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Database: PDB
Entry: 1FC0
LinkDB: 1FC0
Original site: 1FC0 
HEADER    TRANSFERASE                             17-JUL-00   1FC0              
TITLE     HUMAN LIVER GLYCOGEN PHOSPHORYLASE COMPLEXED WITH N-ACETYL-BETA-D-    
TITLE    2 GLUCOPYRANOSYLAMINE                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCOGEN PHOSPHORYLASE, LIVER FORM;                        
COMPND   3 CHAIN: A, B;                                                         
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: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;                               
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PBLUEBAC III                              
KEYWDS    PHOSPHORYLATED PROTEIN, ALLOSTERIC, GLUCOSE ANALOG, INHIBITOR,        
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.L.RATH,M.AMMIRATI,P.K.LEMOTTE,K.F.FENNELL,M.M.MANSOUR,D.E.DANLEY,   
AUTHOR   2 T.R.HYNES,G.K.SCHULTE,D.J.WASILKO,J.PANDIT                           
REVDAT   4   13-JUL-11 1FC0    1       VERSN                                    
REVDAT   3   24-FEB-09 1FC0    1       VERSN                                    
REVDAT   2   01-APR-03 1FC0    1       JRNL                                     
REVDAT   1   25-AUG-00 1FC0    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     : CNS 0.5                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 549432.890                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 78076                          
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 SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 7804                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 10520                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2680                       
REMARK   3   BIN FREE R VALUE                    : 0.2830                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.10                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1183                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.008                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12854                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 255                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.72000                                             
REMARK   3    B22 (A**2) : -2.72000                                             
REMARK   3    B33 (A**2) : 5.43000                                              
REMARK   3    B12 (A**2) : 0.99000                                              
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) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.32                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.33                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.32                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.00                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.52                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.580 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.950 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.020 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.780 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 46.63                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : PLPPHO.PARAM                                   
REMARK   3  PARAMETER FILE  4  : GNC.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : PLPPHO_PATCH.TOP                               
REMARK   3  TOPOLOGY FILE  4   : GNC.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1FC0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011467.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
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) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS II                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 81720                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -2.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.5000                            
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     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17400                            
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: CNS                                                   
REMARK 200 STARTING MODEL: 1FA9                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NAMES, MPD, N-ACETYL-BETA-D-             
REMARK 280  GLYCOPYRANOSYLAMINE, PH 6.0, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 17K                                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
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                                                                      
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       40.76000            
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       81.52000            
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 RELATED BY A TWO FOLD     
REMARK 300 NCS AXIS. MONOMER 1 CONSISTS OF RESIDUES A23-A831, MONOMER 2         
REMARK 300 CONSISTS OF RESIDUES A1023-A1831.                                    
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                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 56140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     ARG A    10                                                      
REMARK 465     ARG A    11                                                      
REMARK 465     GLN A    12                                                      
REMARK 465     ILE A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     ILE A    15                                                      
REMARK 465     ARG A    16                                                      
REMARK 465     GLY A    17                                                      
REMARK 465     ILE A    18                                                      
REMARK 465     VAL A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     VAL A    21                                                      
REMARK 465     GLU A    22                                                      
REMARK 465     ASN A   250                                                      
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   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     GLY A   323                                                      
REMARK 465     LEU A   832                                                      
REMARK 465     LYS A   833                                                      
REMARK 465     ILE A   834                                                      
REMARK 465     SER A   835                                                      
REMARK 465     LEU A   836                                                      
REMARK 465     SER A   837                                                      
REMARK 465     ASN A   838                                                      
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 465     ALA B  1001                                                      
REMARK 465     LYS B  1002                                                      
REMARK 465     PRO B  1003                                                      
REMARK 465     LEU B  1004                                                      
REMARK 465     THR B  1005                                                      
REMARK 465     ASP B  1006                                                      
REMARK 465     GLN B  1007                                                      
REMARK 465     GLU B  1008                                                      
REMARK 465     LYS B  1009                                                      
REMARK 465     ARG B  1010                                                      
REMARK 465     ARG B  1011                                                      
REMARK 465     GLN B  1012                                                      
REMARK 465     ILE B  1013                                                      
REMARK 465     SER B  1014                                                      
REMARK 465     ILE B  1015                                                      
REMARK 465     ARG B  1016                                                      
REMARK 465     GLY B  1017                                                      
REMARK 465     ILE B  1018                                                      
REMARK 465     VAL B  1019                                                      
REMARK 465     GLY B  1020                                                      
REMARK 465     VAL B  1021                                                      
REMARK 465     GLU B  1022                                                      
REMARK 465     ASN B  1250                                                      
REMARK 465     ASP B  1251                                                      
REMARK 465     PHE B  1252                                                      
REMARK 465     ASN B  1253                                                      
REMARK 465     LEU B  1254                                                      
REMARK 465     ARG B  1255                                                      
REMARK 465     ASP B  1256                                                      
REMARK 465     PHE B  1257                                                      
REMARK 465     ASN B  1258                                                      
REMARK 465     VAL B  1259                                                      
REMARK 465     GLY B  1317                                                      
REMARK 465     SER B  1318                                                      
REMARK 465     THR B  1319                                                      
REMARK 465     ARG B  1320                                                      
REMARK 465     GLY B  1321                                                      
REMARK 465     ALA B  1322                                                      
REMARK 465     LEU B  1832                                                      
REMARK 465     LYS B  1833                                                      
REMARK 465     ILE B  1834                                                      
REMARK 465     SER B  1835                                                      
REMARK 465     LEU B  1836                                                      
REMARK 465     SER B  1837                                                      
REMARK 465     ASN B  1838                                                      
REMARK 465     GLU B  1839                                                      
REMARK 465     SER B  1840                                                      
REMARK 465     ASN B  1841                                                      
REMARK 465     LYS B  1842                                                      
REMARK 465     VAL B  1843                                                      
REMARK 465     ASN B  1844                                                      
REMARK 465     GLY B  1845                                                      
REMARK 465     ASN B  1846                                                      
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    CYS A  78       55.68     36.79                                   
REMARK 500    LEU A  95      -76.06    -35.29                                   
REMARK 500    ALA A 129       72.08   -101.34                                   
REMARK 500    LEU A 131       40.96    -88.74                                   
REMARK 500    PHE A 166      157.08    -46.50                                   
REMARK 500    ARG A 193       77.95   -117.98                                   
REMARK 500    TYR A 203     -131.28     69.11                                   
REMARK 500    HIS A 208       71.15   -111.03                                   
REMARK 500    MET A 234       62.84     37.59                                   
REMARK 500    ASN A 235       10.89   -152.01                                   
REMARK 500    ASN A 236       -6.78     77.85                                   
REMARK 500    PRO A 281       35.42    -75.33                                   
REMARK 500    PHE A 326        0.60    -62.73                                   
REMARK 500    ASP A 339     -177.31     70.77                                   
REMARK 500    PRO A 342       30.09    -97.48                                   
REMARK 500    LEU A 344       -9.73    -56.37                                   
REMARK 500    VAL A 379      -44.12   -143.42                                   
REMARK 500    GLU A 434      107.23    -51.39                                   
REMARK 500    LYS A 466      -82.78    -99.10                                   
REMARK 500    ASN A 484      171.08    -56.45                                   
REMARK 500    LEU A 492      -74.09   -152.11                                   
REMARK 500    LYS A 568      178.28    175.48                                   
REMARK 500    ASP A 593       65.13   -177.67                                   
REMARK 500    SER A 674      -60.02   -156.32                                   
REMARK 500    SER A 751       66.10   -156.00                                   
REMARK 500    LYS A 753        0.48    -66.37                                   
REMARK 500    GLN A 754       68.23   -156.36                                   
REMARK 500    PHE A 758       31.09    -96.63                                   
REMARK 500    HIS A 768       44.47   -142.75                                   
REMARK 500    LYS A 772       67.67     30.92                                   
REMARK 500    ILE A 824      -54.94   -125.37                                   
REMARK 500    CYS B1078       56.06     36.05                                   
REMARK 500    LEU B1095      -76.20    -36.03                                   
REMARK 500    LEU B1131       39.59    -89.40                                   
REMARK 500    PHE B1166      157.30    -46.67                                   
REMARK 500    TYR B1203     -132.19     68.73                                   
REMARK 500    THR B1209     -169.86   -109.39                                   
REMARK 500    MET B1234       62.82     37.89                                   
REMARK 500    ASN B1235       11.06   -152.60                                   
REMARK 500    ASN B1236       -7.26     78.36                                   
REMARK 500    PRO B1281       36.50    -75.54                                   
REMARK 500    SER B1314     -172.20    -65.85                                   
REMARK 500    ASP B1339     -179.03     69.78                                   
REMARK 500    LEU B1344       -9.45    -56.53                                   
REMARK 500    GLU B1434      106.52    -51.15                                   
REMARK 500    LYS B1466      -82.48    -99.13                                   
REMARK 500    ASN B1484      172.28    -57.51                                   
REMARK 500    LEU B1492      -73.03   -150.38                                   
REMARK 500    LYS B1568      179.39    175.73                                   
REMARK 500    LYS B1592        1.51    -69.97                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      59 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NBG A 861                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NBG B 1861                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 860                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 1860                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FA9   RELATED DB: PDB                                   
REMARK 900 HUMAN LIVER GLYCOGEN PHOSPHORYLASE COMPLEXED WITH AMP                
DBREF  1FC0 A    1   846  UNP    P06737   PHS1_HUMAN       2    847             
DBREF  1FC0 B 1001  1846  UNP    P06737   PHS1_HUMAN       2    847             
SEQRES   1 A  846  ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG GLN ILE          
SEQRES   2 A  846  SER 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                                                          
SEQRES   1 B  846  ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG GLN ILE          
SEQRES   2 B  846  SER ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL ALA GLU          
SEQRES   3 B  846  LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE THR LEU          
SEQRES   4 B  846  VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP TYR TYR          
SEQRES   5 B  846  PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL GLY          
SEQRES   6 B  846  ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP LYS CYS          
SEQRES   7 B  846  PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE TYR MET          
SEQRES   8 B  846  GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU GLY LEU          
SEQRES   9 B  846  GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU GLY LEU          
SEQRES  10 B  846  ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA GLY          
SEQRES  11 B  846  LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS PHE          
SEQRES  12 B  846  LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR GLY          
SEQRES  13 B  846  TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN GLN LYS          
SEQRES  14 B  846  ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP ASP TRP          
SEQRES  15 B  846  LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG PRO GLU          
SEQRES  16 B  846  PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL GLU HIS          
SEQRES  17 B  846  THR ASN THR GLY THR LYS TRP ILE ASP THR GLN VAL VAL          
SEQRES  18 B  846  LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY TYR MET          
SEQRES  19 B  846  ASN ASN THR VAL ASN THR MET ARG LEU TRP SER ALA ARG          
SEQRES  20 B  846  ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN VAL GLY          
SEQRES  21 B  846  ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA GLU          
SEQRES  22 B  846  ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE PHE          
SEQRES  23 B  846  GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE VAL          
SEQRES  24 B  846  VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE LYS          
SEQRES  25 B  846  ALA SER LYS PHE GLY SER THR ARG GLY ALA GLY THR VAL          
SEQRES  26 B  846  PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN LEU ASN          
SEQRES  27 B  846  ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU MET ARG          
SEQRES  28 B  846  ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER LYS ALA          
SEQRES  29 B  846  TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR ASN HIS          
SEQRES  30 B  846  THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL ASP          
SEQRES  31 B  846  LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU ILE ILE          
SEQRES  32 B  846  TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE VAL ALA          
SEQRES  33 B  846  LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG MET SER          
SEQRES  34 B  846  LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN MET ALA          
SEQRES  35 B  846  HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN GLY VAL          
SEQRES  36 B  846  ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS VAL PHE          
SEQRES  37 B  846  LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE GLN ASN          
SEQRES  38 B  846  LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU LEU LEU          
SEQRES  39 B  846  CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU LYS ILE          
SEQRES  40 B  846  GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU THR LYS          
SEQRES  41 B  846  LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU ARG GLU          
SEQRES  42 B  846  LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE SER          
SEQRES  43 B  846  GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE ASN PRO          
SEQRES  44 B  846  SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE HIS GLU          
SEQRES  45 B  846  TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE THR          
SEQRES  46 B  846  MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS LEU PHE          
SEQRES  47 B  846  VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA ALA PRO          
SEQRES  48 B  846  GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE THR          
SEQRES  49 B  846  SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET VAL GLY          
SEQRES  50 B  846  SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR ARG VAL          
SEQRES  51 B  846  SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP LEU SER          
SEQRES  52 B  846  GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY THR          
SEQRES  53 B  846  GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR ILE          
SEQRES  54 B  846  GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU GLU          
SEQRES  55 B  846  ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET ARG ILE          
SEQRES  56 B  846  ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR GLU ALA          
SEQRES  57 B  846  LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS LEU VAL          
SEQRES  58 B  846  ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO LYS GLN          
SEQRES  59 B  846  PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU PHE TYR          
SEQRES  60 B  846  HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU ALA TYR          
SEQRES  61 B  846  VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR MET ASN          
SEQRES  62 B  846  PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN ILE ALA          
SEQRES  63 B  846  ALA SER GLY LYS PHE SER SER ASP ARG THR ILE LYS GLU          
SEQRES  64 B  846  TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER ASP LEU          
SEQRES  65 B  846  LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL ASN GLY          
SEQRES  66 B  846  ASN                                                          
HET    NBG  A 861      15                                                       
HET    NBG  B1861      15                                                       
HET    PLP  A 860      15                                                       
HET    PLP  B1860      15                                                       
HETNAM     NBG 1-N-ACETYL-BETA-D-GLUCOSAMINE                                    
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   3  NBG    2(C8 H15 N O6)                                               
FORMUL   5  PLP    2(C8 H10 N O6 P)                                             
FORMUL   7  HOH   *255(H2 O)                                                    
HELIX    1   1 ASN A   23  THR A   38  1                                  16    
HELIX    2   2 THR A   47  CYS A   78  1                                  32    
HELIX    3   3 THR A   94  GLY A  103  1                                  10    
HELIX    4   4 LEU A  104  LEU A  115  1                                  12    
HELIX    5   5 ASP A  118  GLU A  124  1                                   7    
HELIX    6   6 GLY A  134  LEU A  150  1                                  17    
HELIX    7   7 PRO A  194  MET A  197  5                                   4    
HELIX    8   8 ASP A  261  ASP A  268  1                                   8    
HELIX    9   9 ARG A  269  ASN A  274  1                                   6    
HELIX   10  10 ILE A  275  ARG A  277  5                                   3    
HELIX   11  11 LYS A  289  LYS A  312  1                                  24    
HELIX   12  12 THR A  324  ASP A  327  5                                   4    
HELIX   13  13 ALA A  328  GLN A  332  1                                   5    
HELIX   14  14 LEU A  344  ILE A  356  1                                  13    
HELIX   15  15 PRO A  360  THR A  371  1                                  12    
HELIX   16  16 VAL A  389  LEU A  396  1                                   8    
HELIX   17  17 LEU A  396  PHE A  418  1                                  23    
HELIX   18  18 ASP A  421  SER A  429  1                                   9    
HELIX   19  19 MET A  441  GLY A  448  1                                   8    
HELIX   20  20 ALA A  456  LYS A  466  1                                  11    
HELIX   21  21 PHE A  468  GLU A  475  1                                   8    
HELIX   22  22 ASN A  496  GLY A  508  1                                  13    
HELIX   23  23 GLU A  509  LYS A  513  5                                   5    
HELIX   24  24 ASP A  514  LEU A  525  5                                  12    
HELIX   25  25 ASP A  527  TYR A  553  1                                  27    
HELIX   26  26 HIS A  571  LYS A  574  5                                   4    
HELIX   27  27 ARG A  575  LYS A  592  1                                  18    
HELIX   28  28 TYR A  613  ASP A  633  1                                  21    
HELIX   29  29 VAL A  636  SER A  638  5                                   3    
HELIX   30  30 ARG A  649  ILE A  657  1                                   9    
HELIX   31  31 PRO A  658  THR A  660  5                                   3    
HELIX   32  32 THR A  676  ASN A  684  1                                   9    
HELIX   33  33 ALA A  695  GLY A  704  1                                  10    
HELIX   34  34 GLU A  705  LEU A  708  5                                   4    
HELIX   35  35 ARG A  714  GLY A  725  1                                  12    
HELIX   36  36 GLU A  727  LEU A  735  1                                   9    
HELIX   37  37 LEU A  735  ASN A  747  1                                  13    
HELIX   38  38 PHE A  758  HIS A  768  1                                  11    
HELIX   39  39 VAL A  773  ALA A  775  5                                   3    
HELIX   40  40 ASP A  776  MET A  792  1                                  17    
HELIX   41  41 ASN A  793  ALA A  806  1                                  14    
HELIX   42  42 ALA A  807  PHE A  811  5                                   5    
HELIX   43  43 SER A  812  ILE A  824  1                                  13    
HELIX   44  44 ASN B 1023  THR B 1038  1                                  16    
HELIX   45  45 THR B 1047  CYS B 1078  1                                  32    
HELIX   46  46 THR B 1094  LEU B 1102  1                                   9    
HELIX   47  47 LEU B 1104  LEU B 1115  1                                  12    
HELIX   48  48 ASP B 1118  GLU B 1124  1                                   7    
HELIX   49  49 GLY B 1134  LEU B 1150  1                                  17    
HELIX   50  50 PRO B 1194  MET B 1197  5                                   4    
HELIX   51  51 ASP B 1261  ASP B 1268  1                                   8    
HELIX   52  52 ARG B 1269  ASN B 1274  1                                   6    
HELIX   53  53 ILE B 1275  ARG B 1277  5                                   3    
HELIX   54  54 LYS B 1289  SER B 1314  1                                  26    
HELIX   55  55 ALA B 1328  GLN B 1332  1                                   5    
HELIX   56  56 LEU B 1344  ILE B 1356  1                                  13    
HELIX   57  57 PRO B 1360  THR B 1371  1                                  12    
HELIX   58  58 LEU B 1380  LEU B 1384  5                                   5    
HELIX   59  59 VAL B 1389  LEU B 1396  1                                   8    
HELIX   60  60 LEU B 1396  PHE B 1418  1                                  23    
HELIX   61  61 ASP B 1421  SER B 1429  1                                   9    
HELIX   62  62 MET B 1441  GLY B 1448  1                                   8    
HELIX   63  63 ALA B 1456  LYS B 1466  1                                  11    
HELIX   64  64 PHE B 1468  GLU B 1475  1                                   8    
HELIX   65  65 ASN B 1496  GLY B 1508  1                                  13    
HELIX   66  66 GLU B 1509  LYS B 1513  5                                   5    
HELIX   67  67 ASP B 1514  LEU B 1525  5                                  12    
HELIX   68  68 ASP B 1527  TYR B 1553  1                                  27    
HELIX   69  69 HIS B 1571  LYS B 1574  5                                   4    
HELIX   70  70 ARG B 1575  LYS B 1592  1                                  18    
HELIX   71  71 TYR B 1613  ASP B 1633  1                                  21    
HELIX   72  72 VAL B 1636  SER B 1638  5                                   3    
HELIX   73  73 ARG B 1649  ILE B 1657  1                                   9    
HELIX   74  74 PRO B 1658  THR B 1660  5                                   3    
HELIX   75  75 THR B 1676  ASN B 1684  1                                   9    
HELIX   76  76 ALA B 1695  GLY B 1704  1                                  10    
HELIX   77  77 GLU B 1705  LEU B 1708  5                                   4    
HELIX   78  78 ARG B 1714  GLY B 1725  1                                  12    
HELIX   79  79 GLU B 1727  LEU B 1735  1                                   9    
HELIX   80  80 LEU B 1735  ASN B 1747  1                                  13    
HELIX   81  81 PHE B 1758  HIS B 1768  1                                  11    
HELIX   82  82 VAL B 1773  ALA B 1775  5                                   3    
HELIX   83  83 ASP B 1776  MET B 1792  1                                  17    
HELIX   84  84 ASN B 1793  ALA B 1806  1                                  14    
HELIX   85  85 ALA B 1807  PHE B 1811  5                                   5    
HELIX   86  86 SER B 1812  ILE B 1824  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 PHE A  89  TYR A  90  0                                        
SHEET    2   C 2 GLY A 130  LEU A 131 -1  O  LEU A 131   N  PHE A  89           
SHEET    1   D 2 ASN A 167  ARG A 171  0                                        
SHEET    2   D 2 TRP A 174  GLU A 178 -1  O  TRP A 174   N  ARG A 171           
SHEET    1   E 2 LYS A 205  THR A 209  0                                        
SHEET    2   E 2 GLY A 212  ILE A 216 -1  N  GLY A 212   O  THR A 209           
SHEET    1   F 3 ARG A 386  PRO A 388  0                                        
SHEET    2   F 3 ARG A 438  ASN A 440 -1  N  ILE A 439   O  TRP A 387           
SHEET    3   F 3 ILE A 431  GLU A 432 -1  N  GLU A 432   O  ARG A 438           
SHEET    1   G 6 LEU A 640  LEU A 645  0                                        
SHEET    2   G 6 ARG A 601  GLY A 606  1  O  ARG A 601   N  LYS A 641           
SHEET    3   G 6 MET A 562  VAL A 567  1  O  MET A 562   N  THR A 602           
SHEET    4   G 6 LEU A 662  GLN A 665  1  O  LEU A 662   N  VAL A 565           
SHEET    5   G 6 LEU A 687  GLY A 690  1  O  LEU A 687   N  SER A 663           
SHEET    6   G 6 PHE A 709  ILE A 710  1  N  PHE A 709   O  THR A 688           
SHEET    1   H 9 PHE B1479  ASN B1481  0                                        
SHEET    2   H 9 ALA B1451  GLY B1454  1  O  VAL B1452   N  GLN B1480           
SHEET    3   H 9 PHE B1372  THR B1375  1  O  PHE B1372   N  ALA B1451           
SHEET    4   H 9 VAL B1333  ASN B1338  1  O  ILE B1335   N  ALA B1373           
SHEET    5   H 9 ARG B1081  LEU B1085  1  O  ARG B1081   N  ALA B1334           
SHEET    6   H 9 ALA B1154  ILE B1159  1  O  TYR B1155   N  TYR B1084           
SHEET    7   H 9 VAL B1238  ARG B1247  1  O  THR B1240   N  GLY B1156           
SHEET    8   H 9 GLN B1219  PRO B1231 -1  N  LEU B1222   O  ARG B1247           
SHEET    9   H 9 LYS B1191  SER B1192 -1  O  LYS B1191   N  ASP B1227           
SHEET    1   I 9 PHE B1479  ASN B1481  0                                        
SHEET    2   I 9 ALA B1451  GLY B1454  1  O  VAL B1452   N  GLN B1480           
SHEET    3   I 9 PHE B1372  THR B1375  1  O  PHE B1372   N  ALA B1451           
SHEET    4   I 9 VAL B1333  ASN B1338  1  O  ILE B1335   N  ALA B1373           
SHEET    5   I 9 ARG B1081  LEU B1085  1  O  ARG B1081   N  ALA B1334           
SHEET    6   I 9 ALA B1154  ILE B1159  1  O  TYR B1155   N  TYR B1084           
SHEET    7   I 9 VAL B1238  ARG B1247  1  O  THR B1240   N  GLY B1156           
SHEET    8   I 9 GLN B1219  PRO B1231 -1  N  LEU B1222   O  ARG B1247           
SHEET    9   I 9 LEU B1198  PHE B1202 -1  O  LEU B1198   N  ALA B1223           
SHEET    1   J 2 PHE B1089  GLY B1092  0                                        
SHEET    2   J 2 ALA B1129  LEU B1131 -1  O  ALA B1129   N  GLY B1092           
SHEET    1   K 2 ASN B1167  ARG B1171  0                                        
SHEET    2   K 2 TRP B1174  GLU B1178 -1  O  TRP B1174   N  ARG B1171           
SHEET    1   L 2 LYS B1205  HIS B1208  0                                        
SHEET    2   L 2 THR B1213  ILE B1216 -1  N  LYS B1214   O  GLU B1207           
SHEET    1   M 3 ARG B1386  PRO B1388  0                                        
SHEET    2   M 3 ARG B1438  ASN B1440 -1  N  ILE B1439   O  TRP B1387           
SHEET    3   M 3 ILE B1431  GLU B1432 -1  N  GLU B1432   O  ARG B1438           
SHEET    1   N 6 LEU B1640  LEU B1645  0                                        
SHEET    2   N 6 ARG B1601  GLY B1606  1  O  ARG B1601   N  LYS B1641           
SHEET    3   N 6 MET B1562  VAL B1567  1  O  MET B1562   N  THR B1602           
SHEET    4   N 6 LEU B1662  GLN B1665  1  O  LEU B1662   N  VAL B1565           
SHEET    5   N 6 LEU B1687  GLY B1690  1  O  LEU B1687   N  SER B1663           
SHEET    6   N 6 PHE B1709  ILE B1710  1  N  PHE B1709   O  THR B1688           
LINK         C4A PLP A 860                 NZ  LYS A 680     1555   1555  1.47  
LINK         C4A PLP B1860                 NZ  LYS B1680     1555   1555  1.44  
SITE     1 AC1 14 LEU A 136  ASN A 284  HIS A 377  THR A 378                    
SITE     2 AC1 14 VAL A 455  ASN A 484  TYR A 573  GLU A 672                    
SITE     3 AC1 14 ALA A 673  SER A 674  GLY A 675  HOH A2052                    
SITE     4 AC1 14 HOH A2173  HOH A2225                                          
SITE     1 AC2 17 GLY B1135  LEU B1136  LEU B1139  ASN B1284                    
SITE     2 AC2 17 ASP B1339  HIS B1377  VAL B1455  ASN B1484                    
SITE     3 AC2 17 TYR B1573  GLU B1672  ALA B1673  SER B1674                    
SITE     4 AC2 17 GLY B1675  HOH B2142  HOH B2153  HOH B2207                    
SITE     5 AC2 17 HOH B2253                                                     
SITE     1 AC3 14 TYR A  90  GLY A 135  TRP A 491  LYS A 568                    
SITE     2 AC3 14 LYS A 574  ARG A 649  VAL A 650  GLY A 675                    
SITE     3 AC3 14 THR A 676  GLY A 677  LYS A 680  HOH A2014                    
SITE     4 AC3 14 HOH A2055  HOH A2162                                          
SITE     1 AC4 14 GLY B1134  TRP B1491  LYS B1568  LYS B1574                    
SITE     2 AC4 14 ARG B1649  VAL B1650  ALA B1653  GLY B1675                    
SITE     3 AC4 14 THR B1676  GLY B1677  LYS B1680  HOH B2049                    
SITE     4 AC4 14 HOH B2056  HOH B2239                                          
CRYST1  124.000  124.000  122.280  90.00  90.00 120.00 P 31          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  0.004656  0.000000        0.00000                         
SCALE2      0.000000  0.009312  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008178        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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