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Database: PDB
Entry: 1FA9
LinkDB: 1FA9
Original site: 1FA9 
HEADER    TRANSFERASE                             12-JUL-00   1FA9              
TITLE     HUMAN LIVER GLYCOGEN PHOSPHORYLASE A COMPLEXED WITH AMP               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCOGEN PHOSPHORYLASE, LIVER FORM;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.4.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: LIVER;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PKK2332                                   
KEYWDS    PROTEIN-LIGAND COMPLEX, ALLOSTERIC PROTEIN, PHOSPHORYLATED PROTEIN,   
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.L.RATH,M.AMMIRATI,P.K.LEMOTTE,K.F.FENNELL,M.N.MANSOUR,D.E.DANLEY,   
AUTHOR   2 T.R.HYNES,G.K.SCHULTE,D.J.WASILKO,J.PANDIT                           
REVDAT   4   13-JUL-11 1FA9    1       VERSN                                    
REVDAT   3   24-FEB-09 1FA9    1       VERSN                                    
REVDAT   2   01-APR-03 1FA9    1       JRNL                                     
REVDAT   1   25-AUG-00 1FA9    0                                                
JRNL        AUTH   V.L.RATH,M.AMMIRATI,P.K.LEMOTTE,K.F.FENNELL,M.N.MANSOUR,     
JRNL        AUTH 2 D.E.DANLEY,T.R.HYNES,G.K.SCHULTE,D.J.WASILKO,J.PANDIT        
JRNL        TITL   ACTIVATION OF HUMAN LIVER GLYCOGEN PHOSPHORYLASE BY          
JRNL        TITL 2 ALTERATION OF THE SECONDARY STRUCTURE AND PACKING OF THE     
JRNL        TITL 3 CATALYTIC CORE.                                              
JRNL        REF    MOL.CELL                      V.   6   139 2000              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   10949035                                                     
JRNL        DOI    10.1016/S1097-2765(00)00015-0                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 43732                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : X-PLOR                          
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.295                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4101                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.42                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3530                       
REMARK   3   BIN FREE R VALUE                    : 0.4760                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6750                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 242                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1FA9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011436.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUL-94                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43732                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -2.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 9.000                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49500                            
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: X-PLOR                                                
REMARK 200 STARTING MODEL: 1GPA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, TRIS/HCL, AMP, GLUCOSE, PH     
REMARK 280  8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 25K                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.56000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       85.12000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       85.12000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       42.56000            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER CONSTRUCTED FROM CHAIN A  
REMARK 300 A SYMMETRY PARTNER GENERATED BY THE TWO-FOLD.                        
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 10080 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 61620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      127.68000            
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     ALA A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     GLU A   839                                                      
REMARK 465     SER A   840                                                      
REMARK 465     ASN A   841                                                      
REMARK 465     LYS A   842                                                      
REMARK 465     VAL A   843                                                      
REMARK 465     ASN A   844                                                      
REMARK 465     GLY A   845                                                      
REMARK 465     ASN A   846                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     THR A   5    OG1  CG2                                            
REMARK 470     SER A 837    OG                                                  
REMARK 470     ASN A 838    CG   OD1                                            
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   O    SER A   318     N    THR A   319              1.41            
REMARK 500   O    SER A   318     OG1  THR A   319              1.56            
REMARK 500   CA   GLY A   321     N    ALA A   322              1.63            
REMARK 500   N    GLY A   321     N    ALA A   322              1.75            
REMARK 500   NH1  ARG A   320     CA   GLY A   323              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CG2  THR A   319     CD2  LEU A   543     5665     1.53            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    THR A 319   C     ARG A 320   N      -0.173                       
REMARK 500    GLY A 321   N     GLY A 321   CA     -0.101                       
REMARK 500    ARG A 320   C     GLY A 321   N      -0.145                       
REMARK 500    GLY A 321   C     ALA A 322   N      -0.586                       
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    THR A 319   CA  -  C   -  N   ANGL. DEV. = -16.6 DEGREES          
REMARK 500    THR A 319   O   -  C   -  N   ANGL. DEV. =  15.3 DEGREES          
REMARK 500    GLY A 321   N   -  CA  -  C   ANGL. DEV. = -25.8 DEGREES          
REMARK 500    ARG A 320   CA  -  C   -  N   ANGL. DEV. = -19.0 DEGREES          
REMARK 500    ARG A 320   O   -  C   -  N   ANGL. DEV. =  18.4 DEGREES          
REMARK 500    GLY A 321   C   -  N   -  CA  ANGL. DEV. =  12.7 DEGREES          
REMARK 500    GLY A 321   CA  -  C   -  N   ANGL. DEV. = -30.2 DEGREES          
REMARK 500    GLY A 321   O   -  C   -  N   ANGL. DEV. =  24.3 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    ASP A   6     -103.71   -153.05                                   
REMARK 500    GLN A   7      179.79     77.69                                   
REMARK 500    ILE A  18       23.61    -76.78                                   
REMARK 500    LEU A  95      -72.15    -50.19                                   
REMARK 500    PHE A 166      159.44    159.59                                   
REMARK 500    TYR A 203     -140.74     57.27                                   
REMARK 500    MET A 234       28.41     45.97                                   
REMARK 500    ASN A 282      108.90    -49.16                                   
REMARK 500    ASN A 284        6.34    -64.99                                   
REMARK 500    ASP A 339     -166.49     74.50                                   
REMARK 500    LEU A 417      -18.38   -159.34                                   
REMARK 500    SER A 436      114.59    139.70                                   
REMARK 500    LYS A 466      -79.07    -75.54                                   
REMARK 500    ASP A 477       -9.75    -59.62                                   
REMARK 500    LEU A 492      -69.46   -142.21                                   
REMARK 500    PHE A 563       77.78     79.23                                   
REMARK 500    LYS A 568      172.46    178.67                                   
REMARK 500    ARG A 575     -101.76     74.71                                   
REMARK 500    GLN A 576      -15.42     55.71                                   
REMARK 500    ASP A 593      133.95    168.58                                   
REMARK 500    PRO A 594     -157.78    -65.03                                   
REMARK 500    LYS A 595      -37.23     68.62                                   
REMARK 500    SER A 638       39.14    -68.54                                   
REMARK 500    GLN A 665       55.08   -118.86                                   
REMARK 500    ILE A 666       37.99    -91.86                                   
REMARK 500    SER A 674     -159.31   -133.78                                   
REMARK 500    ASP A 722       34.98    -82.65                                   
REMARK 500    LYS A 723      -18.33   -142.69                                   
REMARK 500    LYS A 724      -61.30   -106.27                                   
REMARK 500    PRO A 736      -70.77    -64.21                                   
REMARK 500    PHE A 766      -93.21    -78.34                                   
REMARK 500    HIS A 768       22.14   -141.57                                   
REMARK 500    ASP A 769     -175.08    -64.92                                   
REMARK 500    ARG A 770      -21.33   -163.78                                   
REMARK 500    LYS A 772       72.38     49.44                                   
REMARK 500    ILE A 824      -52.03   -122.36                                   
REMARK 500    SER A 837       73.60   -110.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ARG A 320         10.13                                           
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 GLC A 998                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP A 997                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 999                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FC0   RELATED DB: PDB                                   
REMARK 900 1FC0 CONTAINS THE SAME PROTEIN COMPLEXED WITH N-ACETYL-BETA          
REMARK 900 -D-GLUCOPYRANOSYLAMINE                                               
DBREF  1FA9 A    1   846  UNP    P06737   PHS1_HUMAN       2    847             
SEQADV 1FA9 SEP A   14  UNP  P06737    SER    15 MODIFIED RESIDUE               
SEQRES   1 A  846  ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG GLN ILE          
SEQRES   2 A  846  SEP ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL ALA GLU          
SEQRES   3 A  846  LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE THR LEU          
SEQRES   4 A  846  VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP TYR TYR          
SEQRES   5 A  846  PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL GLY          
SEQRES   6 A  846  ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP LYS CYS          
SEQRES   7 A  846  PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE TYR MET          
SEQRES   8 A  846  GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU GLY LEU          
SEQRES   9 A  846  GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU GLY LEU          
SEQRES  10 A  846  ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA GLY          
SEQRES  11 A  846  LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS PHE          
SEQRES  12 A  846  LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR GLY          
SEQRES  13 A  846  TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN GLN LYS          
SEQRES  14 A  846  ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP ASP TRP          
SEQRES  15 A  846  LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG PRO GLU          
SEQRES  16 A  846  PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL GLU HIS          
SEQRES  17 A  846  THR ASN THR GLY THR LYS TRP ILE ASP THR GLN VAL VAL          
SEQRES  18 A  846  LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY TYR MET          
SEQRES  19 A  846  ASN ASN THR VAL ASN THR MET ARG LEU TRP SER ALA ARG          
SEQRES  20 A  846  ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN VAL GLY          
SEQRES  21 A  846  ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA GLU          
SEQRES  22 A  846  ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE PHE          
SEQRES  23 A  846  GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE VAL          
SEQRES  24 A  846  VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE LYS          
SEQRES  25 A  846  ALA SER LYS PHE GLY SER THR ARG GLY ALA GLY THR VAL          
SEQRES  26 A  846  PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN LEU ASN          
SEQRES  27 A  846  ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU MET ARG          
SEQRES  28 A  846  ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER LYS ALA          
SEQRES  29 A  846  TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR ASN HIS          
SEQRES  30 A  846  THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL ASP          
SEQRES  31 A  846  LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU ILE ILE          
SEQRES  32 A  846  TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE VAL ALA          
SEQRES  33 A  846  LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG MET SER          
SEQRES  34 A  846  LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN MET ALA          
SEQRES  35 A  846  HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN GLY VAL          
SEQRES  36 A  846  ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS VAL PHE          
SEQRES  37 A  846  LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE GLN ASN          
SEQRES  38 A  846  LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU LEU LEU          
SEQRES  39 A  846  CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU LYS ILE          
SEQRES  40 A  846  GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU THR LYS          
SEQRES  41 A  846  LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU ARG GLU          
SEQRES  42 A  846  LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE SER          
SEQRES  43 A  846  GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE ASN PRO          
SEQRES  44 A  846  SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE HIS GLU          
SEQRES  45 A  846  TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE THR          
SEQRES  46 A  846  MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS LEU PHE          
SEQRES  47 A  846  VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA ALA PRO          
SEQRES  48 A  846  GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE THR          
SEQRES  49 A  846  SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET VAL GLY          
SEQRES  50 A  846  SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR ARG VAL          
SEQRES  51 A  846  SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP LEU SER          
SEQRES  52 A  846  GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY THR          
SEQRES  53 A  846  GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR ILE          
SEQRES  54 A  846  GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU GLU          
SEQRES  55 A  846  ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET ARG ILE          
SEQRES  56 A  846  ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR GLU ALA          
SEQRES  57 A  846  LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS LEU VAL          
SEQRES  58 A  846  ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO LYS GLN          
SEQRES  59 A  846  PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU PHE TYR          
SEQRES  60 A  846  HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU ALA TYR          
SEQRES  61 A  846  VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR MET ASN          
SEQRES  62 A  846  PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN ILE ALA          
SEQRES  63 A  846  ALA SER GLY LYS PHE SER SER ASP ARG THR ILE LYS GLU          
SEQRES  64 A  846  TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER ASP LEU          
SEQRES  65 A  846  LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL ASN GLY          
SEQRES  66 A  846  ASN                                                          
MODRES 1FA9 SEP A   14  SER  PHOSPHOSERINE                                      
HET    SEP  A  14      10                                                       
HET    GLC  A 998      12                                                       
HET    AMP  A 997      23                                                       
HET    PLP  A 999      15                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   2  GLC    C6 H12 O6                                                    
FORMUL   3  AMP    C10 H14 N5 O7 P                                              
FORMUL   4  PLP    C8 H10 N O6 P                                                
FORMUL   5  HOH   *242(H2 O)                                                    
HELIX    1   1 LYS A    9  ILE A   13  5                                   5    
HELIX    2   2 ASN A   23  PHE A   37  1                                  15    
HELIX    3   3 THR A   47  CYS A   78  1                                  32    
HELIX    4   4 THR A   94  LEU A  102  1                                   9    
HELIX    5   5 LEU A  104  LEU A  115  1                                  12    
HELIX    6   6 ASP A  118  GLU A  124  1                                   7    
HELIX    7   7 GLY A  134  LEU A  150  1                                  17    
HELIX    8   8 ASN A  253  GLY A  260  1                                   8    
HELIX    9   9 ILE A  263  ALA A  265  5                                   3    
HELIX   10  10 VAL A  266  ILE A  275  1                                  10    
HELIX   11  11 PHE A  285  SER A  314  1                                  30    
HELIX   12  12 ALA A  328  GLN A  332  1                                   5    
HELIX   13  13 LEU A  344  ILE A  356  1                                  13    
HELIX   14  14 PRO A  360  THR A  371  1                                  12    
HELIX   15  15 LEU A  380  LEU A  384  5                                   5    
HELIX   16  16 VAL A  389  LEU A  396  1                                   8    
HELIX   17  17 LEU A  396  VAL A  415  1                                  20    
HELIX   18  18 ASP A  421  SER A  429  1                                   9    
HELIX   19  19 MET A  441  SER A  449  1                                   9    
HELIX   20  20 ALA A  456  LYS A  466  1                                  11    
HELIX   21  21 PHE A  468  GLU A  473  1                                   6    
HELIX   22  22 GLU A  475  ASP A  477  5                                   3    
HELIX   23  23 ASN A  496  GLY A  508  1                                  13    
HELIX   24  24 ASP A  514  LEU A  525  5                                  12    
HELIX   25  25 ASP A  527  LYS A  554  1                                  28    
HELIX   26  26 GLN A  576  ASP A  593  1                                  18    
HELIX   27  27 TYR A  613  ASP A  633  1                                  21    
HELIX   28  28 ARG A  649  ILE A  657  1                                   9    
HELIX   29  29 PRO A  658  THR A  660  5                                   3    
HELIX   30  30 GLY A  675  GLY A  685  1                                  11    
HELIX   31  31 GLY A  694  GLY A  704  1                                  11    
HELIX   32  32 GLU A  705  LEU A  708  5                                   4    
HELIX   33  33 ARG A  714  ASP A  722  1                                   9    
HELIX   34  34 ALA A  728  LEU A  735  1                                   8    
HELIX   35  35 LEU A  735  GLY A  748  1                                  14    
HELIX   36  36 GLN A  754  LEU A  757  5                                   4    
HELIX   37  37 PHE A  758  PHE A  766  1                                   9    
HELIX   38  38 LYS A  772  MET A  792  1                                  21    
HELIX   39  39 ASN A  793  ALA A  806  1                                  14    
HELIX   40  40 ALA A  807  PHE A  811  5                                   5    
HELIX   41  41 SER A  812  ILE A  824  1                                  13    
SHEET    1   A 9 PHE A 479  ASN A 481  0                                        
SHEET    2   A 9 ALA A 451  GLY A 454  1  O  VAL A 452   N  GLN A 480           
SHEET    3   A 9 PHE A 372  THR A 375  1  O  PHE A 372   N  ALA A 451           
SHEET    4   A 9 VAL A 333  ASN A 338  1  O  ILE A 335   N  ALA A 373           
SHEET    5   A 9 ARG A  81  LEU A  85  1  O  ARG A  81   N  ALA A 334           
SHEET    6   A 9 ALA A 154  ILE A 159  1  O  TYR A 155   N  TYR A  84           
SHEET    7   A 9 VAL A 238  ARG A 247  1  O  THR A 240   N  GLY A 156           
SHEET    8   A 9 GLN A 219  PRO A 231 -1  N  LEU A 222   O  ARG A 247           
SHEET    9   A 9 LYS A 191  SER A 192 -1  O  LYS A 191   N  ASP A 227           
SHEET    1   B 9 PHE A 479  ASN A 481  0                                        
SHEET    2   B 9 ALA A 451  GLY A 454  1  O  VAL A 452   N  GLN A 480           
SHEET    3   B 9 PHE A 372  THR A 375  1  O  PHE A 372   N  ALA A 451           
SHEET    4   B 9 VAL A 333  ASN A 338  1  O  ILE A 335   N  ALA A 373           
SHEET    5   B 9 ARG A  81  LEU A  85  1  O  ARG A  81   N  ALA A 334           
SHEET    6   B 9 ALA A 154  ILE A 159  1  O  TYR A 155   N  TYR A  84           
SHEET    7   B 9 VAL A 238  ARG A 247  1  O  THR A 240   N  GLY A 156           
SHEET    8   B 9 GLN A 219  PRO A 231 -1  N  LEU A 222   O  ARG A 247           
SHEET    9   B 9 LEU A 198  PHE A 202 -1  O  LEU A 198   N  ALA A 223           
SHEET    1   C 2 ASN A 167  ARG A 171  0                                        
SHEET    2   C 2 TRP A 174  GLU A 178 -1  O  TRP A 174   N  ARG A 171           
SHEET    1   D 2 LYS A 205  THR A 209  0                                        
SHEET    2   D 2 GLY A 212  ILE A 216 -1  O  GLY A 212   N  THR A 209           
SHEET    1   E 3 ARG A 386  PRO A 388  0                                        
SHEET    2   E 3 ARG A 438  ASN A 440 -1  N  ILE A 439   O  TRP A 387           
SHEET    3   E 3 ILE A 431  GLU A 432 -1  N  GLU A 432   O  ARG A 438           
SHEET    1   F 6 LEU A 640  LEU A 645  0                                        
SHEET    2   F 6 ARG A 601  GLY A 606  1  O  ARG A 601   N  LYS A 641           
SHEET    3   F 6 ASP A 564  VAL A 567  1  N  ASP A 564   O  THR A 602           
SHEET    4   F 6 LEU A 662  GLN A 665  1  O  LEU A 662   N  VAL A 565           
SHEET    5   F 6 LEU A 687  GLY A 690  1  O  LEU A 687   N  SER A 663           
SHEET    6   F 6 PHE A 709  ILE A 710  1  N  PHE A 709   O  THR A 688           
LINK         NZ  LYS A 680                 C4A PLP A 999     1555   1555  1.45  
LINK         C   ILE A  13                 N   SEP A  14     1555   1555  1.33  
LINK         C   SEP A  14                 N   ILE A  15     1555   1555  1.34  
SITE     1 AC1 10 GLY A 135  LEU A 136  HIS A 377  ASN A 484                    
SITE     2 AC1 10 SER A 674  GLY A 675  THR A 676  PLP A 999                    
SITE     3 AC1 10 HOH A2090  HOH A2192                                          
SITE     1 AC2  9 ASP A  42  ASN A  44  TRP A  67  GLN A  71                    
SITE     2 AC2  9 TYR A  75  ARG A 309  ARG A 310  HOH A2099                    
SITE     3 AC2  9 HOH A2162                                                     
SITE     1 AC3 11 GLY A 135  TRP A 491  TYR A 648  ARG A 649                    
SITE     2 AC3 11 VAL A 650  THR A 676  GLY A 677  LYS A 680                    
SITE     3 AC3 11 GLC A 998  HOH A2191  HOH A2193                               
CRYST1  123.910  123.910  127.680  90.00  90.00 120.00 P 31 2 1      6          
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      0.008070  0.004659  0.000000        0.00000                         
SCALE2      0.000000  0.009319  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007832        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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