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Database: PDB
Entry: 1EM6
LinkDB: 1EM6
Original site: 1EM6 
HEADER    TRANSFERASE                             16-MAR-00   1EM6              
TITLE     HUMAN LIVER GLYCOGEN PHOSPHORYLASE A COMPLEXED WITH GLCNAC AND CP-526,
TITLE    2 423                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIVER GLYCOGEN PHOSPHORYLASE;                              
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 ORGAN: 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_PLASMID: PBLUEBACII                                
KEYWDS    ALLOSTERIC SITE, ALLOSTERIC BINDING, TRANSFERASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.L.RATH,M.AMMIRATI,D.E.DANLEY,J.L.EKSTROM,T.R.HYNES,T.V.OLSON,       
AUTHOR   2 D.J.HOOVER                                                           
REVDAT   4   13-JUL-11 1EM6    1       VERSN                                    
REVDAT   3   24-FEB-09 1EM6    1       VERSN                                    
REVDAT   2   01-APR-03 1EM6    1       JRNL                                     
REVDAT   1   01-NOV-00 1EM6    0                                                
JRNL        AUTH   V.L.RATH,M.AMMIRATI,D.E.DANLEY,J.L.EKSTROM,E.M.GIBBS,        
JRNL        AUTH 2 T.R.HYNES,A.M.MATHIOWETZ,R.K.MCPHERSON,T.V.OLSON,            
JRNL        AUTH 3 J.L.TREADWAY,D.J.HOOVER                                      
JRNL        TITL   HUMAN LIVER GLYCOGEN PHOSPHORYLASE INHIBITORS BIND AT A NEW  
JRNL        TITL 2 ALLOSTERIC SITE.                                             
JRNL        REF    CHEM.BIOL.                    V.   7   677 2000              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   10980448                                                     
JRNL        DOI    10.1016/S1074-5521(00)00004-1                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 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 : CNS DEFAULT                                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 99.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 194745.340                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 97974                          
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) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 9800                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 12669                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3070                       
REMARK   3   BIN FREE R VALUE                    : 0.3400                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1392                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.009                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12760                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 102                                     
REMARK   3   SOLVENT ATOMS            : 737                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.48000                                             
REMARK   3    B22 (A**2) : -1.48000                                             
REMARK   3    B33 (A**2) : 2.97000                                              
REMARK   3    B12 (A**2) : 1.65000                                              
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) : 0.30                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.30                            
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) : 0.35                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.34                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.76                            
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) : 0.490 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 0.890 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 0.800 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 1.120 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 49.10                                                
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.PAR                                
REMARK   3  PARAMETER FILE  2  : WATER_REP.PAR                                  
REMARK   3  PARAMETER FILE  3  : ALL.PAR                                        
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ALL.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1EM6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB010719.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-APR-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) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.15                               
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   : 103325                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35900                            
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: NULL                         
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   (%): 55.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, MPD, PH 6.0, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 290K                                      
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       40.77300            
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       81.54600            
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: 8040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 54020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 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     MET A     0                                                      
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     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     LYS A   315                                                      
REMARK 465     PHE A   316                                                      
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     LYS A   595                                                      
REMARK 465     LYS A   596                                                      
REMARK 465     LEU A   597                                                      
REMARK 465     ASP A   831                                                      
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     MET B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     GLN B     7                                                      
REMARK 465     GLU B     8                                                      
REMARK 465     LYS B     9                                                      
REMARK 465     ARG B    10                                                      
REMARK 465     ARG B    11                                                      
REMARK 465     GLN B    12                                                      
REMARK 465     ILE B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     ILE B    15                                                      
REMARK 465     ARG B    16                                                      
REMARK 465     GLY B    17                                                      
REMARK 465     ILE B    18                                                      
REMARK 465     VAL B    19                                                      
REMARK 465     GLY B    20                                                      
REMARK 465     VAL B    21                                                      
REMARK 465     ASN B   250                                                      
REMARK 465     ASP B   251                                                      
REMARK 465     PHE B   252                                                      
REMARK 465     ASN B   253                                                      
REMARK 465     LEU B   254                                                      
REMARK 465     ARG B   255                                                      
REMARK 465     ASP B   256                                                      
REMARK 465     PHE B   257                                                      
REMARK 465     ASN B   258                                                      
REMARK 465     VAL B   259                                                      
REMARK 465     LYS B   315                                                      
REMARK 465     PHE B   316                                                      
REMARK 465     GLY B   317                                                      
REMARK 465     SER B   318                                                      
REMARK 465     THR B   319                                                      
REMARK 465     ARG B   320                                                      
REMARK 465     GLY B   321                                                      
REMARK 465     ALA B   322                                                      
REMARK 465     GLY B   323                                                      
REMARK 465     LYS B   595                                                      
REMARK 465     LYS B   596                                                      
REMARK 465     LEU B   597                                                      
REMARK 465     ASP B   831                                                      
REMARK 465     LEU B   832                                                      
REMARK 465     LYS B   833                                                      
REMARK 465     ILE B   834                                                      
REMARK 465     SER B   835                                                      
REMARK 465     LEU B   836                                                      
REMARK 465     SER B   837                                                      
REMARK 465     ASN B   838                                                      
REMARK 465     GLU B   839                                                      
REMARK 465     SER B   840                                                      
REMARK 465     ASN B   841                                                      
REMARK 465     LYS B   842                                                      
REMARK 465     VAL B   843                                                      
REMARK 465     ASN B   844                                                      
REMARK 465     GLY B   845                                                      
REMARK 465     ASN B   846                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLU A   505     NZ   LYS B   312     2555     2.03            
REMARK 500   OD1  ASN A   210     O    HOH B  2026     2665     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 755   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    PRO B 755   C   -  N   -  CA  ANGL. DEV. =   9.5 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       41.86    -87.74                                   
REMARK 500    TYR A 203     -131.53     56.44                                   
REMARK 500    ASN A 235       12.44   -149.87                                   
REMARK 500    ASN A 236       -6.52     69.85                                   
REMARK 500    PRO A 281       29.10    -74.13                                   
REMARK 500    ASP A 339     -174.56     73.94                                   
REMARK 500    VAL A 379      -44.21   -138.14                                   
REMARK 500    ASP A 421       92.76    -66.95                                   
REMARK 500    GLU A 433       54.03   -112.88                                   
REMARK 500    SER A 436       83.81     81.87                                   
REMARK 500    ALA A 456      142.62   -172.73                                   
REMARK 500    LYS A 466      -68.13   -120.91                                   
REMARK 500    LEU A 492      -68.36   -156.36                                   
REMARK 500    ASP A 527       95.69    -67.69                                   
REMARK 500    LYS A 568      170.01    174.48                                   
REMARK 500    SER A 674      -60.40   -151.80                                   
REMARK 500    SER A 751       60.93   -164.06                                   
REMARK 500    GLN A 754       69.99   -158.31                                   
REMARK 500    LYS A 772       60.04     33.21                                   
REMARK 500    ILE A 824      -55.09   -133.21                                   
REMARK 500    LEU B 131       42.21    -89.02                                   
REMARK 500    PHE B 166      151.00    -49.85                                   
REMARK 500    TYR B 203     -131.06     56.14                                   
REMARK 500    ASN B 235       12.36   -149.13                                   
REMARK 500    ASN B 236       -6.65     69.89                                   
REMARK 500    PRO B 281       27.95    -74.46                                   
REMARK 500    ASP B 339     -176.16     74.25                                   
REMARK 500    VAL B 379      -44.54   -138.42                                   
REMARK 500    ASP B 421       92.08    -66.64                                   
REMARK 500    GLU B 433       53.84   -112.57                                   
REMARK 500    SER B 436       83.21     81.11                                   
REMARK 500    ALA B 456      142.95   -173.35                                   
REMARK 500    LYS B 466      -68.39   -120.68                                   
REMARK 500    LEU B 492      -69.12   -155.13                                   
REMARK 500    ASP B 527       95.75    -65.33                                   
REMARK 500    LYS B 568      169.91    175.25                                   
REMARK 500    SER B 674      -60.47   -151.30                                   
REMARK 500    SER B 751       61.87   -164.53                                   
REMARK 500    GLN B 754       69.90   -158.47                                   
REMARK 500    HIS B 768       33.42   -140.29                                   
REMARK 500    LYS B 772       60.48     33.46                                   
REMARK 500    ILE B 824      -54.78   -133.27                                   
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 CP4 A 862                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 860                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 1860                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 1902                
DBREF  1EM6 A    0   846  UNP    P06737   PHS1_HUMAN       1    847             
DBREF  1EM6 B    0   846  UNP    P06737   PHS1_HUMAN       1    847             
SEQADV 1EM6 ARG A  569  UNP  P06737    SER   570 SEE REMARK 999                 
SEQADV 1EM6 ARG B  569  UNP  P06737    SER   570 SEE REMARK 999                 
SEQRES   1 A  847  MET ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG GLN          
SEQRES   2 A  847  ILE SER ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL ALA          
SEQRES   3 A  847  GLU LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE THR          
SEQRES   4 A  847  LEU VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP TYR          
SEQRES   5 A  847  TYR PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL          
SEQRES   6 A  847  GLY ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP LYS          
SEQRES   7 A  847  CYS PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE TYR          
SEQRES   8 A  847  MET GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU GLY          
SEQRES   9 A  847  LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU GLY          
SEQRES  10 A  847  LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA          
SEQRES  11 A  847  GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS          
SEQRES  12 A  847  PHE LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR          
SEQRES  13 A  847  GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN GLN          
SEQRES  14 A  847  LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP ASP          
SEQRES  15 A  847  TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG PRO          
SEQRES  16 A  847  GLU PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL GLU          
SEQRES  17 A  847  HIS THR ASN THR GLY THR LYS TRP ILE ASP THR GLN VAL          
SEQRES  18 A  847  VAL LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY TYR          
SEQRES  19 A  847  MET ASN ASN THR VAL ASN THR MET ARG LEU TRP SER ALA          
SEQRES  20 A  847  ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN VAL          
SEQRES  21 A  847  GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA          
SEQRES  22 A  847  GLU ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE          
SEQRES  23 A  847  PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE          
SEQRES  24 A  847  VAL VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE          
SEQRES  25 A  847  LYS ALA SER LYS PHE GLY SER THR ARG GLY ALA GLY THR          
SEQRES  26 A  847  VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN LEU          
SEQRES  27 A  847  ASN ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU MET          
SEQRES  28 A  847  ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER LYS          
SEQRES  29 A  847  ALA TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR ASN          
SEQRES  30 A  847  HIS THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL          
SEQRES  31 A  847  ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU ILE          
SEQRES  32 A  847  ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE VAL          
SEQRES  33 A  847  ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG MET          
SEQRES  34 A  847  SER LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN MET          
SEQRES  35 A  847  ALA HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN GLY          
SEQRES  36 A  847  VAL ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS VAL          
SEQRES  37 A  847  PHE LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE GLN          
SEQRES  38 A  847  ASN LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU LEU          
SEQRES  39 A  847  LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU LYS          
SEQRES  40 A  847  ILE GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU THR          
SEQRES  41 A  847  LYS LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU ARG          
SEQRES  42 A  847  GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE          
SEQRES  43 A  847  SER GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE ASN          
SEQRES  44 A  847  PRO SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE HIS          
SEQRES  45 A  847  GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE          
SEQRES  46 A  847  THR MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS LEU          
SEQRES  47 A  847  PHE VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA ALA          
SEQRES  48 A  847  PRO GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE          
SEQRES  49 A  847  THR SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET VAL          
SEQRES  50 A  847  GLY SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR ARG          
SEQRES  51 A  847  VAL SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP LEU          
SEQRES  52 A  847  SER GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY          
SEQRES  53 A  847  THR GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR          
SEQRES  54 A  847  ILE GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU          
SEQRES  55 A  847  GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET ARG          
SEQRES  56 A  847  ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR GLU          
SEQRES  57 A  847  ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS LEU          
SEQRES  58 A  847  VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO LYS          
SEQRES  59 A  847  GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU PHE          
SEQRES  60 A  847  TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU ALA          
SEQRES  61 A  847  TYR VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR MET          
SEQRES  62 A  847  ASN PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN ILE          
SEQRES  63 A  847  ALA ALA SER GLY LYS PHE SER SER ASP ARG THR ILE LYS          
SEQRES  64 A  847  GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER ASP          
SEQRES  65 A  847  LEU LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL ASN          
SEQRES  66 A  847  GLY ASN                                                      
SEQRES   1 B  847  MET ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG GLN          
SEQRES   2 B  847  ILE SER ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL ALA          
SEQRES   3 B  847  GLU LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE THR          
SEQRES   4 B  847  LEU VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP TYR          
SEQRES   5 B  847  TYR PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL          
SEQRES   6 B  847  GLY ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP LYS          
SEQRES   7 B  847  CYS PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE TYR          
SEQRES   8 B  847  MET GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU GLY          
SEQRES   9 B  847  LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU GLY          
SEQRES  10 B  847  LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA          
SEQRES  11 B  847  GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS          
SEQRES  12 B  847  PHE LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR          
SEQRES  13 B  847  GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN GLN          
SEQRES  14 B  847  LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP ASP          
SEQRES  15 B  847  TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG PRO          
SEQRES  16 B  847  GLU PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL GLU          
SEQRES  17 B  847  HIS THR ASN THR GLY THR LYS TRP ILE ASP THR GLN VAL          
SEQRES  18 B  847  VAL LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY TYR          
SEQRES  19 B  847  MET ASN ASN THR VAL ASN THR MET ARG LEU TRP SER ALA          
SEQRES  20 B  847  ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN VAL          
SEQRES  21 B  847  GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA          
SEQRES  22 B  847  GLU ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE          
SEQRES  23 B  847  PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE          
SEQRES  24 B  847  VAL VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE          
SEQRES  25 B  847  LYS ALA SER LYS PHE GLY SER THR ARG GLY ALA GLY THR          
SEQRES  26 B  847  VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN LEU          
SEQRES  27 B  847  ASN ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU MET          
SEQRES  28 B  847  ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER LYS          
SEQRES  29 B  847  ALA TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR ASN          
SEQRES  30 B  847  HIS THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL          
SEQRES  31 B  847  ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU ILE          
SEQRES  32 B  847  ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE VAL          
SEQRES  33 B  847  ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG MET          
SEQRES  34 B  847  SER LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN MET          
SEQRES  35 B  847  ALA HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN GLY          
SEQRES  36 B  847  VAL ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS VAL          
SEQRES  37 B  847  PHE LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE GLN          
SEQRES  38 B  847  ASN LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU LEU          
SEQRES  39 B  847  LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU LYS          
SEQRES  40 B  847  ILE GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU THR          
SEQRES  41 B  847  LYS LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU ARG          
SEQRES  42 B  847  GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE          
SEQRES  43 B  847  SER GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE ASN          
SEQRES  44 B  847  PRO SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE HIS          
SEQRES  45 B  847  GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE          
SEQRES  46 B  847  THR MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS LEU          
SEQRES  47 B  847  PHE VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA ALA          
SEQRES  48 B  847  PRO GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE          
SEQRES  49 B  847  THR SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET VAL          
SEQRES  50 B  847  GLY SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR ARG          
SEQRES  51 B  847  VAL SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP LEU          
SEQRES  52 B  847  SER GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY          
SEQRES  53 B  847  THR GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR          
SEQRES  54 B  847  ILE GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU          
SEQRES  55 B  847  GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET ARG          
SEQRES  56 B  847  ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR GLU          
SEQRES  57 B  847  ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS LEU          
SEQRES  58 B  847  VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO LYS          
SEQRES  59 B  847  GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU PHE          
SEQRES  60 B  847  TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU ALA          
SEQRES  61 B  847  TYR VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR MET          
SEQRES  62 B  847  ASN PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN ILE          
SEQRES  63 B  847  ALA ALA SER GLY LYS PHE SER SER ASP ARG THR ILE LYS          
SEQRES  64 B  847  GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER ASP          
SEQRES  65 B  847  LEU LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL ASN          
SEQRES  66 B  847  GLY ASN                                                      
HET    NBG  A 861      15                                                       
HET    NBG  B1861      15                                                       
HET    CP4  A 862      34                                                       
HET    PLP  A 860      15                                                       
HET    PLP  B1860      15                                                       
HET    MPD  B1902       8                                                       
HETNAM     NBG 1-N-ACETYL-BETA-D-GLUCOSAMINE                                    
HETNAM     CP4 BIS[5-CHLORO-1H-INDOL-2-YL-CARBONYL-AMINOETHYL]-                 
HETNAM   2 CP4  ETHYLENE GLYCOL                                                 
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETSYN     CP4 CP-526423; 1,2-BIS(2-(5-CHLOROINDOLE-2-CARBONYLAMINO)            
HETSYN   2 CP4  ETHOXY)ETHANE                                                   
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   3  NBG    2(C8 H15 N O6)                                               
FORMUL   5  CP4    C24 H24 CL2 N4 O4                                            
FORMUL   6  PLP    2(C8 H10 N O6 P)                                             
FORMUL   8  MPD    C6 H14 O2                                                    
FORMUL   9  HOH   *737(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 GLY A  260  ASP A  268  1                                   9    
HELIX    9   9 ASP A  268  ASN A  274  1                                   7    
HELIX   10  10 ILE A  275  ARG A  277  5                                   3    
HELIX   11  11 LYS A  289  ALA A  313  1                                  25    
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 LEU A  380  LEU A  384  5                                   5    
HELIX   17  17 VAL A  389  LEU A  396  1                                   8    
HELIX   18  18 LEU A  396  PHE A  418  1                                  23    
HELIX   19  19 ASP A  421  SER A  429  1                                   9    
HELIX   20  20 MET A  441  SER A  449  1                                   9    
HELIX   21  21 ALA A  456  LYS A  466  1                                  11    
HELIX   22  22 PHE A  468  GLU A  475  1                                   8    
HELIX   23  23 ASN A  496  GLY A  508  1                                  13    
HELIX   24  24 GLU A  509  LYS A  513  5                                   5    
HELIX   25  25 ASP A  514  LEU A  525  5                                  12    
HELIX   26  26 ASP A  527  TYR A  553  1                                  27    
HELIX   27  27 ARG A  575  ASP A  593  1                                  19    
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 ALA A  728  LEU A  735  1                                   8    
HELIX   37  37 LEU A  735  GLY A  748  1                                  14    
HELIX   38  38 PHE A  758  HIS A  768  1                                  11    
HELIX   39  39 LYS A  772  MET A  792  1                                  21    
HELIX   40  40 ASN A  793  ALA A  807  1                                  15    
HELIX   41  41 SER A  808  PHE A  811  5                                   4    
HELIX   42  42 SER A  812  ILE A  824  1                                  13    
HELIX   43  43 ASN B   23  THR B   38  1                                  16    
HELIX   44  44 THR B   47  CYS B   78  1                                  32    
HELIX   45  45 THR B   94  LEU B  102  1                                   9    
HELIX   46  46 LEU B  104  LEU B  115  1                                  12    
HELIX   47  47 ASP B  118  GLU B  124  1                                   7    
HELIX   48  48 GLY B  134  LEU B  150  1                                  17    
HELIX   49  49 PRO B  194  MET B  197  5                                   4    
HELIX   50  50 GLY B  260  ASP B  268  1                                   9    
HELIX   51  51 ASP B  268  ASN B  274  1                                   7    
HELIX   52  52 ILE B  275  ARG B  277  5                                   3    
HELIX   53  53 LYS B  289  ALA B  313  1                                  25    
HELIX   54  54 THR B  324  ASP B  327  5                                   4    
HELIX   55  55 ALA B  328  GLN B  332  1                                   5    
HELIX   56  56 LEU B  344  ILE B  356  1                                  13    
HELIX   57  57 PRO B  360  THR B  371  1                                  12    
HELIX   58  58 LEU B  380  LEU B  384  5                                   5    
HELIX   59  59 VAL B  389  LEU B  396  1                                   8    
HELIX   60  60 LEU B  396  PHE B  418  1                                  23    
HELIX   61  61 ASP B  421  SER B  429  1                                   9    
HELIX   62  62 MET B  441  SER B  449  1                                   9    
HELIX   63  63 ALA B  456  LYS B  466  1                                  11    
HELIX   64  64 PHE B  468  GLU B  475  1                                   8    
HELIX   65  65 ASN B  496  GLY B  508  1                                  13    
HELIX   66  66 GLU B  509  LYS B  513  5                                   5    
HELIX   67  67 ASP B  514  LEU B  525  5                                  12    
HELIX   68  68 ASP B  527  TYR B  553  1                                  27    
HELIX   69  69 HIS B  571  LYS B  574  5                                   4    
HELIX   70  70 ARG B  575  ASP B  593  1                                  19    
HELIX   71  71 TYR B  613  ASP B  633  1                                  21    
HELIX   72  72 VAL B  636  SER B  638  5                                   3    
HELIX   73  73 ARG B  649  ILE B  657  1                                   9    
HELIX   74  74 PRO B  658  THR B  660  5                                   3    
HELIX   75  75 THR B  676  ASN B  684  1                                   9    
HELIX   76  76 ALA B  695  GLY B  704  1                                  10    
HELIX   77  77 GLU B  705  LEU B  708  5                                   4    
HELIX   78  78 ARG B  714  GLY B  725  1                                  12    
HELIX   79  79 ALA B  728  LEU B  735  1                                   8    
HELIX   80  80 LEU B  735  GLY B  748  1                                  14    
HELIX   81  81 PHE B  758  HIS B  768  1                                  11    
HELIX   82  82 LYS B  772  MET B  792  1                                  21    
HELIX   83  83 ASN B  793  ALA B  807  1                                  15    
HELIX   84  84 SER B  808  PHE B  811  5                                   4    
HELIX   85  85 SER B  812  ILE B  824  1                                  13    
SHEET    1   A 9 PHE A 479  ASN A 481  0                                        
SHEET    2   A 9 ALA A 451  GLY A 454  1  O  VAL A 452   N  GLN A 480           
SHEET    3   A 9 PHE A 372  THR A 375  1  O  PHE A 372   N  ALA A 451           
SHEET    4   A 9 VAL A 333  ASN A 338  1  O  ILE A 335   N  ALA A 373           
SHEET    5   A 9 ARG A  81  LEU A  85  1  O  ARG A  81   N  ALA A 334           
SHEET    6   A 9 ALA A 154  ILE A 159  1  O  TYR A 155   N  TYR A  84           
SHEET    7   A 9 VAL A 238  ARG A 247  1  O  THR A 240   N  GLY A 156           
SHEET    8   A 9 GLN A 219  PRO A 231 -1  N  LEU A 222   O  ARG A 247           
SHEET    9   A 9 LYS A 191  SER A 192 -1  O  LYS A 191   N  ASP A 227           
SHEET    1   B 9 PHE A 479  ASN A 481  0                                        
SHEET    2   B 9 ALA A 451  GLY A 454  1  O  VAL A 452   N  GLN A 480           
SHEET    3   B 9 PHE A 372  THR A 375  1  O  PHE A 372   N  ALA A 451           
SHEET    4   B 9 VAL A 333  ASN A 338  1  O  ILE A 335   N  ALA A 373           
SHEET    5   B 9 ARG A  81  LEU A  85  1  O  ARG A  81   N  ALA A 334           
SHEET    6   B 9 ALA A 154  ILE A 159  1  O  TYR A 155   N  TYR A  84           
SHEET    7   B 9 VAL A 238  ARG A 247  1  O  THR A 240   N  GLY A 156           
SHEET    8   B 9 GLN A 219  PRO A 231 -1  N  LEU A 222   O  ARG A 247           
SHEET    9   B 9 LEU A 198  PHE A 202 -1  O  LEU A 198   N  ALA A 223           
SHEET    1   C 2 PHE A  89  GLY A  92  0                                        
SHEET    2   C 2 ALA A 129  LEU A 131 -1  N  ALA A 129   O  GLY A  92           
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  N  LEU A 662   O  PHE A 563           
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 B 479  ASN B 481  0                                        
SHEET    2   H 9 ALA B 451  GLY B 454  1  O  VAL B 452   N  GLN B 480           
SHEET    3   H 9 PHE B 372  THR B 375  1  O  PHE B 372   N  ALA B 451           
SHEET    4   H 9 VAL B 333  ASN B 338  1  O  ILE B 335   N  ALA B 373           
SHEET    5   H 9 ARG B  81  LEU B  85  1  O  ARG B  81   N  ALA B 334           
SHEET    6   H 9 ALA B 154  ILE B 159  1  O  TYR B 155   N  TYR B  84           
SHEET    7   H 9 VAL B 238  ARG B 247  1  O  THR B 240   N  GLY B 156           
SHEET    8   H 9 GLN B 219  PRO B 231 -1  N  LEU B 222   O  ARG B 247           
SHEET    9   H 9 LYS B 191  SER B 192 -1  O  LYS B 191   N  ASP B 227           
SHEET    1   I 9 PHE B 479  ASN B 481  0                                        
SHEET    2   I 9 ALA B 451  GLY B 454  1  O  VAL B 452   N  GLN B 480           
SHEET    3   I 9 PHE B 372  THR B 375  1  O  PHE B 372   N  ALA B 451           
SHEET    4   I 9 VAL B 333  ASN B 338  1  O  ILE B 335   N  ALA B 373           
SHEET    5   I 9 ARG B  81  LEU B  85  1  O  ARG B  81   N  ALA B 334           
SHEET    6   I 9 ALA B 154  ILE B 159  1  O  TYR B 155   N  TYR B  84           
SHEET    7   I 9 VAL B 238  ARG B 247  1  O  THR B 240   N  GLY B 156           
SHEET    8   I 9 GLN B 219  PRO B 231 -1  N  LEU B 222   O  ARG B 247           
SHEET    9   I 9 LEU B 198  PHE B 202 -1  O  LEU B 198   N  ALA B 223           
SHEET    1   J 2 PHE B  89  GLY B  92  0                                        
SHEET    2   J 2 ALA B 129  LEU B 131 -1  O  ALA B 129   N  GLY B  92           
SHEET    1   K 2 ASN B 167  ARG B 171  0                                        
SHEET    2   K 2 TRP B 174  GLU B 178 -1  O  TRP B 174   N  ARG B 171           
SHEET    1   L 2 LYS B 205  THR B 209  0                                        
SHEET    2   L 2 GLY B 212  ILE B 216 -1  N  GLY B 212   O  THR B 209           
SHEET    1   M 3 ARG B 386  PRO B 388  0                                        
SHEET    2   M 3 ARG B 438  ASN B 440 -1  N  ILE B 439   O  TRP B 387           
SHEET    3   M 3 ILE B 431  GLU B 432 -1  N  GLU B 432   O  ARG B 438           
SHEET    1   N 6 LEU B 640  LEU B 645  0                                        
SHEET    2   N 6 ARG B 601  GLY B 606  1  O  ARG B 601   N  LYS B 641           
SHEET    3   N 6 MET B 562  VAL B 567  1  O  MET B 562   N  THR B 602           
SHEET    4   N 6 LEU B 662  GLN B 665  1  N  LEU B 662   O  PHE B 563           
SHEET    5   N 6 LEU B 687  GLY B 690  1  O  LEU B 687   N  SER B 663           
SHEET    6   N 6 PHE B 709  ILE B 710  1  N  PHE B 709   O  THR B 688           
LINK         NZ  LYS A 680                 C4A PLP A 860     1555   1555  1.43  
LINK         NZ  LYS B 680                 C4A PLP B1860     1555   1555  1.42  
SITE     1 AC1 16 LEU A 136  ASN A 284  ASP A 339  HIS A 377                    
SITE     2 AC1 16 THR A 378  VAL A 455  ASN A 484  TYR A 573                    
SITE     3 AC1 16 GLU A 672  ALA A 673  SER A 674  GLY A 675                    
SITE     4 AC1 16 HOH A2075  HOH A2076  HOH A2240  HOH A2651                    
SITE     1 AC2 18 LEU B 136  LEU B 139  ASN B 284  ASP B 339                    
SITE     2 AC2 18 HIS B 377  THR B 378  VAL B 455  ASN B 484                    
SITE     3 AC2 18 TYR B 573  GLU B 672  ALA B 673  SER B 674                    
SITE     4 AC2 18 GLY B 675  HOH B2022  HOH B2144  HOH B2248                    
SITE     5 AC2 18 HOH B2585  HOH B2650                                          
SITE     1 AC3 26 THR A  38  VAL A  40  ARG A  60  LEU A  63                    
SITE     2 AC3 26 VAL A  64  TRP A  67  PRO A 188  TRP A 189                    
SITE     3 AC3 26 GLU A 190  LYS A 191  PRO A 229  HOH A2445                    
SITE     4 AC3 26 HOH A2522  HOH A2584  THR B  38  VAL B  40                    
SITE     5 AC3 26 ARG B  60  LEU B  63  VAL B  64  TRP B  67                    
SITE     6 AC3 26 PRO B 188  GLU B 190  LYS B 191  HOH B2161                    
SITE     7 AC3 26 HOH B2243  HOH B2730                                          
SITE     1 AC4 20 TYR A  90  GLY A 134  GLY A 135  TRP A 491                    
SITE     2 AC4 20 LYS A 568  LYS A 574  TYR A 648  ARG A 649                    
SITE     3 AC4 20 VAL A 650  GLU A 672  GLY A 675  THR A 676                    
SITE     4 AC4 20 GLY A 677  LYS A 680  HOH A2031  HOH A2032                    
SITE     5 AC4 20 HOH A2124  HOH A2197  HOH A2235  HOH A2282                    
SITE     1 AC5 16 TYR B  90  TRP B 491  LYS B 568  LYS B 574                    
SITE     2 AC5 16 TYR B 648  ARG B 649  VAL B 650  GLY B 675                    
SITE     3 AC5 16 THR B 676  GLY B 677  LYS B 680  HOH B2005                    
SITE     4 AC5 16 HOH B2092  HOH B2156  HOH B2165  HOH B2249                    
SITE     1 AC6  6 VAL A  40  VAL A  45  TRP B  67  ARG B 193                    
SITE     2 AC6  6 HOH B2014  HOH B2203                                          
CRYST1  123.314  123.314  122.319  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      0.008109  0.004682  0.000000        0.00000                         
SCALE2      0.000000  0.009364  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008175        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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