ALA SER ILE ASN PRO GLY LYS GLN ARG PHE GLU LYS MET          
SEQRES  22 A  445  ILE SER GLY MET TYR LEU GLY GLU ILE VAL ARG HIS ILE          
SEQRES  23 A  445  LEU LEU HIS LEU THR SER LEU GLY VAL LEU PHE ARG GLY          
SEQRES  24 A  445  GLN GLN ILE GLN ARG LEU GLN THR ARG ASP ILE PHE LYS          
SEQRES  25 A  445  THR LYS PHE LEU SER GLU ILE GLU SER ASP SER LEU ALA          
SEQRES  26 A  445  LEU ARG GLN VAL ARG ALA ILE LEU GLU ASP LEU GLY LEU          
SEQRES  27 A  445  PRO LEU THR SER ASP ASP ALA LEU MET VAL LEU GLU VAL          
SEQRES  28 A  445  CYS GLN ALA VAL SER GLN ARG ALA ALA GLN LEU CYS GLY          
SEQRES  29 A  445  ALA GLY VAL ALA ALA VAL VAL GLU LYS ILE ARG GLU ASN          
SEQRES  30 A  445  ARG GLY LEU GLU GLU LEU ALA VAL SER VAL GLY VAL ASP          
SEQRES  31 A  445  GLY THR LEU TYR LYS LEU HIS PRO ARG PHE SER SER LEU          
SEQRES  32 A  445  VAL ALA ALA THR VAL ARG GLU LEU ALA PRO ARG CYS VAL          
SEQRES  33 A  445  VAL THR PHE LEU GLN SER GLU ASP GLY SER GLY LYS GLY          
SEQRES  34 A  445  ALA ALA LEU VAL THR ALA VAL ALA CYS ARG LEU ALA GLN          
SEQRES  35 A  445  LEU THR ARG                                                  
SEQRES   1 B  445  GLY SER ARG ARG LEU LEU GLU GLU THR LEU ALA PRO PHE          
SEQRES   2 B  445  ARG LEU ASN HIS ASP GLN LEU ALA ALA VAL GLN ALA GLN          
SEQRES   3 B  445  MET ARG LYS ALA MET ALA LYS GLY LEU ARG GLY GLU ALA          
SEQRES   4 B  445  SER SER LEU ARG MET LEU PRO THR PHE VAL ARG ALA THR          
SEQRES   5 B  445  PRO ASP GLY SER GLU ARG GLY ASP PHE LEU ALA LEU ASP          
SEQRES   6 B  445  LEU GLY GLY THR ASN PHE ARG VAL LEU LEU VAL ARG VAL          
SEQRES   7 B  445  THR THR GLY VAL GLN ILE THR SER GLU ILE TYR SER ILE          
SEQRES   8 B  445  PRO GLU THR VAL ALA GLN GLY SER GLY GLN GLN LEU PHE          
SEQRES   9 B  445  ASP HIS ILE VAL ASP CYS ILE VAL ASP PHE GLN GLN LYS          
SEQRES  10 B  445  GLN GLY LEU SER GLY GLN SER LEU PRO LEU GLY PHE THR          
SEQRES  11 B  445  PHE SER PHE PRO CYS ARG GLN LEU GLY LEU ASP GLN GLY          
SEQRES  12 B  445  ILE LEU LEU ASN TRP THR LYS GLY PHE LYS ALA SER ASP          
SEQRES  13 B  445  CYS GLU GLY GLN ASP VAL VAL SER LEU LEU ARG GLU ALA          
SEQRES  14 B  445  ILE THR ARG ARG GLN ALA VAL GLU LEU ASN VAL VAL ALA          
SEQRES  15 B  445  ILE VAL ASN ASP THR VAL GLY THR MET MET SER CYS GLY          
SEQRES  16 B  445  TYR GLU ASP PRO ARG CYS GLU ILE GLY LEU ILE VAL GLY          
SEQRES  17 B  445  THR GLY THR ASN ALA CYS TYR MET GLU GLU LEU ARG ASN          
SEQRES  18 B  445  VAL ALA GLY VAL PRO GLY ASP SER GLY ARG MET CYS ILE          
SEQRES  19 B  445  ASN MET GLU TRP GLY ALA PHE GLY ASP ASP GLY SER LEU          
SEQRES  20 B  445  ALA MET LEU SER THR ARG PHE ASP ALA SER VAL ASP GLN          
SEQRES  21 B  445  ALA SER ILE ASN PRO GLY LYS GLN ARG PHE GLU LYS MET          
SEQRES  22 B  445  ILE SER GLY MET TYR LEU GLY GLU ILE VAL ARG HIS ILE          
SEQRES  23 B  445  LEU LEU HIS LEU THR SER LEU GLY VAL LEU PHE ARG GLY          
SEQRES  24 B  445  GLN GLN ILE GLN ARG LEU GLN THR ARG ASP ILE PHE LYS          
SEQRES  25 B  445  THR LYS PHE LEU SER GLU ILE GLU SER ASP SER LEU ALA          
SEQRES  26 B  445  LEU ARG GLN VAL ARG ALA ILE LEU GLU ASP LEU GLY LEU          
SEQRES  27 B  445  PRO LEU THR SER ASP ASP ALA LEU MET VAL LEU GLU VAL          
SEQRES  28 B  445  CYS GLN ALA VAL SER GLN ARG ALA ALA GLN LEU CYS GLY          
SEQRES  29 B  445  ALA GLY VAL ALA ALA VAL VAL GLU LYS ILE ARG GLU ASN          
SEQRES  30 B  445  ARG GLY LEU GLU GLU LEU ALA VAL SER VAL GLY VAL ASP          
SEQRES  31 B  445  GLY THR LEU TYR LYS LEU HIS PRO ARG PHE SER SER LEU          
SEQRES  32 B  445  VAL ALA ALA THR VAL ARG GLU LEU ALA PRO ARG CYS VAL          
SEQRES  33 B  445  VAL THR PHE LEU GLN SER GLU ASP GLY SER GLY LYS GLY          
SEQRES  34 B  445  ALA ALA LEU VAL THR ALA VAL ALA CYS ARG LEU ALA GLN          
SEQRES  35 B  445  LEU THR ARG                                                  
SEQRES   1 C  445  GLY SER ARG ARG LEU LEU GLU GLU THR LEU ALA PRO PHE          
SEQRES   2 C  445  ARG LEU ASN HIS ASP GLN LEU ALA ALA VAL GLN ALA GLN          
SEQRES   3 C  445  MET ARG LYS ALA MET ALA LYS GLY LEU ARG GLY GLU ALA          
SEQRES   4 C  445  SER SER LEU ARG MET LEU PRO THR PHE VAL ARG ALA THR          
SEQRES   5 C  445  PRO ASP GLY SER GLU ARG GLY ASP PHE LEU ALA LEU ASP          
SEQRES   6 C  445  LEU GLY GLY THR ASN PHE ARG VAL LEU LEU VAL ARG VAL          
SEQRES   7 C  445  THR THR GLY VAL GLN ILE THR SER GLU ILE TYR SER ILE          
SEQRES   8 C  445  PRO GLU THR VAL ALA GLN GLY SER GLY GLN GLN LEU PHE          
SEQRES   9 C  445  ASP HIS ILE VAL ASP CYS ILE VAL ASP PHE GLN GLN LYS          
SEQRES  10 C  445  GLN GLY LEU SER GLY GLN SER LEU PRO LEU GLY PHE THR          
SEQRES  11 C  445  PHE SER PHE PRO CYS ARG GLN LEU GLY LEU ASP GLN GLY          
SEQRES  12 C  445  ILE LEU LEU ASN TRP THR LYS GLY PHE LYS ALA SER ASP          
SEQRES  13 C  445  CYS GLU GLY GLN ASP VAL VAL SER LEU LEU ARG GLU ALA          
SEQRES  14 C  445  ILE THR ARG ARG GLN ALA VAL GLU LEU ASN VAL VAL ALA          
SEQRES  15 C  445  ILE VAL ASN ASP THR VAL GLY THR MET MET SER CYS GLY          
SEQRES  16 C  445  TYR GLU ASP PRO ARG CYS GLU ILE GLY LEU ILE VAL GLY          
SEQRES  17 C  445  THR GLY THR ASN ALA CYS TYR MET GLU GLU LEU ARG ASN          
SEQRES  18 C  445  VAL ALA GLY VAL PRO GLY ASP SER GLY ARG MET CYS ILE          
SEQRES  19 C  445  ASN MET GLU TRP GLY ALA PHE GLY ASP ASP GLY SER LEU          
SEQRES  20 C  445  ALA MET LEU SER THR ARG PHE ASP ALA SER VAL ASP GLN          
SEQRES  21 C  445  ALA SER ILE ASN PRO GLY LYS GLN ARG PHE GLU LYS MET          
SEQRES  22 C  445  ILE SER GLY MET TYR LEU GLY GLU ILE VAL ARG HIS ILE          
SEQRES  23 C  445  LEU LEU HIS LEU THR SER LEU GLY VAL LEU PHE ARG GLY          
SEQRES  24 C  445  GLN GLN ILE GLN ARG LEU GLN THR ARG ASP ILE PHE LYS          
SEQRES  25 C  445  THR LYS PHE LEU SER GLU ILE GLU SER ASP SER LEU ALA          
SEQRES  26 C  445  LEU ARG GLN VAL ARG ALA ILE LEU GLU ASP LEU GLY LEU          
SEQRES  27 C  445  PRO LEU THR SER ASP ASP ALA LEU MET VAL LEU GLU VAL          
SEQRES  28 C  445  CYS GLN ALA VAL SER GLN ARG ALA ALA GLN LEU CYS GLY          
SEQRES  29 C  445  ALA GLY VAL ALA ALA VAL VAL GLU LYS ILE ARG GLU ASN          
SEQRES  30 C  445  ARG GLY LEU GLU GLU LEU ALA VAL SER VAL GLY VAL ASP          
SEQRES  31 C  445  GLY THR LEU TYR LYS LEU HIS PRO ARG PHE SER SER LEU          
SEQRES  32 C  445  VAL ALA ALA THR VAL ARG GLU LEU ALA PRO ARG CYS VAL          
SEQRES  33 C  445  VAL THR PHE LEU GLN SER GLU ASP GLY SER GLY LYS GLY          
SEQRES  34 C  445  ALA ALA LEU VAL THR ALA VAL ALA CYS ARG LEU ALA GLN          
SEQRES  35 C  445  LEU THR ARG                                                  
SEQRES   1 D  445  GLY SER ARG ARG LEU LEU GLU GLU THR LEU ALA PRO PHE          
SEQRES   2 D  445  ARG LEU ASN HIS ASP GLN LEU ALA ALA VAL GLN ALA GLN          
SEQRES   3 D  445  MET ARG LYS ALA MET ALA LYS GLY LEU ARG GLY GLU ALA          
SEQRES   4 D  445  SER SER LEU ARG MET LEU PRO THR PHE VAL ARG ALA THR          
SEQRES   5 D  445  PRO ASP GLY SER GLU ARG GLY ASP PHE LEU ALA LEU ASP          
SEQRES   6 D  445  LEU GLY GLY THR ASN PHE ARG VAL LEU LEU VAL ARG VAL          
SEQRES   7 D  445  THR THR GLY VAL GLN ILE THR SER GLU ILE TYR SER ILE          
SEQRES   8 D  445  PRO GLU THR VAL ALA GLN GLY SER GLY GLN GLN LEU PHE          
SEQRES   9 D  445  ASP HIS ILE VAL ASP CYS ILE VAL ASP PHE GLN GLN LYS          
SEQRES  10 D  445  GLN GLY LEU SER GLY GLN SER LEU PRO LEU GLY PHE THR          
SEQRES  11 D  445  PHE SER PHE PRO CYS ARG GLN LEU GLY LEU ASP GLN GLY          
SEQRES  12 D  445  ILE LEU LEU ASN TRP THR LYS GLY PHE LYS ALA SER ASP          
SEQRES  13 D  445  CYS GLU GLY GLN ASP VAL VAL SER LEU LEU ARG GLU ALA          
SEQRES  14 D  445  ILE THR ARG ARG GLN ALA VAL GLU LEU ASN VAL VAL ALA          
SEQRES  15 D  445  ILE VAL ASN ASP THR VAL GLY THR MET MET SER CYS GLY          
SEQRES  16 D  445  TYR GLU ASP PRO ARG CYS GLU ILE GLY LEU ILE VAL GLY          
SEQRES  17 D  445  THR GLY THR ASN ALA CYS TYR MET GLU GLU LEU ARG ASN          
SEQRES  18 D  445  VAL ALA GLY VAL PRO GLY ASP SER GLY ARG MET CYS ILE          
SEQRES  19 D  445  ASN MET GLU TRP GLY ALA PHE GLY ASP ASP GLY SER LEU          
SEQRES  20 D  445  ALA MET LEU SER THR ARG PHE ASP ALA SER VAL ASP GLN          
SEQRES  21 D  445  ALA SER ILE ASN PRO GLY LYS GLN ARG PHE GLU LYS MET          
SEQRES  22 D  445  ILE SER GLY MET TYR LEU GLY GLU ILE VAL ARG HIS ILE          
SEQRES  23 D  445  LEU LEU HIS LEU THR SER LEU GLY VAL LEU PHE ARG GLY          
SEQRES  24 D  445  GLN GLN ILE GLN ARG LEU GLN THR ARG ASP ILE PHE LYS          
SEQRES  25 D  445  THR LYS PHE LEU SER GLU ILE GLU SER ASP SER LEU ALA          
SEQRES  26 D  445  LEU ARG GLN VAL ARG ALA ILE LEU GLU ASP LEU GLY LEU          
SEQRES  27 D  445  PRO LEU THR SER ASP ASP ALA LEU MET VAL LEU GLU VAL          
SEQRES  28 D  445  CYS GLN ALA VAL SER GLN ARG ALA ALA GLN LEU CYS GLY          
SEQRES  29 D  445  ALA GLY VAL ALA ALA VAL VAL GLU LYS ILE ARG GLU ASN          
SEQRES  30 D  445  ARG GLY LEU GLU GLU LEU ALA VAL SER VAL GLY VAL ASP          
SEQRES  31 D  445  GLY THR LEU TYR LYS LEU HIS PRO ARG PHE SER SER LEU          
SEQRES  32 D  445  VAL ALA ALA THR VAL ARG GLU LEU ALA PRO ARG CYS VAL          
SEQRES  33 D  445  VAL THR PHE LEU GLN SER GLU ASP GLY SER GLY LYS GLY          
SEQRES  34 D  445  ALA ALA LEU VAL THR ALA VAL ALA CYS ARG LEU ALA GLN          
SEQRES  35 D  445  LEU THR ARG                                                  
HET    GLC  A1001      12                                                       
HET    BG6  A1002      16                                                       
HET    GLC  B1001      12                                                       
HET    BG6  B1002      16                                                       
HET    GLC  C1001      12                                                       
HET    BG6  C1002      16                                                       
HET    GLC  D1001      12                                                       
HET    BG6  D1002      16                                                       
HETNAM     GLC ALPHA-D-GLUCOPYRANOSE                                            
HETNAM     BG6 6-O-PHOSPHONO-BETA-D-GLUCOPYRANOSE                               
FORMUL   5  GLC    4(C6 H12 O6)                                                 
FORMUL   6  BG6    4(C6 H13 O9 P)                                               
HELIX    1   1 SER A  479  ALA A  488  1                                  10    
HELIX    2   2 PRO A  489  ARG A  491  5                                   3    
HELIX    3   3 ASN A  493  GLY A  514  1                                  22    
HELIX    4   4 PRO A  569  GLN A  574  1                                   6    
HELIX    5   5 SER A  576  GLY A  596  1                                  21    
HELIX    6   6 ASP A  638  ARG A  650  1                                  13    
HELIX    7   7 ASN A  662  TYR A  673  1                                  12    
HELIX    8   8 ARG A  697  VAL A  699  5                                   3    
HELIX    9   9 GLU A  714  PHE A  718  5                                   5    
HELIX   10  10 THR A  729  ALA A  738  1                                  10    
HELIX   11  11 PHE A  747  ILE A  751  5                                   5    
HELIX   12  12 SER A  752  LEU A  770  1                                  19    
HELIX   13  13 LEU A  773  GLN A  777  5                                   5    
HELIX   14  14 ILE A  779  THR A  784  5                                   6    
HELIX   15  15 LYS A  789  GLU A  797  1                                   9    
HELIX   16  16 ALA A  802  ASP A  812  1                                  11    
HELIX   17  17 THR A  818  ARG A  855  1                                  38    
HELIX   18  18 GLY A  868  HIS A  874  1                                   7    
HELIX   19  19 ARG A  876  ALA A  889  1                                  14    
HELIX   20  20 GLY A  902  GLN A  919  1                                  18    
HELIX   21  21 SER B  479  ALA B  488  1                                  10    
HELIX   22  22 PRO B  489  ARG B  491  5                                   3    
HELIX   23  23 ASN B  493  GLY B  514  1                                  22    
HELIX   24  24 PRO B  569  GLN B  574  1                                   6    
HELIX   25  25 SER B  576  GLY B  596  1                                  21    
HELIX   26  26 ASP B  638  GLN B  651  1                                  14    
HELIX   27  27 ASN B  662  TYR B  673  1                                  12    
HELIX   28  28 ARG B  697  VAL B  699  5                                   3    
HELIX   29  29 GLU B  714  PHE B  718  5                                   5    
HELIX   30  30 THR B  729  ALA B  738  1                                  10    
HELIX   31  31 PHE B  747  ILE B  751  5                                   5    
HELIX   32  32 SER B  752  LEU B  770  1                                  19    
HELIX   33  33 ILE B  779  THR B  784  5                                   6    
HELIX   34  34 LYS B  789  GLU B  797  1                                   9    
HELIX   35  35 ALA B  802  LEU B  813  1                                  12    
HELIX   36  36 THR B  818  ARG B  855  1                                  38    
HELIX   37  37 GLY B  868  HIS B  874  1                                   7    
HELIX   38  38 ARG B  876  ALA B  889  1                                  14    
HELIX   39  39 GLY B  902  GLN B  919  1                                  18    
HELIX   40  40 ARG C  480  ALA C  488  1                                   9    
HELIX   41  41 PRO C  489  ARG C  491  5                                   3    
HELIX   42  42 ASN C  493  GLY C  514  1                                  22    
HELIX   43  43 PRO C  569  GLN C  574  1                                   6    
HELIX   44  44 SER C  576  GLY C  596  1                                  21    
HELIX   45  45 ASP C  638  GLN C  651  1                                  14    
HELIX   46  46 ASN C  662  TYR C  673  1                                  12    
HELIX   47  47 ARG C  697  VAL C  699  5                                   3    
HELIX   48  48 GLU C  714  PHE C  718  5                                   5    
HELIX   49  49 THR C  729  ALA C  738  1                                  10    
HELIX   50  50 PHE C  747  ILE C  751  5                                   5    
HELIX   51  51 SER C  752  LEU C  770  1                                  19    
HELIX   52  52 ILE C  779  THR C  784  5                                   6    
HELIX   53  53 LYS C  789  GLU C  797  1                                   9    
HELIX   54  54 ALA C  802  ASP C  812  1                                  11    
HELIX   55  55 THR C  818  ARG C  855  1                                  38    
HELIX   56  56 GLY C  868  HIS C  874  1                                   7    
HELIX   57  57 ARG C  876  ALA C  889  1                                  14    
HELIX   58  58 GLY C  902  GLN C  919  1                                  18    
HELIX   59  59 SER D  479  ALA D  488  1                                  10    
HELIX   60  60 PRO D  489  ARG D  491  5                                   3    
HELIX   61  61 ASN D  493  GLY D  514  1                                  22    
HELIX   62  62 PRO D  569  GLN D  574  1                                   6    
HELIX   63  63 SER D  576  GLY D  596  1                                  21    
HELIX   64  64 ASP D  638  GLN D  651  1                                  14    
HELIX   65  65 ASN D  662  TYR D  673  1                                  12    
HELIX   66  66 ARG D  697  VAL D  699  5                                   3    
HELIX   67  67 GLU D  714  PHE D  718  5                                   5    
HELIX   68  68 THR D  729  ALA D  738  1                                  10    
HELIX   69  69 PHE D  747  ILE D  751  5                                   5    
HELIX   70  70 SER D  752  LEU D  770  1                                  19    
HELIX   71  71 ILE D  779  THR D  784  5                                   6    
HELIX   72  72 LYS D  789  GLU D  797  1                                   9    
HELIX   73  73 ALA D  802  ASP D  812  1                                  11    
HELIX   74  74 THR D  818  ARG D  855  1                                  38    
HELIX   75  75 GLY D  868  HIS D  874  1                                   7    
HELIX   76  76 ARG D  876  ALA D  889  1                                  14    
HELIX   77  77 GLY D  902  GLN D  919  1                                  18    
SHEET    1   A 6 LEU A 522  PRO A 523  0                                        
SHEET    2   A 6 ARG A 708  ASN A 712 -1  O  ASN A 712   N  LEU A 522           
SHEET    3   A 6 THR A 688  GLU A 695 -1  N  GLU A 694   O  MET A 709           
SHEET    4   A 6 CYS A 678  VAL A 684 -1  N  ILE A 683   O  ASN A 689           
SHEET    5   A 6 LEU A 860  ASP A 867  1  O  GLY A 865   N  LEU A 682           
SHEET    6   A 6 CYS A 892  GLN A 898  1  O  VAL A 893   N  LEU A 860           
SHEET    1   B 5 VAL A 559  TYR A 566  0                                        
SHEET    2   B 5 PHE A 548  VAL A 555 -1  N  ARG A 554   O  GLN A 560           
SHEET    3   B 5 GLY A 536  LEU A 543 -1  N  PHE A 538   O  VAL A 553           
SHEET    4   B 5 LEU A 604  PHE A 608  1  O  THR A 607   N  LEU A 541           
SHEET    5   B 5 VAL A 658  VAL A 661  1  O  VAL A 661   N  PHE A 608           
SHEET    1   C 2 CYS A 612  ARG A 613  0                                        
SHEET    2   C 2 ILE A 621  LEU A 622 -1  O  ILE A 621   N  ARG A 613           
SHEET    1   D 6 LEU B 522  PRO B 523  0                                        
SHEET    2   D 6 ARG B 708  ASN B 712 -1  O  ASN B 712   N  LEU B 522           
SHEET    3   D 6 THR B 688  GLU B 695 -1  N  GLU B 694   O  MET B 709           
SHEET    4   D 6 CYS B 678  VAL B 684 -1  N  ILE B 683   O  ASN B 689           
SHEET    5   D 6 LEU B 860  ASP B 867  1  O  GLY B 865   N  LEU B 682           
SHEET    6   D 6 CYS B 892  GLN B 898  1  O  VAL B 893   N  LEU B 860           
SHEET    1   E 5 VAL B 559  TYR B 566  0                                        
SHEET    2   E 5 PHE B 548  VAL B 555 -1  N  ARG B 554   O  GLN B 560           
SHEET    3   E 5 GLY B 536  LEU B 543 -1  N  PHE B 538   O  VAL B 553           
SHEET    4   E 5 LEU B 604  PHE B 608  1  O  THR B 607   N  LEU B 541           
SHEET    5   E 5 VAL B 658  VAL B 661  1  O  VAL B 661   N  PHE B 608           
SHEET    1   F 2 CYS B 612  GLY B 616  0                                        
SHEET    2   F 2 GLN B 619  LEU B 622 -1  O  ILE B 621   N  ARG B 613           
SHEET    1   G 6 LEU C 522  PRO C 523  0                                        
SHEET    2   G 6 ARG C 708  ASN C 712 -1  O  ASN C 712   N  LEU C 522           
SHEET    3   G 6 THR C 688  GLU C 695 -1  N  GLU C 694   O  MET C 709           
SHEET    4   G 6 CYS C 678  VAL C 684 -1  N  ILE C 683   O  ASN C 689           
SHEET    5   G 6 LEU C 860  ASP C 867  1  O  GLY C 865   N  LEU C 682           
SHEET    6   G 6 CYS C 892  GLN C 898  1  O  VAL C 893   N  LEU C 860           
SHEET    1   H 5 VAL C 559  TYR C 566  0                                        
SHEET    2   H 5 PHE C 548  VAL C 555 -1  N  ARG C 554   O  GLN C 560           
SHEET    3   H 5 GLY C 536  LEU C 543 -1  N  PHE C 538   O  VAL C 553           
SHEET    4   H 5 LEU C 604  PHE C 608  1  O  THR C 607   N  LEU C 541           
SHEET    5   H 5 VAL C 658  VAL C 661  1  O  VAL C 661   N  PHE C 608           
SHEET    1   I 2 CYS C 612  ARG C 613  0                                        
SHEET    2   I 2 ILE C 621  LEU C 622 -1  O  ILE C 621   N  ARG C 613           
SHEET    1   J 6 LEU D 522  PRO D 523  0                                        
SHEET    2   J 6 ARG D 708  ASN D 712 -1  O  ASN D 712   N  LEU D 522           
SHEET    3   J 6 THR D 688  GLU D 695 -1  N  GLU D 694   O  MET D 709           
SHEET    4   J 6 CYS D 678  VAL D 684 -1  N  ILE D 683   O  ASN D 689           
SHEET    5   J 6 LEU D 860  ASP D 867  1  O  GLY D 865   N  LEU D 682           
SHEET    6   J 6 CYS D 892  GLN D 898  1  O  VAL D 893   N  LEU D 860           
SHEET    1   K 5 VAL D 559  TYR D 566  0                                        
SHEET    2   K 5 PHE D 548  VAL D 555 -1  N  ARG D 554   O  GLN D 560           
SHEET    3   K 5 GLY D 536  LEU D 543 -1  N  PHE D 538   O  VAL D 553           
SHEET    4   K 5 LEU D 604  PHE D 608  1  O  THR D 607   N  LEU D 541           
SHEET    5   K 5 VAL D 658  VAL D 661  1  O  VAL D 661   N  PHE D 608           
SHEET    1   L 2 CYS D 612  GLY D 616  0                                        
SHEET    2   L 2 GLN D 619  LEU D 622 -1  O  ILE D 621   N  ARG D 613           
CRYST1   83.904   83.904  323.327  90.00  90.00  90.00 P 41         16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011918  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011918  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003093        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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