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Database: PDB
Entry: 2QLL
LinkDB: 2QLL
Original site: 2QLL 
HEADER    TRANSFERASE                             13-JUL-07   2QLL              
TITLE     HUMAN LIVER GLYCOGEN PHOSPHORYLASE- GL COMPLEX                        
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;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PROTEIN TARGETING TO GLYCOGEN - GL;                        
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: GL-CTERM (281-284);                                        
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PYGL;                                                          
SOURCE   6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL: HIGH FIVE CELLS;                             
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 OTHER_DETAILS: PEPTIDE SYNTHESIS                                     
KEYWDS    DRUG DISCOVERY, GLYCOGEN METABOLISM, PROTEIN-PROTEIN INTERACTION,     
KEYWDS   2 ALLOSTERIC ENZYME, CARBOHYDRATE METABOLISM, DISEASE MUTATION,        
KEYWDS   3 GLYCOGEN STORAGE DISEASE, GLYCOSYLTRANSFERASE, NUCLEOTIDE-BINDING,   
KEYWDS   4 PHOSPHORYLATION, PYRIDOXAL PHOSPHATE, TRANSFERASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.PAUTSCH,R.STREICHER,O.WISSDORF,N.STADLER                            
REVDAT   4   13-JUL-11 2QLL    1       VERSN                                    
REVDAT   3   24-FEB-09 2QLL    1       VERSN                                    
REVDAT   2   24-JUN-08 2QLL    1       JRNL                                     
REVDAT   1   19-FEB-08 2QLL    0                                                
JRNL        AUTH   A.PAUTSCH,N.STADLER,O.WISSDORF,E.LANGKOPF,W.MORETH,          
JRNL        AUTH 2 R.STREICHER                                                  
JRNL        TITL   MOLECULAR RECOGNITION OF THE PROTEIN PHOSPHATASE 1 GLYCOGEN  
JRNL        TITL 2 TARGETING SUBUNIT BY GLYCOGEN PHOSPHORYLASE.                 
JRNL        REF    J.BIOL.CHEM.                  V. 283  8913 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18198182                                                     
JRNL        DOI    10.1074/JBC.M706612200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.56 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT 2.1.1                                     
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,              
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.56                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 37156                          
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)  : 0.206                          
REMARK   3   R VALUE            (WORKING SET)  : 0.203                          
REMARK   3   FREE R VALUE                      : 0.276                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1769                           
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               : 9                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.56                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.71                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 97.36                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : NULL                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : NULL                     
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 5021                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.4000                   
REMARK   3   BIN FREE R VALUE                        : 0.4620                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.00                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 264                      
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            : 6565                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 154                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 57.54                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.26                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.80800                                             
REMARK   3    B22 (A**2) : -1.80800                                             
REMARK   3    B33 (A**2) : 3.61600                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : NULL                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : NULL   ; NULL   ; NULL                
REMARK   3    BOND ANGLES               : NULL   ; NULL   ; NULL                
REMARK   3    TORSION ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : NULL   ; NULL   ; NULL                
REMARK   3    ISOTROPIC THERMAL FACTORS : NULL   ; NULL   ; NULL                
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : NULL   ; NULL   ; NULL                
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : NULL   ; NULL   ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : NULL                     
REMARK   3    BOND ANGLES                  (DEGREES) : NULL                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : NULL                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2QLL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB043751.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37156                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.560                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.56                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8 MG/ML PROTEIN, 0.1 M TRIS, 8% PEG      
REMARK 280  8000, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K       
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       41.89833            
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       83.79667            
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       83.79667            
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       41.89833            
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 SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED BY:  
REMARK 300 Y,X,-Z+1                                                             
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: 2215 ANGSTROM**2                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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      125.69500            
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     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     GLU A   162                                                      
REMARK 465     TYR A   163                                                      
REMARK 465     GLY A   164                                                      
REMARK 465     ILE A   165                                                      
REMARK 465     ASP A   251                                                      
REMARK 465     PHE A   252                                                      
REMARK 465     ASN A   253                                                      
REMARK 465     LEU A   254                                                      
REMARK 465     ARG A   255                                                      
REMARK 465     ASP A   256                                                      
REMARK 465     PHE A   257                                                      
REMARK 465     ASN A   258                                                      
REMARK 465     VAL A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     ASP A   261                                                      
REMARK 465     TYR A   262                                                      
REMARK 465     ILE A   263                                                      
REMARK 465     GLN A   264                                                      
REMARK 465     ALA A   265                                                      
REMARK 465     ASN A   282                                                      
REMARK 465     ASP A   283                                                      
REMARK 465     ASN A   284                                                      
REMARK 465     PHE A   285                                                      
REMARK 465     GLY A   317                                                      
REMARK 465     SER A   318                                                      
REMARK 465     THR A   319                                                      
REMARK 465     ARG A   320                                                      
REMARK 465     GLY A   321                                                      
REMARK 465     ALA A   322                                                      
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     SER A 837    OG                                                  
REMARK 470     ASN A 838    CG   OD1                                            
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    PRO A 199   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    PRO A 342   C   -  N   -  CA  ANGL. DEV. = -11.3 DEGREES          
REMARK 500    PRO A 381   C   -  N   -  CA  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    PRO A 381   C   -  N   -  CD  ANGL. DEV. = -35.6 DEGREES          
REMARK 500    PRO A 419   C   -  N   -  CA  ANGL. DEV. =  11.5 DEGREES          
REMARK 500    PRO A 419   C   -  N   -  CD  ANGL. DEV. = -16.1 DEGREES          
REMARK 500    PRO A 476   C   -  N   -  CA  ANGL. DEV. =  10.8 DEGREES          
REMARK 500    PRO A 476   C   -  N   -  CD  ANGL. DEV. = -24.8 DEGREES          
REMARK 500    PRO A 488   C   -  N   -  CA  ANGL. DEV. =  12.3 DEGREES          
REMARK 500    PRO A 488   C   -  N   -  CD  ANGL. DEV. = -14.5 DEGREES          
REMARK 500    PRO A 559   C   -  N   -  CD  ANGL. DEV. = -16.4 DEGREES          
REMARK 500    PRO A 594   C   -  N   -  CA  ANGL. DEV. =  11.8 DEGREES          
REMARK 500    PRO A 634   C   -  N   -  CA  ANGL. DEV. =  14.3 DEGREES          
REMARK 500    PRO A 634   C   -  N   -  CD  ANGL. DEV. = -18.4 DEGREES          
REMARK 500    PRO A 736   C   -  N   -  CD  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    PRO A 829   C   -  N   -  CD  ANGL. DEV. = -14.0 DEGREES          
REMARK 500    PRO B 282   C   -  N   -  CD  ANGL. DEV. = -14.8 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    THR A   5      114.97     72.70                                   
REMARK 500    ASP A   6     -138.59   -112.84                                   
REMARK 500    GLN A   7       42.94    -76.58                                   
REMARK 500    GLU A  22       46.66   -107.08                                   
REMARK 500    LEU A  95      -79.45    -42.90                                   
REMARK 500    ASN A 133       -3.78   -148.05                                   
REMARK 500    ARG A 171      112.10   -160.23                                   
REMARK 500    ASP A 172       37.59     72.33                                   
REMARK 500    GLU A 177      154.01    -49.43                                   
REMARK 500    ARG A 193       60.21   -113.92                                   
REMARK 500    MET A 197      156.21    -44.56                                   
REMARK 500    TYR A 203     -138.17     58.09                                   
REMARK 500    THR A 211       64.47   -107.42                                   
REMARK 500    PRO A 249      -72.34    -50.85                                   
REMARK 500    LEU A 267        4.91     54.76                                   
REMARK 500    ARG A 269       20.49    -62.33                                   
REMARK 500    ASN A 270      -17.49   -142.74                                   
REMARK 500    ARG A 277      -20.50   -149.19                                   
REMARK 500    ASP A 339     -179.66     69.72                                   
REMARK 500    PRO A 342       44.61   -108.73                                   
REMARK 500    THR A 368      -71.87    -57.62                                   
REMARK 500    LEU A 380      156.81    -37.97                                   
REMARK 500    GLU A 382       63.66   -112.68                                   
REMARK 500    ALA A 383        5.17   -173.85                                   
REMARK 500    ASP A 421       81.29    -35.16                                   
REMARK 500    LEU A 425      -96.30    -49.19                                   
REMARK 500    ARG A 426      -19.76    -38.82                                   
REMARK 500    ARG A 427      -72.14    -71.32                                   
REMARK 500    MET A 428        1.58    -61.26                                   
REMARK 500    GLU A 434     -131.36   -154.41                                   
REMARK 500    LYS A 437      135.68    -21.78                                   
REMARK 500    LYS A 466      -77.15   -114.57                                   
REMARK 500    LEU A 474      -79.25    -66.34                                   
REMARK 500    GLU A 475       69.38   -105.97                                   
REMARK 500    ARG A 489      -70.46    -86.58                                   
REMARK 500    LEU A 492      -64.32   -162.70                                   
REMARK 500    ASN A 496       57.35   -113.18                                   
REMARK 500    GLU A 509       43.61   -105.49                                   
REMARK 500    ASP A 514       83.02   -153.32                                   
REMARK 500    LYS A 520      -15.13    -43.77                                   
REMARK 500    SER A 523        3.81    -59.77                                   
REMARK 500    ASP A 527       81.32    -42.95                                   
REMARK 500    LYS A 554       76.93     44.87                                   
REMARK 500    VAL A 567       78.68   -119.93                                   
REMARK 500    ARG A 575     -100.98     71.91                                   
REMARK 500    GLN A 576      -48.63     58.13                                   
REMARK 500    ASP A 593       67.00    166.79                                   
REMARK 500    PRO A 594       66.62    -64.48                                   
REMARK 500    LYS A 595        5.75    176.96                                   
REMARK 500    LEU A 597      104.97    -42.70                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      80 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    MET A  91        22.4      L          L   OUTSIDE RANGE           
REMARK 500    ILE A 657        24.9      L          L   OUTSIDE RANGE           
REMARK 500    THR A 660        24.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1050        DISTANCE =  8.41 ANGSTROMS                       
REMARK 525    HOH A1054        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH A1082        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH A1126        DISTANCE =  6.53 ANGSTROMS                       
REMARK 525    HOH A1148        DISTANCE =  6.58 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PLP A  999                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
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: 1FA9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1FC0   RELATED DB: PDB                                   
DBREF  2QLL A    0   846  UNP    P06737   PYGL_HUMAN       1    847             
DBREF  2QLL B  281   284  PDB    2QLL     2QLL           281    284             
SEQADV 2QLL SEP A   14  UNP  P06737    SER    15 MODIFIED RESIDUE               
SEQRES   1 A  847  MET ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG GLN          
SEQRES   2 A  847  ILE SEP ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL ALA          
SEQRES   3 A  847  GLU LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE THR          
SEQRES   4 A  847  LEU VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP TYR          
SEQRES   5 A  847  TYR PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL          
SEQRES   6 A  847  GLY ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP LYS          
SEQRES   7 A  847  CYS PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE TYR          
SEQRES   8 A  847  MET GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU GLY          
SEQRES   9 A  847  LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU GLY          
SEQRES  10 A  847  LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA          
SEQRES  11 A  847  GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS          
SEQRES  12 A  847  PHE LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR          
SEQRES  13 A  847  GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN GLN          
SEQRES  14 A  847  LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP ASP          
SEQRES  15 A  847  TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG PRO          
SEQRES  16 A  847  GLU PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL GLU          
SEQRES  17 A  847  HIS THR ASN THR GLY THR LYS TRP ILE ASP THR GLN VAL          
SEQRES  18 A  847  VAL LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY TYR          
SEQRES  19 A  847  MET ASN ASN THR VAL ASN THR MET ARG LEU TRP SER ALA          
SEQRES  20 A  847  ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN VAL          
SEQRES  21 A  847  GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA          
SEQRES  22 A  847  GLU ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE          
SEQRES  23 A  847  PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE          
SEQRES  24 A  847  VAL VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE          
SEQRES  25 A  847  LYS ALA SER LYS PHE GLY SER THR ARG GLY ALA GLY THR          
SEQRES  26 A  847  VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN LEU          
SEQRES  27 A  847  ASN ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU MET          
SEQRES  28 A  847  ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER LYS          
SEQRES  29 A  847  ALA TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR ASN          
SEQRES  30 A  847  HIS THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL          
SEQRES  31 A  847  ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU ILE          
SEQRES  32 A  847  ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE VAL          
SEQRES  33 A  847  ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG MET          
SEQRES  34 A  847  SER LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN MET          
SEQRES  35 A  847  ALA HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN GLY          
SEQRES  36 A  847  VAL ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS VAL          
SEQRES  37 A  847  PHE LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE GLN          
SEQRES  38 A  847  ASN LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU LEU          
SEQRES  39 A  847  LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU LYS          
SEQRES  40 A  847  ILE GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU THR          
SEQRES  41 A  847  LYS LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU ARG          
SEQRES  42 A  847  GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE          
SEQRES  43 A  847  SER GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE ASN          
SEQRES  44 A  847  PRO SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE HIS          
SEQRES  45 A  847  GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE          
SEQRES  46 A  847  THR MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS LEU          
SEQRES  47 A  847  PHE VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA ALA          
SEQRES  48 A  847  PRO GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE          
SEQRES  49 A  847  THR SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET VAL          
SEQRES  50 A  847  GLY SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR ARG          
SEQRES  51 A  847  VAL SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP LEU          
SEQRES  52 A  847  SER GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY          
SEQRES  53 A  847  THR GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR          
SEQRES  54 A  847  ILE GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU          
SEQRES  55 A  847  GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET ARG          
SEQRES  56 A  847  ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR GLU          
SEQRES  57 A  847  ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS LEU          
SEQRES  58 A  847  VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO LYS          
SEQRES  59 A  847  GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU PHE          
SEQRES  60 A  847  TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU ALA          
SEQRES  61 A  847  TYR VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR MET          
SEQRES  62 A  847  ASN PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN ILE          
SEQRES  63 A  847  ALA ALA SER GLY LYS PHE SER SER ASP ARG THR ILE LYS          
SEQRES  64 A  847  GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER ASP          
SEQRES  65 A  847  LEU LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL ASN          
SEQRES  66 A  847  GLY ASN                                                      
SEQRES   1 B    4  GLY PRO TYR TYR                                              
MODRES 2QLL SEP A   14  SER  PHOSPHOSERINE                                      
HET    SEP  A  14      10                                                       
HET    PLP  A 999      15                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   3  PLP    C8 H10 N O6 P                                                
FORMUL   4  HOH   *154(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 PRO A  194  MET A  197  5                                   4    
HELIX    9   9 ALA A  272  ARG A  277  5                                   6    
HELIX   10  10 PHE A  286  ALA A  313  1                                  28    
HELIX   11  11 THR A  324  ASP A  331  5                                   8    
HELIX   12  12 LEU A  344  ILE A  356  1                                  13    
HELIX   13  13 PRO A  360  THR A  371  1                                  12    
HELIX   14  14 VAL A  389  LEU A  396  1                                   8    
HELIX   15  15 LEU A  396  PHE A  418  1                                  23    
HELIX   16  16 ASP A  421  SER A  429  1                                   9    
HELIX   17  17 MET A  441  GLY A  448  1                                   8    
HELIX   18  18 ALA A  456  LYS A  466  1                                  11    
HELIX   19  19 PHE A  468  GLU A  475  1                                   8    
HELIX   20  20 ASN A  496  GLY A  508  1                                  13    
HELIX   21  21 ASP A  514  LEU A  525  5                                  12    
HELIX   22  22 ASP A  527  LYS A  554  1                                  28    
HELIX   23  23 GLN A  576  ARG A  589  1                                  14    
HELIX   24  24 TYR A  613  ASP A  633  1                                  21    
HELIX   25  25 ARG A  649  ILE A  657  1                                   9    
HELIX   26  26 PRO A  658  THR A  660  5                                   3    
HELIX   27  27 GLY A  675  ASN A  684  1                                  10    
HELIX   28  28 ASP A  693  GLY A  704  1                                  12    
HELIX   29  29 GLU A  705  LEU A  708  5                                   4    
HELIX   30  30 ARG A  714  ASP A  722  1                                   9    
HELIX   31  31 ALA A  728  LEU A  735  1                                   8    
HELIX   32  32 LEU A  735  ASN A  747  1                                  13    
HELIX   33  33 ILE A  762  TYR A  767  1                                   6    
HELIX   34  34 LYS A  772  ASN A  793  1                                  22    
HELIX   35  35 ASN A  793  ALA A  806  1                                  14    
HELIX   36  36 ALA A  807  PHE A  811  5                                   5    
HELIX   37  37 SER A  812  ILE A  824  1                                  13    
SHEET    1   A 3 LYS A 191  SER A 192  0                                        
SHEET    2   A 3 GLN A 219  PRO A 231 -1  O  ASP A 227   N  LYS A 191           
SHEET    3   A 3 LEU A 198  PHE A 202 -1  N  VAL A 200   O  VAL A 221           
SHEET    1   B 9 LYS A 191  SER A 192  0                                        
SHEET    2   B 9 GLN A 219  PRO A 231 -1  O  ASP A 227   N  LYS A 191           
SHEET    3   B 9 VAL A 238  ARG A 247 -1  O  LEU A 243   N  TYR A 226           
SHEET    4   B 9 ALA A 154  ILE A 159  1  N  GLY A 156   O  ARG A 242           
SHEET    5   B 9 ARG A  81  LEU A  85  1  N  TYR A  84   O  TYR A 157           
SHEET    6   B 9 VAL A 333  ASN A 338  1  O  GLN A 336   N  TYR A  83           
SHEET    7   B 9 PHE A 372  THR A 375  1  O  THR A 375   N  LEU A 337           
SHEET    8   B 9 ALA A 451  GLY A 454  1  O  ALA A 451   N  TYR A 374           
SHEET    9   B 9 PHE A 479  ASN A 481  1  O  GLN A 480   N  GLY A 454           
SHEET    1   C 2 LYS A 169  ARG A 171  0                                        
SHEET    2   C 2 TRP A 174  VAL A 176 -1  O  VAL A 176   N  LYS A 169           
SHEET    1   D 2 LYS A 205  GLU A 207  0                                        
SHEET    2   D 2 LYS A 214  ILE A 216 -1  O  ILE A 216   N  LYS A 205           
SHEET    1   E 3 ARG A 386  PRO A 388  0                                        
SHEET    2   E 3 ARG A 438  ASN A 440 -1  O  ILE A 439   N  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  N  VAL A 603   O  LYS A 641           
SHEET    3   F 6 MET A 562  VAL A 567  1  N  GLN A 566   O  ILE A 604           
SHEET    4   F 6 LEU A 662  GLN A 665  1  O  GLU A 664   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  O  PHE A 709   N  THR A 688           
LINK         C   ILE A  13                 N   SEP A  14     1555   1555  1.34  
LINK         C   SEP A  14                 N   ILE A  15     1555   1555  1.34  
SITE     1 AC1  9 TYR A  90  GLY A 135  LYS A 568  LYS A 574                    
SITE     2 AC1  9 ARG A 649  VAL A 650  THR A 676  GLY A 677                    
SITE     3 AC1  9 LYS A 680                                                     
CRYST1  123.986  123.986  125.695  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      0.008065  0.004657  0.000000        0.00000                         
SCALE2      0.000000  0.009313  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007956        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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