GenomeNet

Database: PDB
Entry: 4OMT
LinkDB: 4OMT
Original site: 4OMT 
HEADER    TRANSFERASE                             27-JAN-14   4OMT              
TITLE     CRYSTAL STRUCTURE OF HUMAN MUSCLE PHOSPHOFRUCTOKINASE (DISSOCIATED    
TITLE    2 HOMODIMER)                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 6-PHOSPHOFRUCTOKINASE, MUSCLE TYPE;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 8-755;                                        
COMPND   5 SYNONYM: PHOSPHOFRUCTO-1-KINASE ISOZYME A, PFK-A,                    
COMPND   6 PHOSPHOFRUCTOKINASE-M, PHOSPHOFRUCTOKINASE 1, PHOSPHOHEXOKINASE;     
COMPND   7 EC: 2.7.1.11;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PFKM, PFKX;                                                    
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: YEAST;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: HD114-8D;                                  
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PJJH71                                    
KEYWDS    HUMAN 6-PHOSPHOFRUCTOKINASE, 6-PHOSPHOFRUCTOKINASE ACTIVITY, FRUCTOSE 
KEYWDS   2 6-PHOSPHATE, TRANSFERASE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.KLOOS,N.STRAETER                                                    
REVDAT   3   10-DEC-14 4OMT    1       TITLE                                    
REVDAT   2   24-SEP-14 4OMT    1       JRNL                                     
REVDAT   1   14-MAY-14 4OMT    0                                                
JRNL        AUTH   M.KLOOS,A.BRUSER,J.KIRCHBERGER,T.SCHONEBERG,N.STRATER        
JRNL        TITL   CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF 
JRNL        TITL 2 HUMAN MUSCLE PHOSPHOFRUCTOKINASE, THE MAIN REGULATOR OF      
JRNL        TITL 3 GLYCOLYSIS.                                                  
JRNL        REF    ACTA CRYSTALLOGR F STRUCT     V.  70   578 2014              
JRNL        REF  2 BIOL COMMUN                                                  
JRNL        REFN                   ISSN 1744-3091                               
JRNL        PMID   24817713                                                     
JRNL        DOI    10.1107/S2053230X14008723                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    6.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 6.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.95                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.550                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 9802                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.242                           
REMARK   3   R VALUE            (WORKING SET) : 0.238                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 941                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.9562 - 11.4305    0.99     1279   119  0.3275 0.3529        
REMARK   3     2 11.4305 -  9.0943    1.00     1271   130  0.1884 0.2174        
REMARK   3     3  9.0943 -  7.9510    1.00     1259   144  0.1813 0.2379        
REMARK   3     4  7.9510 -  7.2269    1.00     1237   158  0.2272 0.2735        
REMARK   3     5  7.2269 -  6.7105    1.00     1268   144  0.2107 0.2815        
REMARK   3     6  6.7105 -  6.3158    1.00     1262   122  0.2439 0.2739        
REMARK   3     7  6.3158 -  6.0002    1.00     1285   124  0.2706 0.3355        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.810            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.000           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 222.67                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.92000                                              
REMARK   3    B22 (A**2) : 4.92000                                              
REMARK   3    B33 (A**2) : -15.95000                                            
REMARK   3    B12 (A**2) : 4.92000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.013           5813                                  
REMARK   3   ANGLE     :  1.446           7846                                  
REMARK   3   CHIRALITY :  0.093            885                                  
REMARK   3   PLANARITY :  0.006           1015                                  
REMARK   3   DIHEDRAL  : 17.376           2143                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4OMT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB084690.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91841                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 5537                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 6.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.950                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 11.600                             
REMARK 200  R MERGE                    (I) : 0.10600                            
REMARK 200  R SYM                      (I) : 0.11600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 6.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 6.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.10                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.46200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3O8N                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 80.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.6 M LINO3, 0.05 M NAF, 0.1 M SODIUM    
REMARK 280  ACETATE, PH 5.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+2/3                                            
REMARK 290       6555   X-Y,X,Z+1/3                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+2/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+1/3                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.66667            
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       44.33333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       88.66667            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       44.33333            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       88.66667            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       44.33333            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       88.66667            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       44.33333            
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 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     GLU A   756                                                      
REMARK 465     ILE A   757                                                      
REMARK 465     ASP A   758                                                      
REMARK 465     LEU A   759                                                      
REMARK 465     ASP A   760                                                      
REMARK 465     THR A   761                                                      
REMARK 465     SER A   762                                                      
REMARK 465     ASP A   763                                                      
REMARK 465     HIS A   764                                                      
REMARK 465     ALA A   765                                                      
REMARK 465     HIS A   766                                                      
REMARK 465     LEU A   767                                                      
REMARK 465     GLU A   768                                                      
REMARK 465     HIS A   769                                                      
REMARK 465     ILE A   770                                                      
REMARK 465     THR A   771                                                      
REMARK 465     ARG A   772                                                      
REMARK 465     LYS A   773                                                      
REMARK 465     ARG A   774                                                      
REMARK 465     SER A   775                                                      
REMARK 465     GLY A   776                                                      
REMARK 465     GLU A   777                                                      
REMARK 465     ALA A   778                                                      
REMARK 465     ALA A   779                                                      
REMARK 465     VAL A   780                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CZ   TYR A   103     CD2  LEU A   139              0.24            
REMARK 500   N    ASP A   237     CE   LYS A   269              0.61            
REMARK 500   CA   ASP A   237     NZ   LYS A   269              1.11            
REMARK 500   CE2  TYR A   103     CD2  LEU A   139              1.31            
REMARK 500   OH   TYR A   103     CD2  LEU A   139              1.35            
REMARK 500   O    ALA A     9     N    THR A    11              1.47            
REMARK 500   CE1  TYR A   103     CD2  LEU A   139              1.52            
REMARK 500   N    ASP A   237     NZ   LYS A   269              1.52            
REMARK 500   C    ASP A   236     CE   LYS A   269              1.58            
REMARK 500   CB   ASP A   237     NZ   LYS A   269              1.67            
REMARK 500   CZ   TYR A   103     CG   LEU A   139              1.72            
REMARK 500   CG2  THR A   275     OD2  ASP A   278              1.75            
REMARK 500   CA   ASP A   237     CE   LYS A   269              1.83            
REMARK 500   CG   ASP A   237     NZ   LYS A   269              1.95            
REMARK 500   OH   TYR A   103     CG   LEU A   139              2.02            
REMARK 500   N    ASP A   237     CD   LYS A   269              2.03            
REMARK 500   CE   MET A   186     NH1  ARG A   673              2.03            
REMARK 500   CG2  THR A   275     CG   ASP A   278              2.07            
REMARK 500   O    LEU A    99     CD2  TYR A   103              2.08            
REMARK 500   OD1  ASP A   237     NZ   LYS A   269              2.14            
REMARK 500   O    VAL A   609     N    HIS A   611              2.14            
REMARK 500   O    THR A    69     OG   SER A    72              2.16            
REMARK 500   O    THR A   250     OG   SER A   255              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CB   SER A   396     CB   SER A   396     4665     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PRO A 394   C     VAL A 395   N       0.253                       
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    LEU A  79   CA  -  CB  -  CG  ANGL. DEV. =  13.8 DEGREES          
REMARK 500    PRO A 394   CA  -  C   -  N   ANGL. DEV. = -18.1 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    ALA A   9      -96.67   -131.69                                   
REMARK 500    LYS A  10      -24.13     22.01                                   
REMARK 500    VAL A  34      -76.85    -36.98                                   
REMARK 500    THR A  44       32.47    -75.67                                   
REMARK 500    GLU A  53       77.04     59.58                                   
REMARK 500    ASP A  60      -75.44    -53.40                                   
REMARK 500    ALA A  87     -145.73   -114.54                                   
REMARK 500    ARG A  88       32.57   -151.30                                   
REMARK 500    GLU A 131       39.60    -91.17                                   
REMARK 500    LEU A 139       22.98    -75.48                                   
REMARK 500    ALA A 142        0.42   -166.80                                   
REMARK 500    LYS A 152       36.87   -146.96                                   
REMARK 500    SER A 153     -112.75    -62.09                                   
REMARK 500    SER A 154       24.78    -70.21                                   
REMARK 500    TYR A 155       71.25   -109.73                                   
REMARK 500    ILE A 165        5.32    -63.90                                   
REMARK 500    ASN A 167       17.33     57.01                                   
REMARK 500    THR A 195      -34.63   -138.40                                   
REMARK 500    ALA A 196       89.35    -61.44                                   
REMARK 500    SER A 198     -113.11    -75.72                                   
REMARK 500    MET A 208     -163.67    -60.81                                   
REMARK 500    TYR A 214      -76.20    -52.97                                   
REMARK 500    PRO A 235       62.68    -67.25                                   
REMARK 500    ASP A 236      126.48    -38.88                                   
REMARK 500    ASP A 237     -173.75     78.56                                   
REMARK 500    ASP A 238      104.49    -53.18                                   
REMARK 500    ARG A 253      -12.06    -49.02                                   
REMARK 500    ARG A 256      -73.44    -81.97                                   
REMARK 500    LYS A 269      -63.94    -22.60                                   
REMARK 500    HIS A 298       -1.29     63.84                                   
REMARK 500    SER A 337      140.06   -173.25                                   
REMARK 500    SER A 339      109.72   -172.49                                   
REMARK 500    ASN A 341       12.09     91.82                                   
REMARK 500    LYS A 365       15.50    -67.65                                   
REMARK 500    ARG A 376     -123.77     46.22                                   
REMARK 500    TRP A 382      -70.20    -48.33                                   
REMARK 500    HIS A 390      169.91    -44.74                                   
REMARK 500    ARG A 392     -109.15    -46.67                                   
REMARK 500    PRO A 394      179.67    -58.06                                   
REMARK 500    ALA A 418      -72.54    -55.70                                   
REMARK 500    VAL A 419      -54.33    -28.67                                   
REMARK 500    ARG A 424      -70.89    -45.92                                   
REMARK 500    ASP A 438       65.94     70.99                                   
REMARK 500    GLU A 441        1.90    -58.74                                   
REMARK 500    ALA A 444      -85.04    -51.51                                   
REMARK 500    GLN A 447       72.72    -67.44                                   
REMARK 500    THR A 472      146.74    -38.60                                   
REMARK 500    LYS A 476       -4.92    -52.01                                   
REMARK 500    SER A 477       27.78   -143.53                                   
REMARK 500    ASN A 489       38.34     71.43                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      70 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    PRO A 394        -15.11                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3O8N   RELATED DB: PDB                                   
REMARK 900 MR MODEL                                                             
REMARK 900 RELATED ID: 3OPY   RELATED DB: PDB                                   
DBREF  4OMT A    1   780  UNP    P08237   K6PF_HUMAN       1    780             
SEQRES   1 A  780  MET THR HIS GLU GLU HIS HIS ALA ALA LYS THR LEU GLY          
SEQRES   2 A  780  ILE GLY LYS ALA ILE ALA VAL LEU THR SER GLY GLY ASP          
SEQRES   3 A  780  ALA GLN GLY MET ASN ALA ALA VAL ARG ALA VAL VAL ARG          
SEQRES   4 A  780  VAL GLY ILE PHE THR GLY ALA ARG VAL PHE PHE VAL HIS          
SEQRES   5 A  780  GLU GLY TYR GLN GLY LEU VAL ASP GLY GLY ASP HIS ILE          
SEQRES   6 A  780  LYS GLU ALA THR TRP GLU SER VAL SER MET MET LEU GLN          
SEQRES   7 A  780  LEU GLY GLY THR VAL ILE GLY SER ALA ARG CYS LYS ASP          
SEQRES   8 A  780  PHE ARG GLU ARG GLU GLY ARG LEU ARG ALA ALA TYR ASN          
SEQRES   9 A  780  LEU VAL LYS ARG GLY ILE THR ASN LEU CYS VAL ILE GLY          
SEQRES  10 A  780  GLY ASP GLY SER LEU THR GLY ALA ASP THR PHE ARG SER          
SEQRES  11 A  780  GLU TRP SER ASP LEU LEU SER ASP LEU GLN LYS ALA GLY          
SEQRES  12 A  780  LYS ILE THR ASP GLU GLU ALA THR LYS SER SER TYR LEU          
SEQRES  13 A  780  ASN ILE VAL GLY LEU VAL GLY SER ILE ASP ASN ASP PHE          
SEQRES  14 A  780  CYS GLY THR ASP MET THR ILE GLY THR ASP SER ALA LEU          
SEQRES  15 A  780  HIS ARG ILE MET GLU ILE VAL ASP ALA ILE THR THR THR          
SEQRES  16 A  780  ALA GLN SER HIS GLN ARG THR PHE VAL LEU GLU VAL MET          
SEQRES  17 A  780  GLY ARG HIS CYS GLY TYR LEU ALA LEU VAL THR SER LEU          
SEQRES  18 A  780  SER CYS GLY ALA ASP TRP VAL PHE ILE PRO GLU CYS PRO          
SEQRES  19 A  780  PRO ASP ASP ASP TRP GLU GLU HIS LEU CYS ARG ARG LEU          
SEQRES  20 A  780  SER GLU THR ARG THR ARG GLY SER ARG LEU ASN ILE ILE          
SEQRES  21 A  780  ILE VAL ALA GLU GLY ALA ILE ASP LYS ASN GLY LYS PRO          
SEQRES  22 A  780  ILE THR SER GLU ASP ILE LYS ASN LEU VAL VAL LYS ARG          
SEQRES  23 A  780  LEU GLY TYR ASP THR ARG VAL THR VAL LEU GLY HIS VAL          
SEQRES  24 A  780  GLN ARG GLY GLY THR PRO SER ALA PHE ASP ARG ILE LEU          
SEQRES  25 A  780  GLY SER ARG MET GLY VAL GLU ALA VAL MET ALA LEU LEU          
SEQRES  26 A  780  GLU GLY THR PRO ASP THR PRO ALA CYS VAL VAL SER LEU          
SEQRES  27 A  780  SER GLY ASN GLN ALA VAL ARG LEU PRO LEU MET GLU CYS          
SEQRES  28 A  780  VAL GLN VAL THR LYS ASP VAL THR LYS ALA MET ASP GLU          
SEQRES  29 A  780  LYS LYS PHE ASP GLU ALA LEU LYS LEU ARG GLY ARG SER          
SEQRES  30 A  780  PHE MET ASN ASN TRP GLU VAL TYR LYS LEU LEU ALA HIS          
SEQRES  31 A  780  VAL ARG PRO PRO VAL SER LYS SER GLY SER HIS THR VAL          
SEQRES  32 A  780  ALA VAL MET ASN VAL GLY ALA PRO ALA ALA GLY MET ASN          
SEQRES  33 A  780  ALA ALA VAL ARG SER THR VAL ARG ILE GLY LEU ILE GLN          
SEQRES  34 A  780  GLY ASN ARG VAL LEU VAL VAL HIS ASP GLY PHE GLU GLY          
SEQRES  35 A  780  LEU ALA LYS GLY GLN ILE GLU GLU ALA GLY TRP SER TYR          
SEQRES  36 A  780  VAL GLY GLY TRP THR GLY GLN GLY GLY SER LYS LEU GLY          
SEQRES  37 A  780  THR LYS ARG THR LEU PRO LYS LYS SER PHE GLU GLN ILE          
SEQRES  38 A  780  SER ALA ASN ILE THR LYS PHE ASN ILE GLN GLY LEU VAL          
SEQRES  39 A  780  ILE ILE GLY GLY PHE GLU ALA TYR THR GLY GLY LEU GLU          
SEQRES  40 A  780  LEU MET GLU GLY ARG LYS GLN PHE ASP GLU LEU CYS ILE          
SEQRES  41 A  780  PRO PHE VAL VAL ILE PRO ALA THR VAL SER ASN ASN VAL          
SEQRES  42 A  780  PRO GLY SER ASP PHE SER VAL GLY ALA ASP THR ALA LEU          
SEQRES  43 A  780  ASN THR ILE CYS THR THR CYS ASP ARG ILE LYS GLN SER          
SEQRES  44 A  780  ALA ALA GLY THR LYS ARG ARG VAL PHE ILE ILE GLU THR          
SEQRES  45 A  780  MET GLY GLY TYR CYS GLY TYR LEU ALA THR MET ALA GLY          
SEQRES  46 A  780  LEU ALA ALA GLY ALA ASP ALA ALA TYR ILE PHE GLU GLU          
SEQRES  47 A  780  PRO PHE THR ILE ARG ASP LEU GLN ALA ASN VAL GLU HIS          
SEQRES  48 A  780  LEU VAL GLN LYS MET LYS THR THR VAL LYS ARG GLY LEU          
SEQRES  49 A  780  VAL LEU ARG ASN GLU LYS CYS ASN GLU ASN TYR THR THR          
SEQRES  50 A  780  ASP PHE ILE PHE ASN LEU TYR SER GLU GLU GLY LYS GLY          
SEQRES  51 A  780  ILE PHE ASP SER ARG LYS ASN VAL LEU GLY HIS MET GLN          
SEQRES  52 A  780  GLN GLY GLY SER PRO THR PRO PHE ASP ARG ASN PHE ALA          
SEQRES  53 A  780  THR LYS MET GLY ALA LYS ALA MET ASN TRP MET SER GLY          
SEQRES  54 A  780  LYS ILE LYS GLU SER TYR ARG ASN GLY ARG ILE PHE ALA          
SEQRES  55 A  780  ASN THR PRO ASP SER GLY CYS VAL LEU GLY MET ARG LYS          
SEQRES  56 A  780  ARG ALA LEU VAL PHE GLN PRO VAL ALA GLU LEU LYS ASP          
SEQRES  57 A  780  GLN THR ASP PHE GLU HIS ARG ILE PRO LYS GLU GLN TRP          
SEQRES  58 A  780  TRP LEU LYS LEU ARG PRO ILE LEU LYS ILE LEU ALA LYS          
SEQRES  59 A  780  TYR GLU ILE ASP LEU ASP THR SER ASP HIS ALA HIS LEU          
SEQRES  60 A  780  GLU HIS ILE THR ARG LYS ARG SER GLY GLU ALA ALA VAL          
HELIX    1   1 GLY A   29  THR A   44  1                                  16    
HELIX    2   2 TYR A   55  GLY A   61  1                                   7    
HELIX    3   3 GLU A   94  GLY A  109  1                                  16    
HELIX    4   4 GLY A  118  GLU A  131  1                                  14    
HELIX    5   5 SER A  133  LEU A  139  1                                   7    
HELIX    6   6 GLY A  177  THR A  193  1                                  17    
HELIX    7   7 GLY A  213  GLY A  224  1                                  12    
HELIX    8   8 TRP A  239  ARG A  253  1                                  15    
HELIX    9   9 THR A  275  LEU A  287  1                                  13    
HELIX   10  10 SER A  306  GLU A  326  1                                  21    
HELIX   11  11 LEU A  348  LYS A  356  1                                   9    
HELIX   12  12 LYS A  356  GLU A  364  1                                   9    
HELIX   13  13 LYS A  366  GLY A  375  1                                  10    
HELIX   14  14 ARG A  376  HIS A  390  1                                  15    
HELIX   15  15 GLY A  414  GLN A  429  1                                  16    
HELIX   16  16 PHE A  440  GLY A  446  1                                   7    
HELIX   17  17 GLY A  452  GLY A  457  5                                   6    
HELIX   18  18 PRO A  474  LYS A  476  5                                   3    
HELIX   19  19 SER A  477  PHE A  488  1                                  12    
HELIX   20  20 GLY A  498  PHE A  515  1                                  18    
HELIX   21  21 GLY A  541  LYS A  557  1                                  17    
HELIX   22  22 GLY A  578  ALA A  588  1                                  11    
HELIX   23  23 THR A  601  LYS A  617  1                                  17    
HELIX   24  24 THR A  636  GLY A  648  1                                  13    
HELIX   25  25 THR A  669  SER A  694  1                                  26    
HELIX   26  26 THR A  704  ASP A  706  5                                   3    
HELIX   27  27 VAL A  723  LYS A  727  1                                   5    
HELIX   28  28 GLN A  740  LYS A  744  5                                   5    
HELIX   29  29 LEU A  745  ALA A  753  1                                   9    
SHEET    1   A 4 ARG A  47  PHE A  49  0                                        
SHEET    2   A 4 ALA A  17  THR A  22  1  N  ILE A  18   O  PHE A  49           
SHEET    3   A 4 ASN A 112  GLY A 117  1  O  CYS A 114   N  ALA A  19           
SHEET    4   A 4 ASN A 157  VAL A 162  1  O  ASN A 157   N  LEU A 113           
SHEET    1   B 4 TRP A 227  PHE A 229  0                                        
SHEET    2   B 4 ASN A 258  VAL A 262  1  O  ILE A 261   N  TRP A 227           
SHEET    3   B 4 THR A 202  GLU A 206  1  N  LEU A 205   O  VAL A 262           
SHEET    4   B 4 THR A 291  THR A 294  1  O  THR A 294   N  GLU A 206           
SHEET    1   C 2 CYS A 334  SER A 339  0                                        
SHEET    2   C 2 GLN A 342  PRO A 347 -1  O  VAL A 344   N  SER A 337           
SHEET    1   D 7 ILE A 448  GLU A 450  0                                        
SHEET    2   D 7 ARG A 432  VAL A 436 -1  N  VAL A 435   O  GLU A 449           
SHEET    3   D 7 THR A 402  VAL A 408  1  N  VAL A 403   O  LEU A 434           
SHEET    4   D 7 LEU A 493  GLY A 497  1  O  ILE A 496   N  MET A 406           
SHEET    5   D 7 PHE A 522  PRO A 526  1  O  VAL A 523   N  ILE A 495           
SHEET    6   D 7 GLY A 708  ARG A 714  1  O  CYS A 709   N  VAL A 524           
SHEET    7   D 7 ALA A 717  PRO A 722 -1  O  VAL A 719   N  GLY A 712           
SHEET    1   E 4 ALA A 592  TYR A 594  0                                        
SHEET    2   E 4 ARG A 622  ASN A 628  1  O  LEU A 626   N  ALA A 592           
SHEET    3   E 4 ARG A 566  THR A 572  1  N  PHE A 568   O  GLY A 623           
SHEET    4   E 4 ASP A 653  VAL A 658  1  O  ASP A 653   N  VAL A 567           
SHEET    1   F 2 THR A 730  ASP A 731  0                                        
SHEET    2   F 2 ILE A 736  PRO A 737 -1  O  ILE A 736   N  ASP A 731           
CISPEP   1 ALA A    8    ALA A    9          0         0.07                     
CISPEP   2 ARG A  392    PRO A  393          0       -21.13                     
CRYST1  229.700  229.700  133.000  90.00  90.00 120.00 P 62 2 2     12          
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      0.004354  0.002513  0.000000        0.00000                         
SCALE2      0.000000  0.005027  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007519        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system