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Database: PDB
Entry: 4KQ1
LinkDB: 4KQ1
Original site: 4KQ1 
HEADER    TRANSFERASE                             14-MAY-13   4KQ1              
TITLE     CRYSTAL STRUCTURE OF YEAST GLYCOGEN SYNTHASE IN COMPLEX WITH URIDINE- 
TITLE    2 5'-MONOPHOSPHATE                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GSY2P;                                                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 2.4.1.11;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE FOSTERSO;              
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 764101;                                              
SOURCE   5 STRAIN: STRAIN ATCC 204508 / S288C;                                  
SOURCE   6 GENE: FOSTERSO_3265, GSY2 YLR258W L8479.8;                           
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    GLYCOSYLTRANSFERASE, GT-B, ROSSMANN FOLD, GLUCOSYLATION, TRANSFERASE  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.M.CHIKWANA,T.D.HURLEY                                               
REVDAT   2   05-FEB-14 4KQ1    1       JRNL                                     
REVDAT   1   11-DEC-13 4KQ1    0                                                
JRNL        AUTH   V.M.CHIKWANA,M.KHANNA,S.BASKARAN,V.S.TAGLIABRACCI,           
JRNL        AUTH 2 C.J.CONTRERAS,A.DEPAOLI-ROACH,P.J.ROACH,T.D.HURLEY           
JRNL        TITL   STRUCTURAL BASIS FOR 2'-PHOSPHATE INCORPORATION INTO         
JRNL        TITL 2 GLYCOGEN BY GLYCOGEN SYNTHASE.                               
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 110 20976 2013              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24324135                                                     
JRNL        DOI    10.1073/PNAS.1310106111                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.66 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
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) : 2.66                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.46                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 111215                         
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) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5574                            
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) : 2.66                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.73                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7354                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.13                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3480                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 421                          
REMARK   3   BIN FREE R VALUE                    : 0.3930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 20563                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 176                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 69.51                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 80.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.23000                                             
REMARK   3    B22 (A**2) : 9.42000                                              
REMARK   3    B33 (A**2) : -5.19000                                             
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): 0.548         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.317         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.253         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.395        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 21237 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 28785 ; 1.277 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2545 ; 5.627 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1067 ;37.153 ;23.599       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3558 ;18.590 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   156 ;19.253 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3134 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 16257 ; 0.005 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      2       A     205      4                      
REMARK   3           1     B      2       B     205      4                      
REMARK   3           1     C      2       C     205      4                      
REMARK   3           1     D      2       D     205      4                      
REMARK   3           2     A    208       A     278      4                      
REMARK   3           2     B    208       B     278      4                      
REMARK   3           2     C    208       C     278      4                      
REMARK   3           2     D    208       D     278      4                      
REMARK   3           3     A    599       A     639      4                      
REMARK   3           3     B    599       B     639      4                      
REMARK   3           3     C    599       C     639      4                      
REMARK   3           3     D    599       D     639      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   2536 ; 0.510 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   2536 ; 0.500 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   2536 ; 0.490 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   2536 ; 0.510 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   2536 ;14.670 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   2536 ;17.900 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   2536 ;16.380 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   2536 ;24.480 ; 2.000           
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    279       A     598      4                      
REMARK   3           1     B    279       B     598      4                      
REMARK   3           1     C    279       C     598      4                      
REMARK   3           1     D    279       D     598      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):   2592 ; 0.360 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):   2592 ; 0.380 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    C    (A):   2592 ; 0.410 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    D    (A):   2592 ; 0.360 ; 0.500           
REMARK   3   MEDIUM THERMAL     2    A (A**2):   2592 ;10.690 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    B (A**2):   2592 ;12.310 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    C (A**2):   2592 ; 9.640 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    D (A**2):   2592 ; 8.610 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 4KQ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB079650.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-NOV-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
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) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 111217                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.660                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.200                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.66                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 3NB0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 16% PEG 300, PH 6.2,     
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 298K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       96.54450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      102.18600            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      103.22300            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       96.54450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      102.18600            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      103.22300            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       96.54450            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      102.18600            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      103.22300            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       96.54450            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      102.18600            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      103.22300            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17350 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 98090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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     MET A   -18                                                      
REMARK 465     GLY A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     GLY A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     VAL A    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     ARG A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A   640                                                      
REMARK 465     GLY A   641                                                      
REMARK 465     LYS A   642                                                      
REMARK 465     LYS A   643                                                      
REMARK 465     LEU A   644                                                      
REMARK 465     LYS A   645                                                      
REMARK 465     VAL A   646                                                      
REMARK 465     ALA A   647                                                      
REMARK 465     ARG A   648                                                      
REMARK 465     PRO A   649                                                      
REMARK 465     LEU A   650                                                      
REMARK 465     SER A   651                                                      
REMARK 465     VAL A   652                                                      
REMARK 465     PRO A   653                                                      
REMARK 465     GLY A   654                                                      
REMARK 465     SER A   655                                                      
REMARK 465     PRO A   656                                                      
REMARK 465     ARG A   657                                                      
REMARK 465     ASP A   658                                                      
REMARK 465     LEU A   659                                                      
REMARK 465     ARG A   660                                                      
REMARK 465     SER A   661                                                      
REMARK 465     ASN A   662                                                      
REMARK 465     SER A   663                                                      
REMARK 465     THR A   664                                                      
REMARK 465     VAL A   665                                                      
REMARK 465     TYR A   666                                                      
REMARK 465     MET A   667                                                      
REMARK 465     THR A   668                                                      
REMARK 465     PRO A   669                                                      
REMARK 465     GLY A   670                                                      
REMARK 465     ASP A   671                                                      
REMARK 465     LEU A   672                                                      
REMARK 465     GLY A   673                                                      
REMARK 465     THR A   674                                                      
REMARK 465     LEU A   675                                                      
REMARK 465     GLN A   676                                                      
REMARK 465     GLU A   677                                                      
REMARK 465     VAL A   678                                                      
REMARK 465     ASN A   679                                                      
REMARK 465     ASN A   680                                                      
REMARK 465     ALA A   681                                                      
REMARK 465     ASP A   682                                                      
REMARK 465     ASP A   683                                                      
REMARK 465     TYR A   684                                                      
REMARK 465     PHE A   685                                                      
REMARK 465     SER A   686                                                      
REMARK 465     LEU A   687                                                      
REMARK 465     GLY A   688                                                      
REMARK 465     VAL A   689                                                      
REMARK 465     ASN A   690                                                      
REMARK 465     PRO A   691                                                      
REMARK 465     ALA A   692                                                      
REMARK 465     ALA A   693                                                      
REMARK 465     ASP A   694                                                      
REMARK 465     ASP A   695                                                      
REMARK 465     ASP A   696                                                      
REMARK 465     ASP A   697                                                      
REMARK 465     ASP A   698                                                      
REMARK 465     GLY A   699                                                      
REMARK 465     PRO A   700                                                      
REMARK 465     TYR A   701                                                      
REMARK 465     ALA A   702                                                      
REMARK 465     ASP A   703                                                      
REMARK 465     ASP A   704                                                      
REMARK 465     SER A   705                                                      
REMARK 465     MET B   -18                                                      
REMARK 465     GLY B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     SER B    -7                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     VAL B    -4                                                      
REMARK 465     PRO B    -3                                                      
REMARK 465     ARG B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B   640                                                      
REMARK 465     GLY B   641                                                      
REMARK 465     LYS B   642                                                      
REMARK 465     LYS B   643                                                      
REMARK 465     LEU B   644                                                      
REMARK 465     LYS B   645                                                      
REMARK 465     VAL B   646                                                      
REMARK 465     ALA B   647                                                      
REMARK 465     ARG B   648                                                      
REMARK 465     PRO B   649                                                      
REMARK 465     LEU B   650                                                      
REMARK 465     SER B   651                                                      
REMARK 465     VAL B   652                                                      
REMARK 465     PRO B   653                                                      
REMARK 465     GLY B   654                                                      
REMARK 465     SER B   655                                                      
REMARK 465     PRO B   656                                                      
REMARK 465     ARG B   657                                                      
REMARK 465     ASP B   658                                                      
REMARK 465     LEU B   659                                                      
REMARK 465     ARG B   660                                                      
REMARK 465     SER B   661                                                      
REMARK 465     ASN B   662                                                      
REMARK 465     SER B   663                                                      
REMARK 465     THR B   664                                                      
REMARK 465     VAL B   665                                                      
REMARK 465     TYR B   666                                                      
REMARK 465     MET B   667                                                      
REMARK 465     THR B   668                                                      
REMARK 465     PRO B   669                                                      
REMARK 465     GLY B   670                                                      
REMARK 465     ASP B   671                                                      
REMARK 465     LEU B   672                                                      
REMARK 465     GLY B   673                                                      
REMARK 465     THR B   674                                                      
REMARK 465     LEU B   675                                                      
REMARK 465     GLN B   676                                                      
REMARK 465     GLU B   677                                                      
REMARK 465     VAL B   678                                                      
REMARK 465     ASN B   679                                                      
REMARK 465     ASN B   680                                                      
REMARK 465     ALA B   681                                                      
REMARK 465     ASP B   682                                                      
REMARK 465     ASP B   683                                                      
REMARK 465     TYR B   684                                                      
REMARK 465     PHE B   685                                                      
REMARK 465     SER B   686                                                      
REMARK 465     LEU B   687                                                      
REMARK 465     GLY B   688                                                      
REMARK 465     VAL B   689                                                      
REMARK 465     ASN B   690                                                      
REMARK 465     PRO B   691                                                      
REMARK 465     ALA B   692                                                      
REMARK 465     ALA B   693                                                      
REMARK 465     ASP B   694                                                      
REMARK 465     ASP B   695                                                      
REMARK 465     ASP B   696                                                      
REMARK 465     ASP B   697                                                      
REMARK 465     ASP B   698                                                      
REMARK 465     GLY B   699                                                      
REMARK 465     PRO B   700                                                      
REMARK 465     TYR B   701                                                      
REMARK 465     ALA B   702                                                      
REMARK 465     ASP B   703                                                      
REMARK 465     ASP B   704                                                      
REMARK 465     SER B   705                                                      
REMARK 465     MET C   -18                                                      
REMARK 465     GLY C   -17                                                      
REMARK 465     SER C   -16                                                      
REMARK 465     SER C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     HIS C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     SER C    -7                                                      
REMARK 465     GLY C    -6                                                      
REMARK 465     LEU C    -5                                                      
REMARK 465     VAL C    -4                                                      
REMARK 465     PRO C    -3                                                      
REMARK 465     ARG C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY C   640                                                      
REMARK 465     GLY C   641                                                      
REMARK 465     LYS C   642                                                      
REMARK 465     LYS C   643                                                      
REMARK 465     LEU C   644                                                      
REMARK 465     LYS C   645                                                      
REMARK 465     VAL C   646                                                      
REMARK 465     ALA C   647                                                      
REMARK 465     ARG C   648                                                      
REMARK 465     PRO C   649                                                      
REMARK 465     LEU C   650                                                      
REMARK 465     SER C   651                                                      
REMARK 465     VAL C   652                                                      
REMARK 465     PRO C   653                                                      
REMARK 465     GLY C   654                                                      
REMARK 465     SER C   655                                                      
REMARK 465     PRO C   656                                                      
REMARK 465     ARG C   657                                                      
REMARK 465     ASP C   658                                                      
REMARK 465     LEU C   659                                                      
REMARK 465     ARG C   660                                                      
REMARK 465     SER C   661                                                      
REMARK 465     ASN C   662                                                      
REMARK 465     SER C   663                                                      
REMARK 465     THR C   664                                                      
REMARK 465     VAL C   665                                                      
REMARK 465     TYR C   666                                                      
REMARK 465     MET C   667                                                      
REMARK 465     THR C   668                                                      
REMARK 465     PRO C   669                                                      
REMARK 465     GLY C   670                                                      
REMARK 465     ASP C   671                                                      
REMARK 465     LEU C   672                                                      
REMARK 465     GLY C   673                                                      
REMARK 465     THR C   674                                                      
REMARK 465     LEU C   675                                                      
REMARK 465     GLN C   676                                                      
REMARK 465     GLU C   677                                                      
REMARK 465     VAL C   678                                                      
REMARK 465     ASN C   679                                                      
REMARK 465     ASN C   680                                                      
REMARK 465     ALA C   681                                                      
REMARK 465     ASP C   682                                                      
REMARK 465     ASP C   683                                                      
REMARK 465     TYR C   684                                                      
REMARK 465     PHE C   685                                                      
REMARK 465     SER C   686                                                      
REMARK 465     LEU C   687                                                      
REMARK 465     GLY C   688                                                      
REMARK 465     VAL C   689                                                      
REMARK 465     ASN C   690                                                      
REMARK 465     PRO C   691                                                      
REMARK 465     ALA C   692                                                      
REMARK 465     ALA C   693                                                      
REMARK 465     ASP C   694                                                      
REMARK 465     ASP C   695                                                      
REMARK 465     ASP C   696                                                      
REMARK 465     ASP C   697                                                      
REMARK 465     ASP C   698                                                      
REMARK 465     GLY C   699                                                      
REMARK 465     PRO C   700                                                      
REMARK 465     TYR C   701                                                      
REMARK 465     ALA C   702                                                      
REMARK 465     ASP C   703                                                      
REMARK 465     ASP C   704                                                      
REMARK 465     SER C   705                                                      
REMARK 465     MET D   -18                                                      
REMARK 465     GLY D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     SER D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     HIS D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     SER D    -7                                                      
REMARK 465     GLY D    -6                                                      
REMARK 465     LEU D    -5                                                      
REMARK 465     VAL D    -4                                                      
REMARK 465     PRO D    -3                                                      
REMARK 465     ARG D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D   206                                                      
REMARK 465     PHE D   207                                                      
REMARK 465     GLY D   640                                                      
REMARK 465     GLY D   641                                                      
REMARK 465     LYS D   642                                                      
REMARK 465     LYS D   643                                                      
REMARK 465     LEU D   644                                                      
REMARK 465     LYS D   645                                                      
REMARK 465     VAL D   646                                                      
REMARK 465     ALA D   647                                                      
REMARK 465     ARG D   648                                                      
REMARK 465     PRO D   649                                                      
REMARK 465     LEU D   650                                                      
REMARK 465     SER D   651                                                      
REMARK 465     VAL D   652                                                      
REMARK 465     PRO D   653                                                      
REMARK 465     GLY D   654                                                      
REMARK 465     SER D   655                                                      
REMARK 465     PRO D   656                                                      
REMARK 465     ARG D   657                                                      
REMARK 465     ASP D   658                                                      
REMARK 465     LEU D   659                                                      
REMARK 465     ARG D   660                                                      
REMARK 465     SER D   661                                                      
REMARK 465     ASN D   662                                                      
REMARK 465     SER D   663                                                      
REMARK 465     THR D   664                                                      
REMARK 465     VAL D   665                                                      
REMARK 465     TYR D   666                                                      
REMARK 465     MET D   667                                                      
REMARK 465     THR D   668                                                      
REMARK 465     PRO D   669                                                      
REMARK 465     GLY D   670                                                      
REMARK 465     ASP D   671                                                      
REMARK 465     LEU D   672                                                      
REMARK 465     GLY D   673                                                      
REMARK 465     THR D   674                                                      
REMARK 465     LEU D   675                                                      
REMARK 465     GLN D   676                                                      
REMARK 465     GLU D   677                                                      
REMARK 465     VAL D   678                                                      
REMARK 465     ASN D   679                                                      
REMARK 465     ASN D   680                                                      
REMARK 465     ALA D   681                                                      
REMARK 465     ASP D   682                                                      
REMARK 465     ASP D   683                                                      
REMARK 465     TYR D   684                                                      
REMARK 465     PHE D   685                                                      
REMARK 465     SER D   686                                                      
REMARK 465     LEU D   687                                                      
REMARK 465     GLY D   688                                                      
REMARK 465     VAL D   689                                                      
REMARK 465     ASN D   690                                                      
REMARK 465     PRO D   691                                                      
REMARK 465     ALA D   692                                                      
REMARK 465     ALA D   693                                                      
REMARK 465     ASP D   694                                                      
REMARK 465     ASP D   695                                                      
REMARK 465     ASP D   696                                                      
REMARK 465     ASP D   697                                                      
REMARK 465     ASP D   698                                                      
REMARK 465     GLY D   699                                                      
REMARK 465     PRO D   700                                                      
REMARK 465     TYR D   701                                                      
REMARK 465     ALA D   702                                                      
REMARK 465     ASP D   703                                                      
REMARK 465     ASP D   704                                                      
REMARK 465     SER D   705                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP B   450     NH2  ARG B   460              2.12            
REMARK 500   OG1  THR A   195     OE1  GLU A   254              2.16            
REMARK 500   NH2  ARG B     3     O    ASP B   158              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU D 488   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  40     -125.92     52.47                                   
REMARK 500    GLU A  57        5.94   -150.55                                   
REMARK 500    ALA A 100       88.37     50.32                                   
REMARK 500    VAL A 111      -12.47   -145.07                                   
REMARK 500    ARG A 112      -28.42    -39.77                                   
REMARK 500    ASN A 133        7.38    -68.78                                   
REMARK 500    GLU A 169      155.48     59.69                                   
REMARK 500    ARG A 183       56.79     21.92                                   
REMARK 500    ASP A 185       47.17    -82.65                                   
REMARK 500    ALA A 194      126.35    177.87                                   
REMARK 500    GLU A 214       -4.10    -59.98                                   
REMARK 500    PHE A 301       31.66    -95.11                                   
REMARK 500    ASN A 362       49.60   -108.20                                   
REMARK 500    SER A 363     -170.67     68.73                                   
REMARK 500    PRO A 401       41.06   -101.70                                   
REMARK 500    PRO A 435      151.90    -42.60                                   
REMARK 500    GLN A 463       69.61     61.30                                   
REMARK 500    PRO A 478       43.95    -81.17                                   
REMARK 500    TRP A 511      -62.03   -128.13                                   
REMARK 500    MET A 521        2.43    -62.86                                   
REMARK 500    ARG A 557      -73.45   -113.60                                   
REMARK 500    PHE A 558       30.50    -84.77                                   
REMARK 500    PRO A 561      -31.92    -35.37                                   
REMARK 500    TRP A 599      -16.80    -48.49                                   
REMARK 500    VAL A 626      -65.56    -97.10                                   
REMARK 500    GLU B  16       47.59   -105.04                                   
REMARK 500    VAL B  17     -112.77    -70.76                                   
REMARK 500    ASN B  19      105.79   -165.20                                   
REMARK 500    LYS B  40      -99.32     59.57                                   
REMARK 500    PRO B  48     -153.85    -68.52                                   
REMARK 500    THR B  53      -33.82   -133.72                                   
REMARK 500    SER B  85       -4.30    -59.50                                   
REMARK 500    ALA B 100       82.17     22.78                                   
REMARK 500    VAL B 111      -13.17   -152.42                                   
REMARK 500    ARG B 112      -36.13    -37.84                                   
REMARK 500    SER B 115      -82.39    -53.35                                   
REMARK 500    SER B 130       79.72   -158.91                                   
REMARK 500    GLU B 169      141.77     75.11                                   
REMARK 500    ALA B 194      162.88    168.14                                   
REMARK 500    GLU B 214        2.00    -68.41                                   
REMARK 500    HIS B 302      135.97    -37.54                                   
REMARK 500    CYS B 304       44.25   -174.38                                   
REMARK 500    ASN B 362       41.53   -105.03                                   
REMARK 500    SER B 363     -168.90     63.98                                   
REMARK 500    GLU B 367      -63.02    -27.57                                   
REMARK 500    LEU B 413      -33.47    -39.03                                   
REMARK 500    PRO B 478       40.77    -74.43                                   
REMARK 500    ALA B 483      -14.16    -42.65                                   
REMARK 500    GLU B 509       87.61   -163.85                                   
REMARK 500    TRP B 511      -61.42   -121.64                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      89 RAMACHANDRAN OUTLIERS.                        
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 U5P A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U5P B 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P B 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U5P C 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P C 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U5P D 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P D 802                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4KQ2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KQM   RELATED DB: PDB                                   
DBREF  4KQ1 A    1   705  UNP    E7NKU1   E7NKU1_YEASO     1    705             
DBREF  4KQ1 B    1   705  UNP    E7NKU1   E7NKU1_YEASO     1    705             
DBREF  4KQ1 C    1   705  UNP    E7NKU1   E7NKU1_YEASO     1    705             
DBREF  4KQ1 D    1   705  UNP    E7NKU1   E7NKU1_YEASO     1    705             
SEQADV 4KQ1 MET A  -18  UNP  E7NKU1              INITIATING METHIONINE          
SEQADV 4KQ1 GLY A  -17  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER A  -16  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER A  -15  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS A  -14  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS A  -13  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS A  -12  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS A  -11  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS A  -10  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS A   -9  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER A   -8  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER A   -7  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 GLY A   -6  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 LEU A   -5  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 VAL A   -4  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 PRO A   -3  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 ARG A   -2  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 GLY A   -1  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER A    0  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 ALA A  589  UNP  E7NKU1    ARG   589 ENGINEERED MUTATION            
SEQADV 4KQ1 ALA A  592  UNP  E7NKU1    ARG   592 ENGINEERED MUTATION            
SEQADV 4KQ1 MET B  -18  UNP  E7NKU1              INITIATING METHIONINE          
SEQADV 4KQ1 GLY B  -17  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER B  -16  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER B  -15  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS B  -14  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS B  -13  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS B  -12  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS B  -11  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS B  -10  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS B   -9  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER B   -8  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER B   -7  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 GLY B   -6  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 LEU B   -5  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 VAL B   -4  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 PRO B   -3  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 ARG B   -2  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 GLY B   -1  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER B    0  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 ALA B  589  UNP  E7NKU1    ARG   589 ENGINEERED MUTATION            
SEQADV 4KQ1 ALA B  592  UNP  E7NKU1    ARG   592 ENGINEERED MUTATION            
SEQADV 4KQ1 MET C  -18  UNP  E7NKU1              INITIATING METHIONINE          
SEQADV 4KQ1 GLY C  -17  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER C  -16  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER C  -15  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS C  -14  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS C  -13  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS C  -12  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS C  -11  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS C  -10  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS C   -9  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER C   -8  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER C   -7  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 GLY C   -6  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 LEU C   -5  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 VAL C   -4  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 PRO C   -3  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 ARG C   -2  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 GLY C   -1  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER C    0  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 ALA C  589  UNP  E7NKU1    ARG   589 ENGINEERED MUTATION            
SEQADV 4KQ1 ALA C  592  UNP  E7NKU1    ARG   592 ENGINEERED MUTATION            
SEQADV 4KQ1 MET D  -18  UNP  E7NKU1              INITIATING METHIONINE          
SEQADV 4KQ1 GLY D  -17  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER D  -16  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER D  -15  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS D  -14  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS D  -13  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS D  -12  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS D  -11  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS D  -10  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 HIS D   -9  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER D   -8  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER D   -7  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 GLY D   -6  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 LEU D   -5  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 VAL D   -4  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 PRO D   -3  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 ARG D   -2  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 GLY D   -1  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 SER D    0  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQ1 ALA D  589  UNP  E7NKU1    ARG   589 ENGINEERED MUTATION            
SEQADV 4KQ1 ALA D  592  UNP  E7NKU1    ARG   592 ENGINEERED MUTATION            
SEQRES   1 A  724  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  724  LEU VAL PRO ARG GLY SER MET SER ARG ASP LEU GLN ASN          
SEQRES   3 A  724  HIS LEU LEU PHE GLU THR ALA THR GLU VAL ALA ASN ARG          
SEQRES   4 A  724  VAL GLY GLY ILE TYR SER VAL LEU LYS SER LYS ALA PRO          
SEQRES   5 A  724  ILE THR VAL ALA GLN TYR LYS ASP HIS TYR HIS LEU ILE          
SEQRES   6 A  724  GLY PRO LEU ASN LYS ALA THR TYR GLN ASN GLU VAL ASP          
SEQRES   7 A  724  ILE LEU ASP TRP LYS LYS PRO GLU ALA PHE SER ASP GLU          
SEQRES   8 A  724  MET ARG PRO VAL GLN HIS ALA LEU GLN THR MET GLU SER          
SEQRES   9 A  724  ARG GLY VAL HIS PHE VAL TYR GLY ARG TRP LEU ILE GLU          
SEQRES  10 A  724  GLY ALA PRO LYS VAL ILE LEU PHE ASP LEU ASP SER VAL          
SEQRES  11 A  724  ARG GLY TYR SER ASN GLU TRP LYS GLY ASP LEU TRP SER          
SEQRES  12 A  724  LEU VAL GLY ILE PRO SER PRO GLU ASN ASP PHE GLU THR          
SEQRES  13 A  724  ASN ASP ALA ILE LEU LEU GLY TYR THR VAL ALA TRP PHE          
SEQRES  14 A  724  LEU GLY GLU VAL ALA HIS LEU ASP SER GLN HIS ALA ILE          
SEQRES  15 A  724  VAL ALA HIS PHE HIS GLU TRP LEU ALA GLY VAL ALA LEU          
SEQRES  16 A  724  PRO LEU CYS ARG LYS ARG ARG ILE ASP VAL VAL THR ILE          
SEQRES  17 A  724  PHE THR THR HIS ALA THR LEU LEU GLY ARG TYR LEU CYS          
SEQRES  18 A  724  ALA SER GLY SER PHE ASP PHE TYR ASN CYS LEU GLU SER          
SEQRES  19 A  724  VAL ASP VAL ASP HIS GLU ALA GLY ARG PHE GLY ILE TYR          
SEQRES  20 A  724  HIS ARG TYR CYS ILE GLU ARG ALA ALA ALA HIS SER ALA          
SEQRES  21 A  724  ASP VAL PHE THR THR VAL SER GLN ILE THR ALA PHE GLU          
SEQRES  22 A  724  ALA GLU HIS LEU LEU LYS ARG LYS PRO ASP GLY ILE LEU          
SEQRES  23 A  724  PRO ASN GLY LEU ASN VAL ILE LYS PHE GLN ALA PHE HIS          
SEQRES  24 A  724  GLU PHE GLN ASN LEU HIS ALA LEU LYS LYS GLU LYS ILE          
SEQRES  25 A  724  ASN ASP PHE VAL ARG GLY HIS PHE HIS GLY CYS PHE ASP          
SEQRES  26 A  724  PHE ASP LEU ASP ASN THR LEU TYR PHE PHE ILE ALA GLY          
SEQRES  27 A  724  ARG TYR GLU TYR LYS ASN LYS GLY ALA ASP MET PHE ILE          
SEQRES  28 A  724  GLU ALA LEU ALA ARG LEU ASN TYR ARG LEU LYS VAL SER          
SEQRES  29 A  724  GLY SER LYS LYS THR VAL VAL ALA PHE ILE VAL MET PRO          
SEQRES  30 A  724  ALA LYS ASN ASN SER PHE THR VAL GLU ALA LEU LYS GLY          
SEQRES  31 A  724  GLN ALA GLU VAL ARG ALA LEU GLU ASN THR VAL HIS GLU          
SEQRES  32 A  724  VAL THR THR SER ILE GLY LYS ARG ILE PHE ASP HIS ALA          
SEQRES  33 A  724  ILE ARG TYR PRO HIS ASN GLY LEU THR THR GLU LEU PRO          
SEQRES  34 A  724  THR ASP LEU GLY GLU LEU LEU LYS SER SER ASP LYS VAL          
SEQRES  35 A  724  MET LEU LYS ARG ARG ILE LEU ALA LEU ARG ARG PRO GLU          
SEQRES  36 A  724  GLY GLN LEU PRO PRO ILE VAL THR HIS ASN MET VAL ASP          
SEQRES  37 A  724  ASP ALA ASN ASP LEU ILE LEU ASN LYS ILE ARG GLN VAL          
SEQRES  38 A  724  GLN LEU PHE ASN SER PRO SER ASP ARG VAL LYS MET ILE          
SEQRES  39 A  724  PHE HIS PRO GLU PHE LEU ASN ALA ASN ASN PRO ILE LEU          
SEQRES  40 A  724  GLY LEU ASP TYR ASP GLU PHE VAL ARG GLY CYS HIS LEU          
SEQRES  41 A  724  GLY VAL PHE PRO SER TYR TYR GLU PRO TRP GLY TYR THR          
SEQRES  42 A  724  PRO ALA GLU CYS THR VAL MET GLY VAL PRO SER ILE THR          
SEQRES  43 A  724  THR ASN VAL SER GLY PHE GLY SER TYR MET GLU ASP LEU          
SEQRES  44 A  724  ILE GLU THR ASN GLN ALA LYS ASP TYR GLY ILE TYR ILE          
SEQRES  45 A  724  VAL ASP ARG ARG PHE LYS ALA PRO ASP GLU SER VAL GLU          
SEQRES  46 A  724  GLN LEU VAL ASP TYR MET GLU GLU PHE VAL LYS LYS THR          
SEQRES  47 A  724  ARG ARG GLN ARG ILE ASN GLN ARG ASN ALA THR GLU ALA          
SEQRES  48 A  724  LEU SER ASP LEU LEU ASP TRP LYS ARG MET GLY LEU GLU          
SEQRES  49 A  724  TYR VAL LYS ALA ARG GLN LEU ALA LEU ARG ARG GLY TYR          
SEQRES  50 A  724  PRO ASP GLN PHE ARG GLU LEU VAL GLY GLU GLU LEU ASN          
SEQRES  51 A  724  ASP SER ASN MET ASP ALA LEU ALA GLY GLY LYS LYS LEU          
SEQRES  52 A  724  LYS VAL ALA ARG PRO LEU SER VAL PRO GLY SER PRO ARG          
SEQRES  53 A  724  ASP LEU ARG SER ASN SER THR VAL TYR MET THR PRO GLY          
SEQRES  54 A  724  ASP LEU GLY THR LEU GLN GLU VAL ASN ASN ALA ASP ASP          
SEQRES  55 A  724  TYR PHE SER LEU GLY VAL ASN PRO ALA ALA ASP ASP ASP          
SEQRES  56 A  724  ASP ASP GLY PRO TYR ALA ASP ASP SER                          
SEQRES   1 B  724  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  724  LEU VAL PRO ARG GLY SER MET SER ARG ASP LEU GLN ASN          
SEQRES   3 B  724  HIS LEU LEU PHE GLU THR ALA THR GLU VAL ALA ASN ARG          
SEQRES   4 B  724  VAL GLY GLY ILE TYR SER VAL LEU LYS SER LYS ALA PRO          
SEQRES   5 B  724  ILE THR VAL ALA GLN TYR LYS ASP HIS TYR HIS LEU ILE          
SEQRES   6 B  724  GLY PRO LEU ASN LYS ALA THR TYR GLN ASN GLU VAL ASP          
SEQRES   7 B  724  ILE LEU ASP TRP LYS LYS PRO GLU ALA PHE SER ASP GLU          
SEQRES   8 B  724  MET ARG PRO VAL GLN HIS ALA LEU GLN THR MET GLU SER          
SEQRES   9 B  724  ARG GLY VAL HIS PHE VAL TYR GLY ARG TRP LEU ILE GLU          
SEQRES  10 B  724  GLY ALA PRO LYS VAL ILE LEU PHE ASP LEU ASP SER VAL          
SEQRES  11 B  724  ARG GLY TYR SER ASN GLU TRP LYS GLY ASP LEU TRP SER          
SEQRES  12 B  724  LEU VAL GLY ILE PRO SER PRO GLU ASN ASP PHE GLU THR          
SEQRES  13 B  724  ASN ASP ALA ILE LEU LEU GLY TYR THR VAL ALA TRP PHE          
SEQRES  14 B  724  LEU GLY GLU VAL ALA HIS LEU ASP SER GLN HIS ALA ILE          
SEQRES  15 B  724  VAL ALA HIS PHE HIS GLU TRP LEU ALA GLY VAL ALA LEU          
SEQRES  16 B  724  PRO LEU CYS ARG LYS ARG ARG ILE ASP VAL VAL THR ILE          
SEQRES  17 B  724  PHE THR THR HIS ALA THR LEU LEU GLY ARG TYR LEU CYS          
SEQRES  18 B  724  ALA SER GLY SER PHE ASP PHE TYR ASN CYS LEU GLU SER          
SEQRES  19 B  724  VAL ASP VAL ASP HIS GLU ALA GLY ARG PHE GLY ILE TYR          
SEQRES  20 B  724  HIS ARG TYR CYS ILE GLU ARG ALA ALA ALA HIS SER ALA          
SEQRES  21 B  724  ASP VAL PHE THR THR VAL SER GLN ILE THR ALA PHE GLU          
SEQRES  22 B  724  ALA GLU HIS LEU LEU LYS ARG LYS PRO ASP GLY ILE LEU          
SEQRES  23 B  724  PRO ASN GLY LEU ASN VAL ILE LYS PHE GLN ALA PHE HIS          
SEQRES  24 B  724  GLU PHE GLN ASN LEU HIS ALA LEU LYS LYS GLU LYS ILE          
SEQRES  25 B  724  ASN ASP PHE VAL ARG GLY HIS PHE HIS GLY CYS PHE ASP          
SEQRES  26 B  724  PHE ASP LEU ASP ASN THR LEU TYR PHE PHE ILE ALA GLY          
SEQRES  27 B  724  ARG TYR GLU TYR LYS ASN LYS GLY ALA ASP MET PHE ILE          
SEQRES  28 B  724  GLU ALA LEU ALA ARG LEU ASN TYR ARG LEU LYS VAL SER          
SEQRES  29 B  724  GLY SER LYS LYS THR VAL VAL ALA PHE ILE VAL MET PRO          
SEQRES  30 B  724  ALA LYS ASN ASN SER PHE THR VAL GLU ALA LEU LYS GLY          
SEQRES  31 B  724  GLN ALA GLU VAL ARG ALA LEU GLU ASN THR VAL HIS GLU          
SEQRES  32 B  724  VAL THR THR SER ILE GLY LYS ARG ILE PHE ASP HIS ALA          
SEQRES  33 B  724  ILE ARG TYR PRO HIS ASN GLY LEU THR THR GLU LEU PRO          
SEQRES  34 B  724  THR ASP LEU GLY GLU LEU LEU LYS SER SER ASP LYS VAL          
SEQRES  35 B  724  MET LEU LYS ARG ARG ILE LEU ALA LEU ARG ARG PRO GLU          
SEQRES  36 B  724  GLY GLN LEU PRO PRO ILE VAL THR HIS ASN MET VAL ASP          
SEQRES  37 B  724  ASP ALA ASN ASP LEU ILE LEU ASN LYS ILE ARG GLN VAL          
SEQRES  38 B  724  GLN LEU PHE ASN SER PRO SER ASP ARG VAL LYS MET ILE          
SEQRES  39 B  724  PHE HIS PRO GLU PHE LEU ASN ALA ASN ASN PRO ILE LEU          
SEQRES  40 B  724  GLY LEU ASP TYR ASP GLU PHE VAL ARG GLY CYS HIS LEU          
SEQRES  41 B  724  GLY VAL PHE PRO SER TYR TYR GLU PRO TRP GLY TYR THR          
SEQRES  42 B  724  PRO ALA GLU CYS THR VAL MET GLY VAL PRO SER ILE THR          
SEQRES  43 B  724  THR ASN VAL SER GLY PHE GLY SER TYR MET GLU ASP LEU          
SEQRES  44 B  724  ILE GLU THR ASN GLN ALA LYS ASP TYR GLY ILE TYR ILE          
SEQRES  45 B  724  VAL ASP ARG ARG PHE LYS ALA PRO ASP GLU SER VAL GLU          
SEQRES  46 B  724  GLN LEU VAL ASP TYR MET GLU GLU PHE VAL LYS LYS THR          
SEQRES  47 B  724  ARG ARG GLN ARG ILE ASN GLN ARG ASN ALA THR GLU ALA          
SEQRES  48 B  724  LEU SER ASP LEU LEU ASP TRP LYS ARG MET GLY LEU GLU          
SEQRES  49 B  724  TYR VAL LYS ALA ARG GLN LEU ALA LEU ARG ARG GLY TYR          
SEQRES  50 B  724  PRO ASP GLN PHE ARG GLU LEU VAL GLY GLU GLU LEU ASN          
SEQRES  51 B  724  ASP SER ASN MET ASP ALA LEU ALA GLY GLY LYS LYS LEU          
SEQRES  52 B  724  LYS VAL ALA ARG PRO LEU SER VAL PRO GLY SER PRO ARG          
SEQRES  53 B  724  ASP LEU ARG SER ASN SER THR VAL TYR MET THR PRO GLY          
SEQRES  54 B  724  ASP LEU GLY THR LEU GLN GLU VAL ASN ASN ALA ASP ASP          
SEQRES  55 B  724  TYR PHE SER LEU GLY VAL ASN PRO ALA ALA ASP ASP ASP          
SEQRES  56 B  724  ASP ASP GLY PRO TYR ALA ASP ASP SER                          
SEQRES   1 C  724  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  724  LEU VAL PRO ARG GLY SER MET SER ARG ASP LEU GLN ASN          
SEQRES   3 C  724  HIS LEU LEU PHE GLU THR ALA THR GLU VAL ALA ASN ARG          
SEQRES   4 C  724  VAL GLY GLY ILE TYR SER VAL LEU LYS SER LYS ALA PRO          
SEQRES   5 C  724  ILE THR VAL ALA GLN TYR LYS ASP HIS TYR HIS LEU ILE          
SEQRES   6 C  724  GLY PRO LEU ASN LYS ALA THR TYR GLN ASN GLU VAL ASP          
SEQRES   7 C  724  ILE LEU ASP TRP LYS LYS PRO GLU ALA PHE SER ASP GLU          
SEQRES   8 C  724  MET ARG PRO VAL GLN HIS ALA LEU GLN THR MET GLU SER          
SEQRES   9 C  724  ARG GLY VAL HIS PHE VAL TYR GLY ARG TRP LEU ILE GLU          
SEQRES  10 C  724  GLY ALA PRO LYS VAL ILE LEU PHE ASP LEU ASP SER VAL          
SEQRES  11 C  724  ARG GLY TYR SER ASN GLU TRP LYS GLY ASP LEU TRP SER          
SEQRES  12 C  724  LEU VAL GLY ILE PRO SER PRO GLU ASN ASP PHE GLU THR          
SEQRES  13 C  724  ASN ASP ALA ILE LEU LEU GLY TYR THR VAL ALA TRP PHE          
SEQRES  14 C  724  LEU GLY GLU VAL ALA HIS LEU ASP SER GLN HIS ALA ILE          
SEQRES  15 C  724  VAL ALA HIS PHE HIS GLU TRP LEU ALA GLY VAL ALA LEU          
SEQRES  16 C  724  PRO LEU CYS ARG LYS ARG ARG ILE ASP VAL VAL THR ILE          
SEQRES  17 C  724  PHE THR THR HIS ALA THR LEU LEU GLY ARG TYR LEU CYS          
SEQRES  18 C  724  ALA SER GLY SER PHE ASP PHE TYR ASN CYS LEU GLU SER          
SEQRES  19 C  724  VAL ASP VAL ASP HIS GLU ALA GLY ARG PHE GLY ILE TYR          
SEQRES  20 C  724  HIS ARG TYR CYS ILE GLU ARG ALA ALA ALA HIS SER ALA          
SEQRES  21 C  724  ASP VAL PHE THR THR VAL SER GLN ILE THR ALA PHE GLU          
SEQRES  22 C  724  ALA GLU HIS LEU LEU LYS ARG LYS PRO ASP GLY ILE LEU          
SEQRES  23 C  724  PRO ASN GLY LEU ASN VAL ILE LYS PHE GLN ALA PHE HIS          
SEQRES  24 C  724  GLU PHE GLN ASN LEU HIS ALA LEU LYS LYS GLU LYS ILE          
SEQRES  25 C  724  ASN ASP PHE VAL ARG GLY HIS PHE HIS GLY CYS PHE ASP          
SEQRES  26 C  724  PHE ASP LEU ASP ASN THR LEU TYR PHE PHE ILE ALA GLY          
SEQRES  27 C  724  ARG TYR GLU TYR LYS ASN LYS GLY ALA ASP MET PHE ILE          
SEQRES  28 C  724  GLU ALA LEU ALA ARG LEU ASN TYR ARG LEU LYS VAL SER          
SEQRES  29 C  724  GLY SER LYS LYS THR VAL VAL ALA PHE ILE VAL MET PRO          
SEQRES  30 C  724  ALA LYS ASN ASN SER PHE THR VAL GLU ALA LEU LYS GLY          
SEQRES  31 C  724  GLN ALA GLU VAL ARG ALA LEU GLU ASN THR VAL HIS GLU          
SEQRES  32 C  724  VAL THR THR SER ILE GLY LYS ARG ILE PHE ASP HIS ALA          
SEQRES  33 C  724  ILE ARG TYR PRO HIS ASN GLY LEU THR THR GLU LEU PRO          
SEQRES  34 C  724  THR ASP LEU GLY GLU LEU LEU LYS SER SER ASP LYS VAL          
SEQRES  35 C  724  MET LEU LYS ARG ARG ILE LEU ALA LEU ARG ARG PRO GLU          
SEQRES  36 C  724  GLY GLN LEU PRO PRO ILE VAL THR HIS ASN MET VAL ASP          
SEQRES  37 C  724  ASP ALA ASN ASP LEU ILE LEU ASN LYS ILE ARG GLN VAL          
SEQRES  38 C  724  GLN LEU PHE ASN SER PRO SER ASP ARG VAL LYS MET ILE          
SEQRES  39 C  724  PHE HIS PRO GLU PHE LEU ASN ALA ASN ASN PRO ILE LEU          
SEQRES  40 C  724  GLY LEU ASP TYR ASP GLU PHE VAL ARG GLY CYS HIS LEU          
SEQRES  41 C  724  GLY VAL PHE PRO SER TYR TYR GLU PRO TRP GLY TYR THR          
SEQRES  42 C  724  PRO ALA GLU CYS THR VAL MET GLY VAL PRO SER ILE THR          
SEQRES  43 C  724  THR ASN VAL SER GLY PHE GLY SER TYR MET GLU ASP LEU          
SEQRES  44 C  724  ILE GLU THR ASN GLN ALA LYS ASP TYR GLY ILE TYR ILE          
SEQRES  45 C  724  VAL ASP ARG ARG PHE LYS ALA PRO ASP GLU SER VAL GLU          
SEQRES  46 C  724  GLN LEU VAL ASP TYR MET GLU GLU PHE VAL LYS LYS THR          
SEQRES  47 C  724  ARG ARG GLN ARG ILE ASN GLN ARG ASN ALA THR GLU ALA          
SEQRES  48 C  724  LEU SER ASP LEU LEU ASP TRP LYS ARG MET GLY LEU GLU          
SEQRES  49 C  724  TYR VAL LYS ALA ARG GLN LEU ALA LEU ARG ARG GLY TYR          
SEQRES  50 C  724  PRO ASP GLN PHE ARG GLU LEU VAL GLY GLU GLU LEU ASN          
SEQRES  51 C  724  ASP SER ASN MET ASP ALA LEU ALA GLY GLY LYS LYS LEU          
SEQRES  52 C  724  LYS VAL ALA ARG PRO LEU SER VAL PRO GLY SER PRO ARG          
SEQRES  53 C  724  ASP LEU ARG SER ASN SER THR VAL TYR MET THR PRO GLY          
SEQRES  54 C  724  ASP LEU GLY THR LEU GLN GLU VAL ASN ASN ALA ASP ASP          
SEQRES  55 C  724  TYR PHE SER LEU GLY VAL ASN PRO ALA ALA ASP ASP ASP          
SEQRES  56 C  724  ASP ASP GLY PRO TYR ALA ASP ASP SER                          
SEQRES   1 D  724  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  724  LEU VAL PRO ARG GLY SER MET SER ARG ASP LEU GLN ASN          
SEQRES   3 D  724  HIS LEU LEU PHE GLU THR ALA THR GLU VAL ALA ASN ARG          
SEQRES   4 D  724  VAL GLY GLY ILE TYR SER VAL LEU LYS SER LYS ALA PRO          
SEQRES   5 D  724  ILE THR VAL ALA GLN TYR LYS ASP HIS TYR HIS LEU ILE          
SEQRES   6 D  724  GLY PRO LEU ASN LYS ALA THR TYR GLN ASN GLU VAL ASP          
SEQRES   7 D  724  ILE LEU ASP TRP LYS LYS PRO GLU ALA PHE SER ASP GLU          
SEQRES   8 D  724  MET ARG PRO VAL GLN HIS ALA LEU GLN THR MET GLU SER          
SEQRES   9 D  724  ARG GLY VAL HIS PHE VAL TYR GLY ARG TRP LEU ILE GLU          
SEQRES  10 D  724  GLY ALA PRO LYS VAL ILE LEU PHE ASP LEU ASP SER VAL          
SEQRES  11 D  724  ARG GLY TYR SER ASN GLU TRP LYS GLY ASP LEU TRP SER          
SEQRES  12 D  724  LEU VAL GLY ILE PRO SER PRO GLU ASN ASP PHE GLU THR          
SEQRES  13 D  724  ASN ASP ALA ILE LEU LEU GLY TYR THR VAL ALA TRP PHE          
SEQRES  14 D  724  LEU GLY GLU VAL ALA HIS LEU ASP SER GLN HIS ALA ILE          
SEQRES  15 D  724  VAL ALA HIS PHE HIS GLU TRP LEU ALA GLY VAL ALA LEU          
SEQRES  16 D  724  PRO LEU CYS ARG LYS ARG ARG ILE ASP VAL VAL THR ILE          
SEQRES  17 D  724  PHE THR THR HIS ALA THR LEU LEU GLY ARG TYR LEU CYS          
SEQRES  18 D  724  ALA SER GLY SER PHE ASP PHE TYR ASN CYS LEU GLU SER          
SEQRES  19 D  724  VAL ASP VAL ASP HIS GLU ALA GLY ARG PHE GLY ILE TYR          
SEQRES  20 D  724  HIS ARG TYR CYS ILE GLU ARG ALA ALA ALA HIS SER ALA          
SEQRES  21 D  724  ASP VAL PHE THR THR VAL SER GLN ILE THR ALA PHE GLU          
SEQRES  22 D  724  ALA GLU HIS LEU LEU LYS ARG LYS PRO ASP GLY ILE LEU          
SEQRES  23 D  724  PRO ASN GLY LEU ASN VAL ILE LYS PHE GLN ALA PHE HIS          
SEQRES  24 D  724  GLU PHE GLN ASN LEU HIS ALA LEU LYS LYS GLU LYS ILE          
SEQRES  25 D  724  ASN ASP PHE VAL ARG GLY HIS PHE HIS GLY CYS PHE ASP          
SEQRES  26 D  724  PHE ASP LEU ASP ASN THR LEU TYR PHE PHE ILE ALA GLY          
SEQRES  27 D  724  ARG TYR GLU TYR LYS ASN LYS GLY ALA ASP MET PHE ILE          
SEQRES  28 D  724  GLU ALA LEU ALA ARG LEU ASN TYR ARG LEU LYS VAL SER          
SEQRES  29 D  724  GLY SER LYS LYS THR VAL VAL ALA PHE ILE VAL MET PRO          
SEQRES  30 D  724  ALA LYS ASN ASN SER PHE THR VAL GLU ALA LEU LYS GLY          
SEQRES  31 D  724  GLN ALA GLU VAL ARG ALA LEU GLU ASN THR VAL HIS GLU          
SEQRES  32 D  724  VAL THR THR SER ILE GLY LYS ARG ILE PHE ASP HIS ALA          
SEQRES  33 D  724  ILE ARG TYR PRO HIS ASN GLY LEU THR THR GLU LEU PRO          
SEQRES  34 D  724  THR ASP LEU GLY GLU LEU LEU LYS SER SER ASP LYS VAL          
SEQRES  35 D  724  MET LEU LYS ARG ARG ILE LEU ALA LEU ARG ARG PRO GLU          
SEQRES  36 D  724  GLY GLN LEU PRO PRO ILE VAL THR HIS ASN MET VAL ASP          
SEQRES  37 D  724  ASP ALA ASN ASP LEU ILE LEU ASN LYS ILE ARG GLN VAL          
SEQRES  38 D  724  GLN LEU PHE ASN SER PRO SER ASP ARG VAL LYS MET ILE          
SEQRES  39 D  724  PHE HIS PRO GLU PHE LEU ASN ALA ASN ASN PRO ILE LEU          
SEQRES  40 D  724  GLY LEU ASP TYR ASP GLU PHE VAL ARG GLY CYS HIS LEU          
SEQRES  41 D  724  GLY VAL PHE PRO SER TYR TYR GLU PRO TRP GLY TYR THR          
SEQRES  42 D  724  PRO ALA GLU CYS THR VAL MET GLY VAL PRO SER ILE THR          
SEQRES  43 D  724  THR ASN VAL SER GLY PHE GLY SER TYR MET GLU ASP LEU          
SEQRES  44 D  724  ILE GLU THR ASN GLN ALA LYS ASP TYR GLY ILE TYR ILE          
SEQRES  45 D  724  VAL ASP ARG ARG PHE LYS ALA PRO ASP GLU SER VAL GLU          
SEQRES  46 D  724  GLN LEU VAL ASP TYR MET GLU GLU PHE VAL LYS LYS THR          
SEQRES  47 D  724  ARG ARG GLN ARG ILE ASN GLN ARG ASN ALA THR GLU ALA          
SEQRES  48 D  724  LEU SER ASP LEU LEU ASP TRP LYS ARG MET GLY LEU GLU          
SEQRES  49 D  724  TYR VAL LYS ALA ARG GLN LEU ALA LEU ARG ARG GLY TYR          
SEQRES  50 D  724  PRO ASP GLN PHE ARG GLU LEU VAL GLY GLU GLU LEU ASN          
SEQRES  51 D  724  ASP SER ASN MET ASP ALA LEU ALA GLY GLY LYS LYS LEU          
SEQRES  52 D  724  LYS VAL ALA ARG PRO LEU SER VAL PRO GLY SER PRO ARG          
SEQRES  53 D  724  ASP LEU ARG SER ASN SER THR VAL TYR MET THR PRO GLY          
SEQRES  54 D  724  ASP LEU GLY THR LEU GLN GLU VAL ASN ASN ALA ASP ASP          
SEQRES  55 D  724  TYR PHE SER LEU GLY VAL ASN PRO ALA ALA ASP ASP ASP          
SEQRES  56 D  724  ASP ASP GLY PRO TYR ALA ASP ASP SER                          
HET    U5P  A 801      21                                                       
HET    G6P  A 802      16                                                       
HET    PEG  B1001       7                                                       
HET    U5P  B1002      21                                                       
HET    G6P  B1003      16                                                       
HET    PEG  B1004       7                                                       
HET    U5P  C 801      21                                                       
HET    G6P  C 802      16                                                       
HET    PEG  C 803       7                                                       
HET    U5P  D 801      21                                                       
HET    G6P  D 802      16                                                       
HET    PEG  D 803       7                                                       
HETNAM     U5P URIDINE-5'-MONOPHOSPHATE                                         
HETNAM     G6P ALPHA-D-GLUCOSE-6-PHOSPHATE                                      
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
FORMUL   5  U5P    4(C9 H13 N2 O9 P)                                            
FORMUL   6  G6P    4(C6 H13 O9 P)                                               
FORMUL   7  PEG    4(C4 H10 O3)                                                 
HELIX    1   1 GLY A   23  LYS A   40  1                                  18    
HELIX    2   2 THR A   53  ASN A   56  5                                   4    
HELIX    3   3 MET A   73  ARG A   86  1                                  14    
HELIX    4   4 LEU A  108  GLY A  113  5                                   6    
HELIX    5   5 TYR A  114  VAL A  126  1                                  13    
HELIX    6   6 ASP A  134  ASP A  158  1                                  25    
HELIX    7   7 TRP A  170  GLY A  173  5                                   4    
HELIX    8   8 VAL A  174  ARG A  182  1                                   9    
HELIX    9   9 THR A  195  GLY A  205  1                                  11    
HELIX   10  10 ASP A  217  PHE A  225  1                                   9    
HELIX   11  11 ILE A  227  ALA A  241  1                                  15    
HELIX   12  12 SER A  248  LYS A  260  1                                  13    
HELIX   13  13 HIS A  280  PHE A  301  1                                  22    
HELIX   14  14 ASP A  308  ASP A  310  5                                   3    
HELIX   15  15 GLY A  327  GLY A  346  1                                  20    
HELIX   16  16 THR A  365  TYR A  400  1                                  36    
HELIX   17  17 ASP A  412  LEU A  416  5                                   5    
HELIX   18  18 LYS A  418  ALA A  431  1                                  14    
HELIX   19  19 ASP A  453  GLN A  463  1                                  11    
HELIX   20  20 ASP A  491  CYS A  499  1                                   9    
HELIX   21  21 GLY A  512  MET A  521  1                                  10    
HELIX   22  22 SER A  531  ASP A  539  1                                   9    
HELIX   23  23 GLU A  542  TYR A  549  1                                   8    
HELIX   24  24 ALA A  560  LYS A  578  1                                  19    
HELIX   25  25 THR A  579  SER A  594  1                                  16    
HELIX   26  26 ASP A  595  LEU A  597  5                                   3    
HELIX   27  27 ASP A  598  TYR A  618  1                                  21    
HELIX   28  28 TYR A  618  GLY A  627  1                                  10    
HELIX   29  29 ASN A  634  ALA A  639  1                                   6    
HELIX   30  30 GLY B   23  LYS B   40  1                                  18    
HELIX   31  31 THR B   53  ASN B   56  5                                   4    
HELIX   32  32 MET B   73  SER B   85  1                                  13    
HELIX   33  33 VAL B  111  GLY B  113  5                                   3    
HELIX   34  34 TYR B  114  VAL B  126  1                                  13    
HELIX   35  35 ASP B  134  ASP B  158  1                                  25    
HELIX   36  36 TRP B  170  GLY B  173  5                                   4    
HELIX   37  37 VAL B  174  ARG B  182  1                                   9    
HELIX   38  38 THR B  195  CYS B  202  1                                   8    
HELIX   39  39 ASP B  208  LEU B  213  1                                   6    
HELIX   40  40 GLU B  214  VAL B  216  5                                   3    
HELIX   41  41 ASP B  217  PHE B  225  1                                   9    
HELIX   42  42 ILE B  227  ALA B  241  1                                  15    
HELIX   43  43 SER B  248  LYS B  260  1                                  13    
HELIX   44  44 HIS B  280  PHE B  301  1                                  22    
HELIX   45  45 ASP B  308  ASP B  310  5                                   3    
HELIX   46  46 GLY B  327  SER B  345  1                                  19    
HELIX   47  47 THR B  365  TYR B  400  1                                  36    
HELIX   48  48 ASP B  412  LEU B  417  1                                   6    
HELIX   49  49 LYS B  418  LEU B  432  1                                  15    
HELIX   50  50 ASP B  449  ASN B  452  5                                   4    
HELIX   51  51 ASP B  453  VAL B  462  1                                  10    
HELIX   52  52 ASP B  491  CYS B  499  1                                   9    
HELIX   53  53 GLY B  512  MET B  521  1                                  10    
HELIX   54  54 SER B  531  ILE B  541  1                                  11    
HELIX   55  55 GLU B  542  TYR B  549  1                                   8    
HELIX   56  56 ALA B  560  LYS B  578  1                                  19    
HELIX   57  57 THR B  579  SER B  594  1                                  16    
HELIX   58  58 ASP B  595  LEU B  597  5                                   3    
HELIX   59  59 ASP B  598  TYR B  618  1                                  21    
HELIX   60  60 TYR B  618  LEU B  625  1                                   8    
HELIX   61  61 GLY C   23  LYS C   40  1                                  18    
HELIX   62  62 THR C   53  GLU C   57  1                                   5    
HELIX   63  63 LYS C   65  PHE C   69  5                                   5    
HELIX   64  64 ARG C   74  SER C   85  1                                  12    
HELIX   65  65 LEU C  108  GLY C  113  5                                   6    
HELIX   66  66 TYR C  114  VAL C  126  1                                  13    
HELIX   67  67 ASP C  134  ASP C  158  1                                  25    
HELIX   68  68 TRP C  170  GLY C  173  5                                   4    
HELIX   69  69 VAL C  174  ARG C  182  1                                   9    
HELIX   70  70 THR C  195  SER C  204  1                                  10    
HELIX   71  71 ASP C  217  ARG C  224  1                                   8    
HELIX   72  72 ILE C  227  ALA C  241  1                                  15    
HELIX   73  73 SER C  248  LYS C  260  1                                  13    
HELIX   74  74 HIS C  280  PHE C  301  1                                  22    
HELIX   75  75 ASP C  308  ASP C  310  5                                   3    
HELIX   76  76 GLY C  327  SER C  345  1                                  19    
HELIX   77  77 THR C  365  TYR C  400  1                                  36    
HELIX   78  78 ASP C  412  LEU C  416  5                                   5    
HELIX   79  79 LYS C  418  LEU C  432  1                                  15    
HELIX   80  80 ASP C  453  GLN C  463  1                                  11    
HELIX   81  81 ASP C  491  CYS C  499  1                                   9    
HELIX   82  82 GLY C  512  MET C  521  1                                  10    
HELIX   83  83 SER C  531  ASP C  539  1                                   9    
HELIX   84  84 ASN C  544  ASP C  548  5                                   5    
HELIX   85  85 ALA C  560  LYS C  577  1                                  18    
HELIX   86  86 THR C  579  LEU C  593  1                                  15    
HELIX   87  87 SER C  594  LEU C  597  5                                   4    
HELIX   88  88 ASP C  598  TYR C  618  1                                  21    
HELIX   89  89 TYR C  618  GLY C  627  1                                  10    
HELIX   90  90 ASN C  634  ALA C  639  1                                   6    
HELIX   91  91 GLY D   23  LYS D   40  1                                  18    
HELIX   92  92 THR D   53  GLU D   57  1                                   5    
HELIX   93  93 LYS D   65  PHE D   69  5                                   5    
HELIX   94  94 MET D   73  SER D   85  1                                  13    
HELIX   95  95 LEU D  108  GLY D  113  5                                   6    
HELIX   96  96 TYR D  114  VAL D  126  1                                  13    
HELIX   97  97 ASP D  134  ASP D  158  1                                  25    
HELIX   98  98 TRP D  170  GLY D  173  5                                   4    
HELIX   99  99 VAL D  174  ARG D  182  1                                   9    
HELIX  100 100 THR D  195  GLY D  205  1                                  11    
HELIX  101 101 ASP D  217  PHE D  225  1                                   9    
HELIX  102 102 ILE D  227  ALA D  241  1                                  15    
HELIX  103 103 SER D  248  LYS D  260  1                                  13    
HELIX  104 104 HIS D  280  PHE D  301  1                                  22    
HELIX  105 105 ASP D  308  ASP D  310  5                                   3    
HELIX  106 106 GLY D  327  SER D  345  1                                  19    
HELIX  107 107 THR D  365  TYR D  400  1                                  36    
HELIX  108 108 ASP D  412  LEU D  416  5                                   5    
HELIX  109 109 LYS D  418  ARG D  433  1                                  16    
HELIX  110 110 ASP D  453  VAL D  462  1                                  10    
HELIX  111 111 ASP D  491  CYS D  499  1                                   9    
HELIX  112 112 GLY D  512  MET D  521  1                                  10    
HELIX  113 113 SER D  531  ILE D  541  1                                  11    
HELIX  114 114 GLU D  542  TYR D  549  1                                   8    
HELIX  115 115 ALA D  560  LYS D  578  1                                  19    
HELIX  116 116 THR D  579  SER D  594  1                                  16    
HELIX  117 117 ASP D  595  LEU D  597  5                                   3    
HELIX  118 118 ASP D  598  GLY D  603  1                                   6    
HELIX  119 119 GLY D  603  TYR D  618  1                                  16    
HELIX  120 120 TYR D  618  GLY D  627  1                                  10    
SHEET    1   A 9 VAL A  58  ILE A  60  0                                        
SHEET    2   A 9 PHE A  90  TRP A  95 -1  O  ARG A  94   N  ASP A  59           
SHEET    3   A 9 LYS A 102  PHE A 106 -1  O  LEU A 105   N  VAL A  91           
SHEET    4   A 9 TYR A  43  PRO A  48  1  N  LEU A  45   O  LYS A 102           
SHEET    5   A 9 ASP A   4  THR A  13  1  N  GLU A  12   O  ILE A  46           
SHEET    6   A 9 HIS A 161  HIS A 168  1  O  HIS A 166   N  THR A  13           
SHEET    7   A 9 VAL A 187  THR A 192  1  O  VAL A 187   N  ALA A 165           
SHEET    8   A 9 VAL A 243  THR A 246  1  O  VAL A 243   N  PHE A 190           
SHEET    9   A 9 GLY A 265  ILE A 266  1  O  GLY A 265   N  THR A 246           
SHEET    1   B 6 VAL A 472  HIS A 477  0                                        
SHEET    2   B 6 THR A 350  VAL A 356  1  N  VAL A 351   O  LYS A 473           
SHEET    3   B 6 THR A 312  ALA A 318  1  N  PHE A 315   O  PHE A 354           
SHEET    4   B 6 LEU A 501  PHE A 504  1  O  VAL A 503   N  PHE A 316           
SHEET    5   B 6 SER A 525  THR A 528  1  O  ILE A 526   N  PHE A 504           
SHEET    6   B 6 ILE A 551  VAL A 554  1  O  TYR A 552   N  THR A 527           
SHEET    1   C 2 ASN A 361  PHE A 364  0                                        
SHEET    2   C 2 HIS A 445  MET A 447 -1  O  ASN A 446   N  ASN A 362           
SHEET    1   D 9 VAL B  58  ILE B  60  0                                        
SHEET    2   D 9 PHE B  90  TRP B  95 -1  O  ARG B  94   N  ASP B  59           
SHEET    3   D 9 LYS B 102  PHE B 106 -1  O  VAL B 103   N  GLY B  93           
SHEET    4   D 9 TYR B  43  GLY B  47  1  N  LEU B  45   O  ILE B 104           
SHEET    5   D 9 ASP B   4  THR B  13  1  N  GLU B  12   O  ILE B  46           
SHEET    6   D 9 HIS B 161  HIS B 168  1  O  HIS B 166   N  PHE B  11           
SHEET    7   D 9 VAL B 187  THR B 192  1  O  ILE B 189   N  ALA B 165           
SHEET    8   D 9 VAL B 243  THR B 246  1  O  THR B 245   N  THR B 192           
SHEET    9   D 9 GLY B 265  ILE B 266  1  O  GLY B 265   N  THR B 246           
SHEET    1   E 6 VAL B 472  PHE B 476  0                                        
SHEET    2   E 6 THR B 350  VAL B 356  1  N  VAL B 351   O  LYS B 473           
SHEET    3   E 6 THR B 312  ALA B 318  1  N  PHE B 315   O  PHE B 354           
SHEET    4   E 6 LEU B 501  VAL B 503  1  O  VAL B 503   N  PHE B 316           
SHEET    5   E 6 SER B 525  THR B 528  1  O  ILE B 526   N  GLY B 502           
SHEET    6   E 6 ILE B 551  VAL B 554  1  O  TYR B 552   N  THR B 527           
SHEET    1   F 2 ASN B 361  PHE B 364  0                                        
SHEET    2   F 2 HIS B 445  MET B 447 -1  O  ASN B 446   N  ASN B 362           
SHEET    1   G 8 VAL C  58  ILE C  60  0                                        
SHEET    2   G 8 PHE C  90  TRP C  95 -1  O  ARG C  94   N  ASP C  59           
SHEET    3   G 8 LYS C 102  PHE C 106 -1  O  LEU C 105   N  VAL C  91           
SHEET    4   G 8 TYR C  43  PRO C  48  1  N  LEU C  45   O  LYS C 102           
SHEET    5   G 8 ASP C   4  THR C  13  1  N  GLU C  12   O  ILE C  46           
SHEET    6   G 8 HIS C 161  HIS C 168  1  O  VAL C 164   N  PHE C  11           
SHEET    7   G 8 VAL C 187  THR C 191  1  O  THR C 191   N  PHE C 167           
SHEET    8   G 8 VAL C 243  THR C 245  1  O  THR C 245   N  PHE C 190           
SHEET    1   H 6 VAL C 472  HIS C 477  0                                        
SHEET    2   H 6 THR C 350  VAL C 356  1  N  VAL C 351   O  LYS C 473           
SHEET    3   H 6 THR C 312  ALA C 318  1  N  ILE C 317   O  VAL C 356           
SHEET    4   H 6 LEU C 501  VAL C 503  1  O  VAL C 503   N  PHE C 316           
SHEET    5   H 6 SER C 525  THR C 528  1  O  ILE C 526   N  GLY C 502           
SHEET    6   H 6 ILE C 551  VAL C 554  1  O  TYR C 552   N  THR C 527           
SHEET    1   I 2 ASN C 361  PHE C 364  0                                        
SHEET    2   I 2 HIS C 445  MET C 447 -1  O  ASN C 446   N  ASN C 362           
SHEET    1   J 9 VAL D  58  ILE D  60  0                                        
SHEET    2   J 9 PHE D  90  TRP D  95 -1  O  ARG D  94   N  ASP D  59           
SHEET    3   J 9 LYS D 102  PHE D 106 -1  O  LEU D 105   N  VAL D  91           
SHEET    4   J 9 TYR D  43  PRO D  48  1  N  LEU D  45   O  ILE D 104           
SHEET    5   J 9 ASP D   4  THR D  13  1  N  GLU D  12   O  ILE D  46           
SHEET    6   J 9 HIS D 161  HIS D 168  1  O  HIS D 166   N  PHE D  11           
SHEET    7   J 9 VAL D 187  THR D 192  1  O  THR D 191   N  PHE D 167           
SHEET    8   J 9 VAL D 243  THR D 246  1  O  VAL D 243   N  PHE D 190           
SHEET    9   J 9 GLY D 265  ILE D 266  1  O  GLY D 265   N  THR D 246           
SHEET    1   K 6 VAL D 472  PHE D 476  0                                        
SHEET    2   K 6 THR D 350  VAL D 356  1  N  ALA D 353   O  LYS D 473           
SHEET    3   K 6 THR D 312  ALA D 318  1  N  PHE D 315   O  PHE D 354           
SHEET    4   K 6 LEU D 501  VAL D 503  1  O  VAL D 503   N  PHE D 316           
SHEET    5   K 6 SER D 525  THR D 528  1  O  ILE D 526   N  GLY D 502           
SHEET    6   K 6 ILE D 551  VAL D 554  1  O  VAL D 554   N  THR D 527           
SHEET    1   L 2 ASN D 361  PHE D 364  0                                        
SHEET    2   L 2 HIS D 445  MET D 447 -1  O  ASN D 446   N  ASN D 362           
CISPEP   1 TYR A  400    PRO A  401          0        -1.30                     
CISPEP   2 TYR B  400    PRO B  401          0         9.45                     
CISPEP   3 TYR C  400    PRO C  401          0        -2.30                     
CISPEP   4 TYR D  400    PRO D  401          0         3.38                     
SITE     1 AC1  9 GLY A 319  ARG A 320  LYS A 326  PHE A 480                    
SITE     2 AC1  9 LEU A 481  TYR A 492  TYR A 513  THR A 514                    
SITE     3 AC1  9 GLU A 517                                                     
SITE     1 AC2  9 GLN A 283  HIS A 286  ALA A 287  LYS A 290                    
SITE     2 AC2  9 HIS A 500  ARG A 580  ARG A 583  ARG A 587                    
SITE     3 AC2  9 HIS D 280                                                     
SITE     1 AC3  3 LYS A 391  PHE A 394  ARG B 298                               
SITE     1 AC4  7 ARG B 320  LYS B 326  PHE B 480  LEU B 481                    
SITE     2 AC4  7 TYR B 492  THR B 514  GLU B 517                               
SITE     1 AC5  8 GLN B 283  HIS B 286  LYS B 290  HIS B 500                    
SITE     2 AC5  8 ARG B 580  ARG B 583  ARG B 587  HIS C 280                    
SITE     1 AC6  3 GLU A 379  LYS B 391  PHE B 394                               
SITE     1 AC7  9 ARG C  20  GLY C 319  ARG C 320  LYS C 326                    
SITE     2 AC7  9 PHE C 480  LEU C 481  TYR C 492  THR C 514                    
SITE     3 AC7  9 GLU C 517                                                     
SITE     1 AC8  8 HIS B 280  GLN C 283  HIS C 286  LYS C 290                    
SITE     2 AC8  8 HIS C 500  ARG C 580  ARG C 583  ARG C 587                    
SITE     1 AC9  3 LYS C 391  PHE C 394  GLU D 379                               
SITE     1 BC1  8 GLY D 319  ARG D 320  LYS D 326  PHE D 480                    
SITE     2 BC1  8 LEU D 481  TYR D 492  THR D 514  GLU D 517                    
SITE     1 BC2  8 HIS A 280  GLN D 283  HIS D 286  LYS D 290                    
SITE     2 BC2  8 HIS D 500  ARG D 580  ARG D 583  ARG D 587                    
CRYST1  193.089  204.372  206.446  90.00  90.00  90.00 I 2 2 2      32          
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      0.005179  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004893  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004844        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system