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Database: PDB
Entry: 1XOI
LinkDB: 1XOI
Original site: 1XOI 
HEADER    TRANSFERASE                             06-OCT-04   1XOI              
TITLE     HUMAN LIVER GLYCOGEN PHOSPHORYLASE A COMPLEXED WITH CHLOROINDOLOYL    
TITLE    2 GLYCINE AMIDE                                                        
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 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    ALLOSTERIC ENZYME, GLYCOGEN STORAGE DISEASE, GLYCOSYLTRANSFERASE,     
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.W.WRIGHT,V.L.RATH,E.M.GIBBS,J.L.TREADWAY                            
REVDAT   3   13-JUL-11 1XOI    1       VERSN                                    
REVDAT   2   24-FEB-09 1XOI    1       VERSN                                    
REVDAT   1   12-APR-05 1XOI    0                                                
JRNL        AUTH   S.W.WRIGHT,V.L.RATH,P.E.GENEREUX,D.L.HAGEMAN,C.B.LEVY,       
JRNL        AUTH 2 L.D.MCCLURE,S.C.MCCOID,R.K.MCPHERSON,T.M.SCHELHORN,          
JRNL        AUTH 3 D.E.WILDER,W.J.ZAVADOSKI,E.M.GIBBS,J.L.TREADWAY              
JRNL        TITL   5-CHLOROINDOLOYL GLYCINE AMIDE INHIBITORS OF GLYCOGEN        
JRNL        TITL 2 PHOSPHORYLASE: SYNTHESIS, IN VITRO, IN VIVO, AND X-RAY       
JRNL        TITL 3 CRYSTALLOGRAPHIC CHARACTERIZATION.                           
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  15   459 2005              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   15603973                                                     
JRNL        DOI    10.1016/J.BMCL.2004.10.048                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 99.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 114216                         
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) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 11451                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13016                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 110                                     
REMARK   3   SOLVENT ATOMS            : 636                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1XOI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-OCT-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030580.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRANDEIS - B4                      
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 121683                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: AB INITIO PHASING            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 290.0K                                                  
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       41.03433            
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       82.06867            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 57790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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   260                                                      
REMARK 465     ASP A   261                                                      
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  1260                                                      
REMARK 465     ASP B  1261                                                      
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: 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 B1755   C   -  N   -  CA  ANGL. DEV. =   9.0 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    LEU A 131       43.93    -86.99                                   
REMARK 500    PHE A 166      150.57    -49.82                                   
REMARK 500    ARG A 193       72.38   -119.57                                   
REMARK 500    TYR A 203     -132.00     53.87                                   
REMARK 500    ASN A 235       11.95   -144.52                                   
REMARK 500    PRO A 281       25.71    -70.72                                   
REMARK 500    LYS A 315       17.29     59.66                                   
REMARK 500    PHE A 316      158.74    -34.12                                   
REMARK 500    SER A 318      103.78     42.43                                   
REMARK 500    ARG A 320      129.75    -15.10                                   
REMARK 500    ALA A 322      -88.05     47.47                                   
REMARK 500    THR A 324       34.04     33.48                                   
REMARK 500    VAL A 325      -86.27     78.40                                   
REMARK 500    PHE A 326       -5.50     54.29                                   
REMARK 500    ASP A 339     -174.54     69.97                                   
REMARK 500    VAL A 379      -60.20   -124.63                                   
REMARK 500    GLU A 434      131.85    -37.47                                   
REMARK 500    ALA A 456      141.28   -172.13                                   
REMARK 500    LYS A 466      -76.18   -115.14                                   
REMARK 500    PRO A 476      -71.89    -48.41                                   
REMARK 500    ASP A 477       -8.98    -46.63                                   
REMARK 500    LEU A 492      -70.37   -154.77                                   
REMARK 500    LYS A 568      170.61    175.27                                   
REMARK 500    ASP A 593       67.84   -150.01                                   
REMARK 500    PRO A 594       -7.76    -46.98                                   
REMARK 500    SER A 674      -57.86   -148.54                                   
REMARK 500    SER A 751       64.07   -155.11                                   
REMARK 500    LYS A 753        3.31    -66.64                                   
REMARK 500    GLN A 754       72.79   -165.33                                   
REMARK 500    ILE A 824      -54.37   -132.64                                   
REMARK 500    LEU A 832     -153.64   -136.47                                   
REMARK 500    LYS A 833      107.89   -176.76                                   
REMARK 500    ILE A 834      100.70    -54.17                                   
REMARK 500    LEU A 836      -87.39   -125.36                                   
REMARK 500    SER A 837     -169.84    -76.17                                   
REMARK 500    LEU B1131       44.57    -87.13                                   
REMARK 500    ARG B1193       71.01   -117.19                                   
REMARK 500    TYR B1203     -131.00     53.92                                   
REMARK 500    ASN B1235       11.35   -143.14                                   
REMARK 500    PRO B1281       25.65    -70.67                                   
REMARK 500    LYS B1315       83.59     34.74                                   
REMARK 500    SER B1318      119.32     57.63                                   
REMARK 500    ARG B1320      -93.95    -32.15                                   
REMARK 500    ALA B1322      -72.97     13.34                                   
REMARK 500    THR B1324       35.47    -70.70                                   
REMARK 500    VAL B1325      -49.42     70.76                                   
REMARK 500    PHE B1326       -0.46     46.57                                   
REMARK 500    ASP B1339     -174.84     70.11                                   
REMARK 500    THR B1378      144.66    179.63                                   
REMARK 500    GLU B1434      132.16    -37.70                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      68 RAMACHANDRAN OUTLIERS.                        
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 B2302        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH B2497        DISTANCE =  5.33 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  860                                                       
REMARK 610     PLP B 1860                                                       
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 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 288 A 862                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 288 B 1862                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1EM6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1EXV   RELATED DB: PDB                                   
DBREF  1XOI A    1   846  UNP    P06737   PHS1_HUMAN       1    846             
DBREF  1XOI B 1001  1846  UNP    P06737   PHS1_HUMAN       1    846             
SEQADV 1XOI ALA A  323  UNP  P06737    GLY   323 CONFLICT                       
SEQADV 1XOI ALA B 1323  UNP  P06737    GLY   323 CONFLICT                       
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 ALA 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 ALA 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                                                       
HET    288  A 862      25                                                       
HET    288  B1862      25                                                       
HETNAM     NBG 1-N-ACETYL-BETA-D-GLUCOSAMINE                                    
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     288 5-CHLORO-1H-INDOLE-2-CARBOXYLIC ACID{[CYCLOPENTYL-(2-            
HETNAM   2 288  HYDROXY-ETHYL)-CARBAMOYL]-METHYL}-AMIDE                         
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   3  NBG    2(C8 H15 N O6)                                               
FORMUL   5  PLP    2(C8 H10 N O6 P)                                             
FORMUL   7  288    2(C18 H24 CL N3 O3)                                          
FORMUL   9  HOH   *636(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  LEU A  102  1                                   9    
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 TYR A  262  ASP A  268  1                                   7    
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 ALA A  328  GLN A  332  1                                   5    
HELIX   13  13 LEU A  344  ILE A  356  1                                  13    
HELIX   14  14 PRO A  360  THR A  371  1                                  12    
HELIX   15  15 LEU A  380  LEU A  384  5                                   5    
HELIX   16  16 VAL A  389  LEU A  396  1                                   8    
HELIX   17  17 LEU A  396  PHE A  418  1                                  23    
HELIX   18  18 ASP A  421  SER A  429  1                                   9    
HELIX   19  19 MET A  441  SER A  449  1                                   9    
HELIX   20  20 ALA A  456  LYS A  466  1                                  11    
HELIX   21  21 PHE A  468  GLU A  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 ARG A  575  ASP A  593  1                                  19    
HELIX   27  27 TYR A  613  ASP A  633  1                                  21    
HELIX   28  28 VAL A  636  SER A  638  5                                   3    
HELIX   29  29 ARG A  649  ILE A  657  1                                   9    
HELIX   30  30 PRO A  658  THR A  660  5                                   3    
HELIX   31  31 THR A  676  ASN A  684  1                                   9    
HELIX   32  32 ALA A  695  GLY A  704  1                                  10    
HELIX   33  33 GLU A  705  LEU A  708  5                                   4    
HELIX   34  34 ARG A  714  GLY A  725  1                                  12    
HELIX   35  35 GLU A  727  LEU A  735  1                                   9    
HELIX   36  36 LEU A  735  GLY A  748  1                                  14    
HELIX   37  37 PHE A  758  HIS A  768  1                                  11    
HELIX   38  38 LYS A  772  MET A  792  1                                  21    
HELIX   39  39 ASN A  793  ALA A  807  1                                  15    
HELIX   40  40 SER A  808  PHE A  811  5                                   4    
HELIX   41  41 SER A  812  ILE A  824  1                                  13    
HELIX   42  42 ASN B 1023  THR B 1038  1                                  16    
HELIX   43  43 THR B 1047  CYS B 1078  1                                  32    
HELIX   44  44 THR B 1094  LEU B 1102  1                                   9    
HELIX   45  45 LEU B 1104  LEU B 1115  1                                  12    
HELIX   46  46 ASP B 1118  GLU B 1126  1                                   9    
HELIX   47  47 GLY B 1134  LEU B 1150  1                                  17    
HELIX   48  48 PRO B 1194  MET B 1197  5                                   4    
HELIX   49  49 TYR B 1262  ASP B 1268  1                                   7    
HELIX   50  50 ARG B 1269  ASN B 1274  1                                   6    
HELIX   51  51 ILE B 1275  ARG B 1277  5                                   3    
HELIX   52  52 LYS B 1289  ALA B 1313  1                                  25    
HELIX   53  53 ALA B 1328  GLN B 1332  1                                   5    
HELIX   54  54 LEU B 1344  ILE B 1356  1                                  13    
HELIX   55  55 PRO B 1360  THR B 1371  1                                  12    
HELIX   56  56 LEU B 1380  LEU B 1384  5                                   5    
HELIX   57  57 VAL B 1389  LEU B 1396  1                                   8    
HELIX   58  58 LEU B 1396  PHE B 1418  1                                  23    
HELIX   59  59 ASP B 1421  SER B 1429  1                                   9    
HELIX   60  60 MET B 1441  SER B 1449  1                                   9    
HELIX   61  61 ALA B 1456  LYS B 1466  1                                  11    
HELIX   62  62 PHE B 1468  GLU B 1475  1                                   8    
HELIX   63  63 ASN B 1496  GLY B 1508  1                                  13    
HELIX   64  64 GLU B 1509  LYS B 1513  5                                   5    
HELIX   65  65 ASP B 1514  LEU B 1525  5                                  12    
HELIX   66  66 ASP B 1527  TYR B 1553  1                                  27    
HELIX   67  67 HIS B 1571  LYS B 1574  5                                   4    
HELIX   68  68 ARG B 1575  ASP B 1593  1                                  19    
HELIX   69  69 TYR B 1613  ASP B 1633  1                                  21    
HELIX   70  70 VAL B 1636  SER B 1638  5                                   3    
HELIX   71  71 ARG B 1649  ILE B 1657  1                                   9    
HELIX   72  72 PRO B 1658  THR B 1660  5                                   3    
HELIX   73  73 THR B 1676  ASN B 1684  1                                   9    
HELIX   74  74 ALA B 1695  GLY B 1704  1                                  10    
HELIX   75  75 GLU B 1705  LEU B 1708  5                                   4    
HELIX   76  76 ARG B 1714  GLY B 1725  1                                  12    
HELIX   77  77 GLU B 1727  LEU B 1735  1                                   9    
HELIX   78  78 LEU B 1735  GLY B 1748  1                                  14    
HELIX   79  79 PHE B 1758  HIS B 1768  1                                  11    
HELIX   80  80 LYS B 1772  MET B 1792  1                                  21    
HELIX   81  81 ASN B 1793  ALA B 1807  1                                  15    
HELIX   82  82 SER B 1808  PHE B 1811  5                                   4    
HELIX   83  83 SER B 1812  ILE B 1824  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  LEU A 198   O  ALA A 223           
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  ARG A 247   N  LEU A 222           
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 155           
SHEET    6   B 9 VAL A 333  ASN A 338  1  O  ALA A 334   N  TYR A  83           
SHEET    7   B 9 PHE A 372  THR A 375  1  O  ALA A 373   N  LEU A 337           
SHEET    8   B 9 VAL A 452  GLY A 454  1  O  ASN A 453   N  TYR A 374           
SHEET    9   B 9 PHE A 479  ASN A 481  1  O  GLN A 480   N  VAL A 452           
SHEET    1   C 2 PHE A  89  GLY A  92  0                                        
SHEET    2   C 2 ALA A 129  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  VAL A 176   N  LYS A 169           
SHEET    1   E 2 LYS A 205  THR A 209  0                                        
SHEET    2   E 2 GLY A 212  ILE A 216 -1  O  LYS A 214   N  GLU A 207           
SHEET    1   F 3 ARG A 386  PRO A 388  0                                        
SHEET    2   F 3 ARG A 438  ASN A 440 -1  O  ILE A 439   N  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  N  VAL A 603   O  LYS A 641           
SHEET    3   G 6 MET A 562  VAL A 567  1  N  ASP A 564   O  ILE A 604           
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  O  PHE A 709   N  THR A 688           
SHEET    1   H 3 LYS B1191  SER B1192  0                                        
SHEET    2   H 3 GLN B1219  PRO B1231 -1  O  ASP B1227   N  LYS B1191           
SHEET    3   H 3 LEU B1198  PHE B1202 -1  N  LEU B1198   O  ALA B1223           
SHEET    1   I 9 LYS B1191  SER B1192  0                                        
SHEET    2   I 9 GLN B1219  PRO B1231 -1  O  ASP B1227   N  LYS B1191           
SHEET    3   I 9 VAL B1238  ARG B1247 -1  O  ARG B1247   N  LEU B1222           
SHEET    4   I 9 ALA B1154  ILE B1159  1  N  GLY B1156   O  ARG B1242           
SHEET    5   I 9 ARG B1081  LEU B1085  1  N  TYR B1084   O  TYR B1155           
SHEET    6   I 9 VAL B1333  ASN B1338  1  O  ALA B1334   N  TYR B1083           
SHEET    7   I 9 PHE B1372  THR B1375  1  O  ALA B1373   N  LEU B1337           
SHEET    8   I 9 VAL B1452  GLY B1454  1  O  ASN B1453   N  TYR B1374           
SHEET    9   I 9 PHE B1479  ASN B1481  1  O  GLN B1480   N  VAL B1452           
SHEET    1   J 2 PHE B1089  GLY B1092  0                                        
SHEET    2   J 2 ALA B1129  LEU B1131 -1  O  LEU B1131   N  PHE B1089           
SHEET    1   K 2 ASN B1167  ARG B1171  0                                        
SHEET    2   K 2 TRP B1174  GLU B1178 -1  O  VAL B1176   N  LYS B1169           
SHEET    1   L 2 LYS B1205  THR B1209  0                                        
SHEET    2   L 2 GLY B1212  ILE B1216 -1  O  LYS B1214   N  GLU B1207           
SHEET    1   M 3 ARG B1386  PRO B1388  0                                        
SHEET    2   M 3 ARG B1438  ASN B1440 -1  O  ILE B1439   N  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  N  VAL B1603   O  LYS B1641           
SHEET    3   N 6 MET B1562  VAL B1567  1  N  ASP B1564   O  ILE B1604           
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  O  PHE B1709   N  THR B1688           
SITE     1 AC1 12 ASN A 284  HIS A 377  VAL A 455  ASN A 484                    
SITE     2 AC1 12 TYR A 573  GLU A 672  ALA A 673  SER A 674                    
SITE     3 AC1 12 GLY A 675  HOH A1981  HOH A2115  HOH A2223                    
SITE     1 AC2 17 GLY B1135  LEU B1136  ASN B1284  ASP B1339                    
SITE     2 AC2 17 HIS B1377  THR B1378  VAL B1455  ASN B1484                    
SITE     3 AC2 17 TYR B1573  GLU B1672  ALA B1673  SER B1674                    
SITE     4 AC2 17 GLY B1675  HOH B1864  HOH B2086  HOH B2253                    
SITE     5 AC2 17 HOH B2254                                                     
SITE     1 AC3 17 GLY A 134  GLY A 135  LYS A 568  LYS A 574                    
SITE     2 AC3 17 TYR A 648  ARG A 649  VAL A 650  GLY A 675                    
SITE     3 AC3 17 THR A 676  GLY A 677  LYS A 680  HOH A1886                    
SITE     4 AC3 17 HOH A1891  HOH A1981  HOH A2053  HOH A2063                    
SITE     5 AC3 17 HOH A2154                                                     
SITE     1 AC4 17 GLY B1134  GLY B1135  TRP B1491  LYS B1568                    
SITE     2 AC4 17 LYS B1574  TYR B1648  ARG B1649  VAL B1650                    
SITE     3 AC4 17 GLY B1675  THR B1676  GLY B1677  LYS B1680                    
SITE     4 AC4 17 HOH B1907  HOH B1920  HOH B1936  HOH B2015                    
SITE     5 AC4 17 HOH B2182                                                     
SITE     1 AC5 19 ARG A  60  LEU A  63  VAL A  64  TRP A  67                    
SITE     2 AC5 19 PRO A 188  GLU A 190  LYS A 191  SER A 192                    
SITE     3 AC5 19 PRO A 194  HOH A1991  HOH A1994  THR B1038                    
SITE     4 AC5 19 VAL B1040  HIS B1057  TYR B1185  GLY B1186                    
SITE     5 AC5 19 ASN B1187  PRO B1188  HOH B2228                               
SITE     1 AC6 16 THR A  38  VAL A  40  HIS A  57  TYR A 185                    
SITE     2 AC6 16 PRO A 188  ARG B1060  LEU B1063  VAL B1064                    
SITE     3 AC6 16 TRP B1067  PRO B1188  GLU B1190  LYS B1191                    
SITE     4 AC6 16 SER B1192  HOH B1911  HOH B1948  HOH B2068                    
CRYST1  123.906  123.906  123.103  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      0.008071  0.004660  0.000000        0.00000                         
SCALE2      0.000000  0.009319  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008123        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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