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Database: PDB
Entry: 2PFK
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HEADER    TRANSFERASE(PHOSPHOTRANSFERASE)         25-JAN-88   2PFK              
TITLE     THE CRYSTAL STRUCTURE OF UNLIGANDED PHOSPHOFRUCTOKINASE FROM          
TITLE    2 ESCHERICHIA COLI                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 6-PHOSPHOFRUCTOKINASE ISOZYME I;                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 2.7.1.11;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562                                                  
KEYWDS    TRANSFERASE(PHOSPHOTRANSFERASE)                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.R.RYPNIEWSKI,P.R.EVANS                                              
REVDAT   7   13-JUL-11 2PFK    1       VERSN                                    
REVDAT   6   24-FEB-09 2PFK    1       VERSN                                    
REVDAT   5   01-APR-03 2PFK    1       JRNL                                     
REVDAT   4   15-OCT-92 2PFK    1       SEQRES                                   
REVDAT   3   15-JUL-90 2PFK    1       JRNL                                     
REVDAT   2   19-APR-89 2PFK    1       REMARK                                   
REVDAT   1   09-JAN-89 2PFK    0                                                
JRNL        AUTH   W.R.RYPNIEWSKI,P.R.EVANS                                     
JRNL        TITL   CRYSTAL STRUCTURE OF UNLIGANDED PHOSPHOFRUCTOKINASE FROM     
JRNL        TITL 2 ESCHERICHIA COLI.                                            
JRNL        REF    J.MOL.BIOL.                   V. 207   805 1989              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   2527305                                                      
JRNL        DOI    10.1016/0022-2836(89)90246-5                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   Y.SHIRAKIHARA,P.R.EVANS                                      
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM 
REMARK   1  TITL 2 ESCHERICHIA COLI WITH ITS REACTION PRODUCTS                  
REMARK   1  REF    J.MOL.BIOL.                   V. 204   973 1988              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   P.R.EVANS,G.W.FARRANTS,M.C.LAWRENCE                          
REMARK   1  TITL   CRYSTALLOGRAPHIC STRUCTURE OF ALLOSTERICALLY INHIBITED       
REMARK   1  TITL 2 PHOSPHOFRUCTOKINASE AT 7 ANGSTROMS RESOLUTION                
REMARK   1  REF    J.MOL.BIOL.                   V. 191   713 1986              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   H.W.HELLINGA,P.R.EVANS                                       
REMARK   1  TITL   NUCLEOTIDE SEQUENCE AND HIGH-LEVEL EXPRESSION OF THE MAJOR   
REMARK   1  TITL 2 ESCHERICHIA COLI PHOSPHOFRUCTOKINASE                         
REMARK   1  REF    EUR.J.BIOCHEM.                V. 149   363 1985              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   P.R.EVANS,G.W.FARRANTS,P.J.HUDSON                            
REMARK   1  TITL   PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL                   
REMARK   1  REF    PHILOS.TRANS.R.SOC.LONDON,    V. 293    53 1981              
REMARK   1  REF  2 SER.B                                                        
REMARK   1  REFN                   ISSN 0080-4622                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   P.R.EVANS,P.J.HUDSON                                         
REMARK   1  TITL   STRUCTURE AND CONTROL OF PHOSPHOFRUCTOKINASE FROM BACILLUS   
REMARK   1  TITL 2 STEAROTHERMOPHILUS                                           
REMARK   1  REF    NATURE                        V. 279   500 1979              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   P.R.EVANS,P.J.HUDSON                                         
REMARK   1  TITL   THE THREE-DIMENSIONAL STRUCTURE OF PHOSPHOFRUCTOKINASE FROM  
REMARK   1  TITL 2 BACILLUS STEAROTHERMOPHILUS                                  
REMARK   1  REF    PROC.FEBS MEET.               V.  52   349 1978              
REMARK   1  REFN                   ISSN 0071-4402                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9024                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 347                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.012 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.042 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  THE SPACE GROUP HAS BEEN CONSIDERED AS C 21, I.E. C 2 WITH          
REMARK   3  THE ORIGIN ON A 21 AXIS.  THIS IS THE SAME AS P 21 PLUS THE         
REMARK   3  C-CENTERING.  THE COORDINATES IN THIS ENTRY ARE IN THE              
REMARK   3  A*, B, C ORTHOGONAL COORDINATE FRAME.  THE CRYSTALLOGRAPHIC         
REMARK   3  SYMMETRY OPERATIONS ARE (X, Y, Z), (-X, 1/2+Y, -Z), (1/2+X,         
REMARK   3  1/2+Y, Z), AND (1/2-X, Y, -Z).  THE ASYMMETRIC UNIT                 
REMARK   3  CONTAINS TWO HALF-TETRAMERS, I. E. THERE ARE TWO DIFFERENT          
REMARK   3  SORTS OF TETRAMERS WHICH SIT ON DIFFERENT CRYSTALLOGRAPHIC          
REMARK   3  DYAD AXES, AT (-1/4, 0, 0) AND (1/4, 0, 1/2).  THUS THERE           
REMARK   3  ARE FOUR DIFFERENT SUBUNITS IN THE UNIT CELL.  THESE                
REMARK   3  SUBUNITS HAVE BEEN ASSIGNED CHAIN IDENTIFIERS A, B, C, AND          
REMARK   3  D.  SUBUNITS A AND B ARE RELATED BY A PSEUDO-DYAD.  THE             
REMARK   3  TRANSFORMATION PRESENTED ON THE *MTRIX 1* RECORDS BELOW             
REMARK   3  WILL YIELD COORDINATES FOR CHAIN B WHEN APPLIED TO CHAIN A          
REMARK   3  AND VICE VERSA.  SUBUNITS C AND D ARE RELATED BY A                  
REMARK   3  PSEUDO-DYAD.  THE TRANSFORMATION PRESENTED ON THE *MTRIX 2*         
REMARK   3  RECORDS BELOW WILL YIELD COORDINATES FOR CHAIN D WHEN               
REMARK   3  APPLIED TO CHAIN C AND VICE VERSA.  TO GENERATE A TETRAMER          
REMARK   3  FROM SUBUNITS A AND B ONE MUST APPLY THE FOLLOWING                  
REMARK   3  CRYSTALLOGRAPHIC SYMMETRY OPERATION TO THE COORDINATES              
REMARK   3  PRESENTED BELOW FOR CHAINS A AND B -                                
REMARK   3                                                                      
REMARK   3     -1.0      0.0      0.0               -77.53963                   
REMARK   3      0.0      1.0      0.0                 0.0                       
REMARK   3      0.0      0.0     -1.0                42.68050                   
REMARK   3                                                                      
REMARK   3  TO GENERATE A TETRAMER FROM SUBUNITS C AND D ONE MUST               
REMARK   3  APPLY THE FOLLOWING CRYSTALLOGRAPHIC SYMMETRY OPERATION TO          
REMARK   3  THE COORDINATES PRESENTED BELOW FOR CHAINS C AND D -                
REMARK   3                                                                      
REMARK   3     -1.0      0.0      0.0                77.53963                   
REMARK   3      0.0      1.0      0.0                 0.0                       
REMARK   3      0.0      0.0     -1.0               111.28951                   
REMARK   3                                                                      
REMARK   3  THE TETRAMER FORMED FROM SUBUNITS A AND B IS CENTERED AT            
REMARK   3  (-1/4, 0, 0) AND THE TETRAMER FORMED FROM SUBUNITS C AND D          
REMARK   3  IS CENTERED AT (1/4, 20.89/66.4, 1/2).  THE SUBUNITS ARE            
REMARK   3  ALL SIMILAR IN CONFORMATION.  THE TRANSFORMATION PRESENTED          
REMARK   3  ON THE *MTRIX 3* RECORDS BELOW WILL YIELD COORDINATES FOR           
REMARK   3  CHAIN C WHEN APPLIED TO CHAIN A.  ALL OTHER                         
REMARK   3  TRANSFORMATIONS BETWEEN CHAINS CAN BE GENERATED FROM THE            
REMARK   3  GIVEN TRANSFORMATIONS.                                              
REMARK   4                                                                      
REMARK   4 2PFK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 285                                                                      
REMARK 285 THE ENTRY COORDINATES                                                
REMARK 285 ARE NOT PRESENTED IN THE STANDARD CRYSTAL FRAME.                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y,-Z                                             
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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       33.20053            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       77.55545            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.20053            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      -42.63520            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       77.55545            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000      -42.63520            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       77.55545            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -42.63520            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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       77.55545            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      111.35310            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 365  LIES ON A SPECIAL POSITION.                          
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     GLU A   301                                                      
REMARK 465     ASN A   302                                                      
REMARK 465     MET A   303                                                      
REMARK 465     LYS A   304                                                      
REMARK 465     ARG A   305                                                      
REMARK 465     PRO A   306                                                      
REMARK 465     PHE A   307                                                      
REMARK 465     LYS A   308                                                      
REMARK 465     GLY A   309                                                      
REMARK 465     ASP A   310                                                      
REMARK 465     TRP A   311                                                      
REMARK 465     LEU A   312                                                      
REMARK 465     ASP A   313                                                      
REMARK 465     CYS A   314                                                      
REMARK 465     ALA A   315                                                      
REMARK 465     LYS A   316                                                      
REMARK 465     LYS A   317                                                      
REMARK 465     LEU A   318                                                      
REMARK 465     TYR A   319                                                      
REMARK 465     GLU B   301                                                      
REMARK 465     ASN B   302                                                      
REMARK 465     MET B   303                                                      
REMARK 465     LYS B   304                                                      
REMARK 465     ARG B   305                                                      
REMARK 465     PRO B   306                                                      
REMARK 465     PHE B   307                                                      
REMARK 465     LYS B   308                                                      
REMARK 465     GLY B   309                                                      
REMARK 465     ASP B   310                                                      
REMARK 465     TRP B   311                                                      
REMARK 465     LEU B   312                                                      
REMARK 465     ASP B   313                                                      
REMARK 465     CYS B   314                                                      
REMARK 465     ALA B   315                                                      
REMARK 465     LYS B   316                                                      
REMARK 465     LYS B   317                                                      
REMARK 465     LEU B   318                                                      
REMARK 465     TYR B   319                                                      
REMARK 465     ASN C   302                                                      
REMARK 465     MET C   303                                                      
REMARK 465     LYS C   304                                                      
REMARK 465     ARG C   305                                                      
REMARK 465     PRO C   306                                                      
REMARK 465     PHE C   307                                                      
REMARK 465     LYS C   308                                                      
REMARK 465     GLY C   309                                                      
REMARK 465     ASP C   310                                                      
REMARK 465     TRP C   311                                                      
REMARK 465     LEU C   312                                                      
REMARK 465     ASP C   313                                                      
REMARK 465     CYS C   314                                                      
REMARK 465     ALA C   315                                                      
REMARK 465     LYS C   316                                                      
REMARK 465     LYS C   317                                                      
REMARK 465     LEU C   318                                                      
REMARK 465     TYR C   319                                                      
REMARK 465     ARG D   305                                                      
REMARK 465     PRO D   306                                                      
REMARK 465     PHE D   307                                                      
REMARK 465     LYS D   308                                                      
REMARK 465     GLY D   309                                                      
REMARK 465     ASP D   310                                                      
REMARK 465     TRP D   311                                                      
REMARK 465     LEU D   312                                                      
REMARK 465     ASP D   313                                                      
REMARK 465     CYS D   314                                                      
REMARK 465     ALA D   315                                                      
REMARK 465     LYS D   316                                                      
REMARK 465     LYS D   317                                                      
REMARK 465     LEU D   318                                                      
REMARK 465     TYR D   319                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     TYR A  55    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     ARG A  72    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 131    CG   CD   CE   NZ                                   
REMARK 470     GLU A 195    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 213    CE   NZ                                             
REMARK 470     LYS B   2    CE   NZ                                             
REMARK 470     TYR B  55    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     ARG B  72    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B  77    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B  79    CD   OE1  OE2                                       
REMARK 470     GLU B  87    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 195    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 211    CB   CG   CD   CE   NZ                              
REMARK 470     LYS B 213    CE   NZ                                             
REMARK 470     GLN B 290    CG   CD   OE1  NE2                                  
REMARK 470     ILE B 300    CG1  CG2  CD1                                       
REMARK 470     MET C   0    CB   CG   SD   CE                                   
REMARK 470     LYS C   2    CD   CE   NZ                                        
REMARK 470     TYR C  55    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG C  72    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C  77    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 301    CA   C    O    CB   CG   CD   OE1                   
REMARK 470     GLU C 301    OE2                                                 
REMARK 470     MET D   0    N    CB   CG   SD   CE                              
REMARK 470     LYS D   2    CD   CE   NZ                                        
REMARK 470     ARG D  72    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D  77    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 211    CE   NZ                                             
REMARK 470     LYS D 213    CD   CE   NZ                                        
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   O    HOH D   389     O    HOH D   389     4556     1.95            
REMARK 500   NZ   LYS C   236     CD2  HIS D   232     4546     2.07            
REMARK 500   OH   TYR A   279     OE2  GLU C    87     4556     2.10            
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    LYS A   2   CA  -  CB  -  CG  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    ARG A  21   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG A  25   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG A  48   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    GLN A  51   CA  -  CB  -  CG  ANGL. DEV. =  18.3 DEGREES          
REMARK 500    ASP A  78   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    GLU A  79   CA  -  CB  -  CG  ANGL. DEV. =  13.7 DEGREES          
REMARK 500    ARG A  92   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ASP A 103   CA  -  CB  -  CG  ANGL. DEV. =  17.7 DEGREES          
REMARK 500    ARG A 111   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    GLY A 116   C   -  N   -  CA  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    ASP A 129   CB  -  CG  -  OD2 ANGL. DEV. =  -9.5 DEGREES          
REMARK 500    TYR A 135   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG A 152   CG  -  CD  -  NE  ANGL. DEV. = -16.0 DEGREES          
REMARK 500    ARG A 152   NE  -  CZ  -  NH1 ANGL. DEV. =   7.7 DEGREES          
REMARK 500    ARG A 152   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    ARG A 154   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG A 154   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ASP A 155   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    SER A 158   CB  -  CA  -  C   ANGL. DEV. =  12.2 DEGREES          
REMARK 500    SER A 158   N   -  CA  -  CB  ANGL. DEV. = -11.2 DEGREES          
REMARK 500    ARG A 162   CD  -  NE  -  CZ  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ASP A 175   CB  -  CG  -  OD1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG A 198   CA  -  CB  -  CG  ANGL. DEV. =  18.2 DEGREES          
REMARK 500    ARG A 240   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A 240   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A 243   CD  -  NE  -  CZ  ANGL. DEV. =   8.9 DEGREES          
REMARK 500    ARG A 243   NE  -  CZ  -  NH1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG A 243   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG A 252   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 266   CD  -  NE  -  CZ  ANGL. DEV. =  31.7 DEGREES          
REMARK 500    ASP B  12   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG B  21   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG B  21   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG B  25   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG B  25   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG B  48   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ASP B  59   N   -  CA  -  CB  ANGL. DEV. = -12.1 DEGREES          
REMARK 500    ARG B  92   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    TYR B 106   CB  -  CG  -  CD1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG B 111   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ASP B 151   CB  -  CG  -  OD1 ANGL. DEV. =  11.0 DEGREES          
REMARK 500    ASP B 151   CB  -  CG  -  OD2 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ARG B 152   CD  -  NE  -  CZ  ANGL. DEV. =  28.4 DEGREES          
REMARK 500    ARG B 152   NE  -  CZ  -  NH1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG B 152   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    ARG B 162   NH1 -  CZ  -  NH2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG B 162   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    GLU B 199   C   -  N   -  CA  ANGL. DEV. =  15.4 DEGREES          
REMARK 500    ALA B 231   CB  -  CA  -  C   ANGL. DEV. =   9.3 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     126 ANGLE DEVIATIONS.                             
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    GLU A  75        0.40    -62.18                                   
REMARK 500    GLU A 114      -72.32    -52.47                                   
REMARK 500    MET A 115       13.84    -50.62                                   
REMARK 500    HIS A 249       -1.08    -57.22                                   
REMARK 500    ASN A 288       50.62     39.54                                   
REMARK 500    PHE B  73       77.28   -152.39                                   
REMARK 500    PHE C  73       71.03   -152.93                                   
REMARK 500    ARG C 171      -36.71    -39.23                                   
REMARK 500    LYS C 211       36.63    -72.01                                   
REMARK 500    GLU C 289        1.50     82.54                                   
REMARK 500    THR D 125      137.97   -173.65                                   
REMARK 500    ASN D 128       -0.70     71.98                                   
REMARK 500    ASP D 129       51.04    -68.49                                   
REMARK 500    LYS D 211        4.30    -66.03                                   
REMARK 500    GLU D 289       19.54     58.88                                   
REMARK 500    GLU D 301      -61.46    -93.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG D 152         0.09    SIDE CHAIN                              
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    ILE C 300        -19.10                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    HIS A 249        22.7      L          L   OUTSIDE RANGE           
REMARK 500    HIS B 249        23.9      L          L   OUTSIDE RANGE           
REMARK 500    GLU C  79        22.9      L          L   OUTSIDE RANGE           
REMARK 500    ARG C 171        22.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2PFK A    0   319  PIR    KIECFA   KIECFA           1    320             
DBREF  2PFK B    0   319  PIR    KIECFA   KIECFA           1    320             
DBREF  2PFK C    0   319  PIR    KIECFA   KIECFA           1    320             
DBREF  2PFK D    0   319  PIR    KIECFA   KIECFA           1    320             
SEQRES   1 A  320  MET ILE LYS LYS ILE GLY VAL LEU THR SER GLY GLY ASP          
SEQRES   2 A  320  ALA PRO GLY MET ASN ALA ALA ILE ARG GLY VAL VAL ARG          
SEQRES   3 A  320  SER ALA LEU THR GLU GLY LEU GLU VAL MET GLY ILE TYR          
SEQRES   4 A  320  ASP GLY TYR LEU GLY LEU TYR GLU ASP ARG MET VAL GLN          
SEQRES   5 A  320  LEU ASP ARG TYR SER VAL SER ASP MET ILE ASN ARG GLY          
SEQRES   6 A  320  GLY THR PHE LEU GLY SER ALA ARG PHE PRO GLU PHE ARG          
SEQRES   7 A  320  ASP GLU ASN ILE ARG ALA VAL ALA ILE GLU ASN LEU LYS          
SEQRES   8 A  320  LYS ARG GLY ILE ASP ALA LEU VAL VAL ILE GLY GLY ASP          
SEQRES   9 A  320  GLY SER TYR MET GLY ALA MET ARG LEU THR GLU MET GLY          
SEQRES  10 A  320  PHE PRO CYS ILE GLY LEU PRO GLY THR ILE ASP ASN ASP          
SEQRES  11 A  320  ILE LYS GLY THR ASP TYR THR ILE GLY PHE PHE THR ALA          
SEQRES  12 A  320  LEU SER THR VAL VAL GLU ALA ILE ASP ARG LEU ARG ASP          
SEQRES  13 A  320  THR SER SER SER HIS GLN ARG ILE SER VAL VAL GLU VAL          
SEQRES  14 A  320  MET GLY ARG TYR CYS GLY ASP LEU THR LEU ALA ALA ALA          
SEQRES  15 A  320  ILE ALA GLY GLY CYS GLU PHE VAL VAL VAL PRO GLU VAL          
SEQRES  16 A  320  GLU PHE SER ARG GLU ASP LEU VAL ASN GLU ILE LYS ALA          
SEQRES  17 A  320  GLY ILE ALA LYS GLY LYS LYS HIS ALA ILE VAL ALA ILE          
SEQRES  18 A  320  THR GLU HIS MET CYS ASP VAL ASP GLU LEU ALA HIS PHE          
SEQRES  19 A  320  ILE GLU LYS GLU THR GLY ARG GLU THR ARG ALA THR VAL          
SEQRES  20 A  320  LEU GLY HIS ILE GLN ARG GLY GLY SER PRO VAL PRO TYR          
SEQRES  21 A  320  ASP ARG ILE LEU ALA SER ARG MET GLY ALA TYR ALA ILE          
SEQRES  22 A  320  ASP LEU LEU LEU ALA GLY TYR GLY GLY ARG CYS VAL GLY          
SEQRES  23 A  320  ILE GLN ASN GLU GLN LEU VAL HIS HIS ASP ILE ILE ASP          
SEQRES  24 A  320  ALA ILE GLU ASN MET LYS ARG PRO PHE LYS GLY ASP TRP          
SEQRES  25 A  320  LEU ASP CYS ALA LYS LYS LEU TYR                              
SEQRES   1 B  320  MET ILE LYS LYS ILE GLY VAL LEU THR SER GLY GLY ASP          
SEQRES   2 B  320  ALA PRO GLY MET ASN ALA ALA ILE ARG GLY VAL VAL ARG          
SEQRES   3 B  320  SER ALA LEU THR GLU GLY LEU GLU VAL MET GLY ILE TYR          
SEQRES   4 B  320  ASP GLY TYR LEU GLY LEU TYR GLU ASP ARG MET VAL GLN          
SEQRES   5 B  320  LEU ASP ARG TYR SER VAL SER ASP MET ILE ASN ARG GLY          
SEQRES   6 B  320  GLY THR PHE LEU GLY SER ALA ARG PHE PRO GLU PHE ARG          
SEQRES   7 B  320  ASP GLU ASN ILE ARG ALA VAL ALA ILE GLU ASN LEU LYS          
SEQRES   8 B  320  LYS ARG GLY ILE ASP ALA LEU VAL VAL ILE GLY GLY ASP          
SEQRES   9 B  320  GLY SER TYR MET GLY ALA MET ARG LEU THR GLU MET GLY          
SEQRES  10 B  320  PHE PRO CYS ILE GLY LEU PRO GLY THR ILE ASP ASN ASP          
SEQRES  11 B  320  ILE LYS GLY THR ASP TYR THR ILE GLY PHE PHE THR ALA          
SEQRES  12 B  320  LEU SER THR VAL VAL GLU ALA ILE ASP ARG LEU ARG ASP          
SEQRES  13 B  320  THR SER SER SER HIS GLN ARG ILE SER VAL VAL GLU VAL          
SEQRES  14 B  320  MET GLY ARG TYR CYS GLY ASP LEU THR LEU ALA ALA ALA          
SEQRES  15 B  320  ILE ALA GLY GLY CYS GLU PHE VAL VAL VAL PRO GLU VAL          
SEQRES  16 B  320  GLU PHE SER ARG GLU ASP LEU VAL ASN GLU ILE LYS ALA          
SEQRES  17 B  320  GLY ILE ALA LYS GLY LYS LYS HIS ALA ILE VAL ALA ILE          
SEQRES  18 B  320  THR GLU HIS MET CYS ASP VAL ASP GLU LEU ALA HIS PHE          
SEQRES  19 B  320  ILE GLU LYS GLU THR GLY ARG GLU THR ARG ALA THR VAL          
SEQRES  20 B  320  LEU GLY HIS ILE GLN ARG GLY GLY SER PRO VAL PRO TYR          
SEQRES  21 B  320  ASP ARG ILE LEU ALA SER ARG MET GLY ALA TYR ALA ILE          
SEQRES  22 B  320  ASP LEU LEU LEU ALA GLY TYR GLY GLY ARG CYS VAL GLY          
SEQRES  23 B  320  ILE GLN ASN GLU GLN LEU VAL HIS HIS ASP ILE ILE ASP          
SEQRES  24 B  320  ALA ILE GLU ASN MET LYS ARG PRO PHE LYS GLY ASP TRP          
SEQRES  25 B  320  LEU ASP CYS ALA LYS LYS LEU TYR                              
SEQRES   1 C  320  MET ILE LYS LYS ILE GLY VAL LEU THR SER GLY GLY ASP          
SEQRES   2 C  320  ALA PRO GLY MET ASN ALA ALA ILE ARG GLY VAL VAL ARG          
SEQRES   3 C  320  SER ALA LEU THR GLU GLY LEU GLU VAL MET GLY ILE TYR          
SEQRES   4 C  320  ASP GLY TYR LEU GLY LEU TYR GLU ASP ARG MET VAL GLN          
SEQRES   5 C  320  LEU ASP ARG TYR SER VAL SER ASP MET ILE ASN ARG GLY          
SEQRES   6 C  320  GLY THR PHE LEU GLY SER ALA ARG PHE PRO GLU PHE ARG          
SEQRES   7 C  320  ASP GLU ASN ILE ARG ALA VAL ALA ILE GLU ASN LEU LYS          
SEQRES   8 C  320  LYS ARG GLY ILE ASP ALA LEU VAL VAL ILE GLY GLY ASP          
SEQRES   9 C  320  GLY SER TYR MET GLY ALA MET ARG LEU THR GLU MET GLY          
SEQRES  10 C  320  PHE PRO CYS ILE GLY LEU PRO GLY THR ILE ASP ASN ASP          
SEQRES  11 C  320  ILE LYS GLY THR ASP TYR THR ILE GLY PHE PHE THR ALA          
SEQRES  12 C  320  LEU SER THR VAL VAL GLU ALA ILE ASP ARG LEU ARG ASP          
SEQRES  13 C  320  THR SER SER SER HIS GLN ARG ILE SER VAL VAL GLU VAL          
SEQRES  14 C  320  MET GLY ARG TYR CYS GLY ASP LEU THR LEU ALA ALA ALA          
SEQRES  15 C  320  ILE ALA GLY GLY CYS GLU PHE VAL VAL VAL PRO GLU VAL          
SEQRES  16 C  320  GLU PHE SER ARG GLU ASP LEU VAL ASN GLU ILE LYS ALA          
SEQRES  17 C  320  GLY ILE ALA LYS GLY LYS LYS HIS ALA ILE VAL ALA ILE          
SEQRES  18 C  320  THR GLU HIS MET CYS ASP VAL ASP GLU LEU ALA HIS PHE          
SEQRES  19 C  320  ILE GLU LYS GLU THR GLY ARG GLU THR ARG ALA THR VAL          
SEQRES  20 C  320  LEU GLY HIS ILE GLN ARG GLY GLY SER PRO VAL PRO TYR          
SEQRES  21 C  320  ASP ARG ILE LEU ALA SER ARG MET GLY ALA TYR ALA ILE          
SEQRES  22 C  320  ASP LEU LEU LEU ALA GLY TYR GLY GLY ARG CYS VAL GLY          
SEQRES  23 C  320  ILE GLN ASN GLU GLN LEU VAL HIS HIS ASP ILE ILE ASP          
SEQRES  24 C  320  ALA ILE GLU ASN MET LYS ARG PRO PHE LYS GLY ASP TRP          
SEQRES  25 C  320  LEU ASP CYS ALA LYS LYS LEU TYR                              
SEQRES   1 D  320  MET ILE LYS LYS ILE GLY VAL LEU THR SER GLY GLY ASP          
SEQRES   2 D  320  ALA PRO GLY MET ASN ALA ALA ILE ARG GLY VAL VAL ARG          
SEQRES   3 D  320  SER ALA LEU THR GLU GLY LEU GLU VAL MET GLY ILE TYR          
SEQRES   4 D  320  ASP GLY TYR LEU GLY LEU TYR GLU ASP ARG MET VAL GLN          
SEQRES   5 D  320  LEU ASP ARG TYR SER VAL SER ASP MET ILE ASN ARG GLY          
SEQRES   6 D  320  GLY THR PHE LEU GLY SER ALA ARG PHE PRO GLU PHE ARG          
SEQRES   7 D  320  ASP GLU ASN ILE ARG ALA VAL ALA ILE GLU ASN LEU LYS          
SEQRES   8 D  320  LYS ARG GLY ILE ASP ALA LEU VAL VAL ILE GLY GLY ASP          
SEQRES   9 D  320  GLY SER TYR MET GLY ALA MET ARG LEU THR GLU MET GLY          
SEQRES  10 D  320  PHE PRO CYS ILE GLY LEU PRO GLY THR ILE ASP ASN ASP          
SEQRES  11 D  320  ILE LYS GLY THR ASP TYR THR ILE GLY PHE PHE THR ALA          
SEQRES  12 D  320  LEU SER THR VAL VAL GLU ALA ILE ASP ARG LEU ARG ASP          
SEQRES  13 D  320  THR SER SER SER HIS GLN ARG ILE SER VAL VAL GLU VAL          
SEQRES  14 D  320  MET GLY ARG TYR CYS GLY ASP LEU THR LEU ALA ALA ALA          
SEQRES  15 D  320  ILE ALA GLY GLY CYS GLU PHE VAL VAL VAL PRO GLU VAL          
SEQRES  16 D  320  GLU PHE SER ARG GLU ASP LEU VAL ASN GLU ILE LYS ALA          
SEQRES  17 D  320  GLY ILE ALA LYS GLY LYS LYS HIS ALA ILE VAL ALA ILE          
SEQRES  18 D  320  THR GLU HIS MET CYS ASP VAL ASP GLU LEU ALA HIS PHE          
SEQRES  19 D  320  ILE GLU LYS GLU THR GLY ARG GLU THR ARG ALA THR VAL          
SEQRES  20 D  320  LEU GLY HIS ILE GLN ARG GLY GLY SER PRO VAL PRO TYR          
SEQRES  21 D  320  ASP ARG ILE LEU ALA SER ARG MET GLY ALA TYR ALA ILE          
SEQRES  22 D  320  ASP LEU LEU LEU ALA GLY TYR GLY GLY ARG CYS VAL GLY          
SEQRES  23 D  320  ILE GLN ASN GLU GLN LEU VAL HIS HIS ASP ILE ILE ASP          
SEQRES  24 D  320  ALA ILE GLU ASN MET LYS ARG PRO PHE LYS GLY ASP TRP          
SEQRES  25 D  320  LEU ASP CYS ALA LYS LYS LEU TYR                              
FORMUL   5  HOH   *347(H2 O)                                                    
HELIX    1  1A GLY A   15  GLU A   30  13/10 END                          16    
HELIX    2  2A GLY A   40  ASP A   47  13/10 BEGINNING AND END             8    
HELIX    3 4AA PHE A   73  ASP A   78  5                                   6    
HELIX    4  4A ASP A   78  GLY A   93  13/10 END                          16    
HELIX    5  5A GLY A  102  GLY A  116  1                                  15    
HELIX    6  6A GLY A  138  HIS A  160  1                                  23    
HELIX    7  7A THR A  177  GLY A  185  1                                   9    
HELIX    8  8A SER A  197  GLY A  212  13/10 BEGINNING AND END            16    
HELIX    9  9A ASP A  226  GLY A  239  1                                  14    
HELIX   10 10A GLY A  248  ARG A  252  5                                   5    
HELIX   11 11A VAL A  257  GLY A  278  13/10 END                          22    
HELIX   12 12A ASP A  295  ILE A  300  1                                   6    
HELIX   13  1B GLY B   15  GLU B   30  13/10 END                          16    
HELIX   14  2B GLY B   40  ASP B   47  13/10 BEGINNING AND END             8    
HELIX   15 4AB PHE B   73  ASP B   78  5                                   6    
HELIX   16  4B ASP B   78  GLY B   93  13/10 END                          16    
HELIX   17  5B GLY B  102  GLY B  116  1                                  15    
HELIX   18  6B GLY B  138  HIS B  160  1                                  23    
HELIX   19  7B THR B  177  GLY B  185  1                                   9    
HELIX   20  8B SER B  197  GLY B  212  13/10 BEGINNING AND END            16    
HELIX   21  9B ASP B  226  GLY B  239  1                                  14    
HELIX   22 10B GLY B  248  ARG B  252  5                                   5    
HELIX   23 11B VAL B  257  GLY B  278  13/10 END                          22    
HELIX   24 12B ASP B  295  ILE B  300  1                                   6    
HELIX   25  1C GLY C   15  GLU C   30  13/10 END                          16    
HELIX   26  2C GLY C   40  ASP C   47  13/10 BEGINNING AND END             8    
HELIX   27 4AC PHE C   73  ASP C   78  5                                   6    
HELIX   28  4C ASP C   78  GLY C   93  13/10 END                          16    
HELIX   29  5C GLY C  102  GLY C  116  1                                  15    
HELIX   30  6C GLY C  138  HIS C  160  1                                  23    
HELIX   31  7C THR C  177  GLY C  185  1                                   9    
HELIX   32  8C SER C  197  GLY C  212  13/10 BEGINNING AND END            16    
HELIX   33  9C ASP C  226  GLY C  239  1                                  14    
HELIX   34 10C GLY C  248  ARG C  252  5                                   5    
HELIX   35 11C VAL C  257  GLY C  278  13/10 END                          22    
HELIX   36 12C ASP C  295  ILE C  300  1                                   6    
HELIX   37  1D GLY D   15  GLU D   30  13/10 END                          16    
HELIX   38  2D GLY D   40  ASP D   47  13/10 BEGINNING AND END             8    
HELIX   39 4AD PHE D   73  ASP D   78  5                                   6    
HELIX   40  4D ASP D   78  GLY D   93  13/10 END                          16    
HELIX   41  5D GLY D  102  GLY D  116  1                                  15    
HELIX   42  6D GLY D  138  HIS D  160  1                                  23    
HELIX   43  7D THR D  177  GLY D  185  1                                   9    
HELIX   44  8D SER D  197  GLY D  212  13/10 BEGINNING AND END            16    
HELIX   45  9D ASP D  226  GLY D  239  1                                  14    
HELIX   46 10D GLY D  248  ARG D  252  5                                   5    
HELIX   47 11D VAL D  257  GLY D  278  13/10 END                          22    
HELIX   48 12D ASP D  295  ASN D  302  1                                   8    
SHEET    1 S1A 7 ARG A  48  LEU A  52  0                                        
SHEET    2 S1A 7 GLU A  33  TYR A  38 -1  O  GLY A  36   N  VAL A  50           
SHEET    3 S1A 7 LYS A   2  SER A   9  1  O  VAL A   6   N  ILE A  37           
SHEET    4 S1A 7 ALA A  96  GLY A 101  1  O  VAL A  98   N  LEU A   7           
SHEET    5 S1A 7 PRO A 118  LEU A 122  1  O  ILE A 120   N  VAL A  99           
SHEET    6 S1A 7 GLY A 281  GLN A 287  1  O  ARG A 282   N  GLY A 121           
SHEET    7 S1A 7 GLN A 290  ASP A 295 -1  O  HIS A 294   N  CYS A 283           
SHEET    1 S2A 4 PHE A 188  VAL A 190  0                                        
SHEET    2 S2A 4 ALA A 216  THR A 221  1  O  ALA A 219   N  VAL A 190           
SHEET    3 S2A 4 ARG A 162  VAL A 168  1  O  VAL A 166   N  ILE A 220           
SHEET    4 S2A 4 GLU A 241  LEU A 247  1  O  THR A 245   N  GLU A 167           
SHEET    1 S1B 7 ARG B  48  LEU B  52  0                                        
SHEET    2 S1B 7 GLU B  33  TYR B  38 -1  O  GLY B  36   N  VAL B  50           
SHEET    3 S1B 7 LYS B   2  SER B   9  1  O  VAL B   6   N  ILE B  37           
SHEET    4 S1B 7 ALA B  96  GLY B 101  1  O  VAL B  98   N  LEU B   7           
SHEET    5 S1B 7 PRO B 118  LEU B 122  1  O  ILE B 120   N  VAL B  99           
SHEET    6 S1B 7 GLY B 281  GLN B 287  1  O  ARG B 282   N  GLY B 121           
SHEET    7 S1B 7 GLN B 290  ASP B 295 -1  O  HIS B 294   N  CYS B 283           
SHEET    1 S2B 4 PHE B 188  VAL B 190  0                                        
SHEET    2 S2B 4 ALA B 216  THR B 221  1  O  ALA B 219   N  VAL B 190           
SHEET    3 S2B 4 ARG B 162  VAL B 168  1  O  VAL B 166   N  ILE B 220           
SHEET    4 S2B 4 GLU B 241  LEU B 247  1  O  THR B 245   N  GLU B 167           
SHEET    1 S1C 7 ARG C  48  LEU C  52  0                                        
SHEET    2 S1C 7 GLU C  33  TYR C  38 -1  O  GLY C  36   N  VAL C  50           
SHEET    3 S1C 7 LYS C   2  SER C   9  1  O  VAL C   6   N  ILE C  37           
SHEET    4 S1C 7 ALA C  96  GLY C 101  1  O  VAL C  98   N  LEU C   7           
SHEET    5 S1C 7 PRO C 118  LEU C 122  1  O  ILE C 120   N  VAL C  99           
SHEET    6 S1C 7 GLY C 281  GLN C 287  1  O  ARG C 282   N  GLY C 121           
SHEET    7 S1C 7 GLN C 290  ASP C 295 -1  O  HIS C 294   N  CYS C 283           
SHEET    1 S2C 4 PHE C 188  VAL C 190  0                                        
SHEET    2 S2C 4 ALA C 216  THR C 221  1  O  ALA C 219   N  VAL C 190           
SHEET    3 S2C 4 ARG C 162  VAL C 168  1  O  VAL C 166   N  ILE C 220           
SHEET    4 S2C 4 GLU C 241  LEU C 247  1  O  THR C 245   N  GLU C 167           
SHEET    1 S1D 7 ARG D  48  LEU D  52  0                                        
SHEET    2 S1D 7 GLU D  33  TYR D  38 -1  O  GLY D  36   N  VAL D  50           
SHEET    3 S1D 7 LYS D   2  SER D   9  1  O  VAL D   6   N  ILE D  37           
SHEET    4 S1D 7 ALA D  96  GLY D 101  1  O  VAL D  98   N  LEU D   7           
SHEET    5 S1D 7 PRO D 118  LEU D 122  1  O  ILE D 120   N  VAL D  99           
SHEET    6 S1D 7 GLY D 281  GLN D 287  1  O  ARG D 282   N  GLY D 121           
SHEET    7 S1D 7 GLN D 290  ASP D 295 -1  O  HIS D 294   N  CYS D 283           
SHEET    1 S2D 4 PHE D 188  VAL D 190  0                                        
SHEET    2 S2D 4 ALA D 216  THR D 221  1  O  ALA D 219   N  VAL D 190           
SHEET    3 S2D 4 ARG D 162  VAL D 168  1  O  VAL D 166   N  ILE D 220           
SHEET    4 S2D 4 GLU D 241  LEU D 247  1  O  THR D 245   N  GLU D 167           
CRYST1  177.000   66.400  154.000  90.00 118.80  90.00 C 1 21 1      8          
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      0.006447  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015060  0.000000        0.00000                         
SCALE3      0.003570  0.000000  0.006494        0.00000                         
MTRIX1   1 -0.041580  0.000000  0.999140      -61.70351    1                    
MTRIX2   1  0.000000 -1.000000  0.000000        0.02603    1                    
MTRIX3   1  0.999140  0.000000  0.041580       59.18931    1                    
MTRIX1   2 -0.998910  0.000000 -0.046660       80.09368    1                    
MTRIX2   2  0.000000 -1.000000  0.000000       41.78273    1                    
MTRIX3   2 -0.046660  0.000000  0.998910        1.86952    1                    
MTRIX1   3  0.705310  0.000000 -0.708900       81.24258    1                    
MTRIX2   3  0.000000  1.000000  0.000000       20.87835    1                    
MTRIX3   3  0.708900  0.000000  0.705310       68.07738    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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