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Database: PDB
Entry: 1ATP
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Original site: 1ATP 
HEADER    TRANSFERASE(PHOSPHOTRANSFERASE)         08-JAN-93   1ATP              
TITLE     2.2 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF    
TITLE    2 CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH MNATP AND A PEPTIDE     
TITLE    3 INHIBITOR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE;                             
COMPND   3 CHAIN: E;                                                            
COMPND   4 EC: 2.7.1.37;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PEPTIDE INHIBITOR PKI(5-24);                               
COMPND   8 CHAIN: I;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   7 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   8 ORGANISM_TAXID: 10090                                                
KEYWDS    TRANSFERASE(PHOSPHOTRANSFERASE)                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.ZHENG,E.A.TRAFNY,D.R.KNIGHTON,N.-H.XUONG,S.S.TAYLOR,L.F.TENEYCK,    
AUTHOR   2 J.M.SOWADSKI                                                         
REVDAT   4   14-AUG-19 1ATP    1       REMARK                                   
REVDAT   3   17-JUL-19 1ATP    1       REMARK LINK                              
REVDAT   2   24-FEB-09 1ATP    1       VERSN                                    
REVDAT   1   15-APR-93 1ATP    0                                                
JRNL        AUTH   J.ZHENG,E.A.TRAFNY,D.R.KNIGHTON,N.H.XUONG,S.S.TAYLOR,        
JRNL        AUTH 2 L.F.TEN EYCK,J.M.SOWADSKI                                    
JRNL        TITL   2.2 A REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF  
JRNL        TITL 2 CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH MNATP AND A     
JRNL        TITL 3 PEPTIDE INHIBITOR.                                           
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  49   362 1993              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   15299527                                                     
JRNL        DOI    10.1107/S0907444993000423                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   D.R.KNIGHTON,S.M.BELL,J.ZHENG,L.F.TENEYCK,N.-H.XUONG,        
REMARK   1  AUTH 2 S.S.TAYLOR,J.M.SOWADSKI                                      
REMARK   1  TITL   2.0 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE CATALYTIC      
REMARK   1  TITL 2 SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A    
REMARK   1  TITL 3 PEPTIDE INHIBITOR AND DETERGENT                              
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.ZHENG,D.R.KNIGHTON,L.F.TENEYCK,R.KARLSSON,N.-H.XUONG,      
REMARK   1  AUTH 2 S.S.TAYLOR,J.M.SOWADSKI                                      
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT 
REMARK   1  TITL 2 PROTEIN KINASE COMPLEXED WITH MG/ATP AND PEPTIDE INHIBITOR   
REMARK   1  REF    BIOCHEMISTRY                  V.  32  2154 1993              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   D.R.KNIGHTON,J.ZHENG,L.F.TENEYCK,V.A.XUONG,N.-H.ASHFORD,     
REMARK   1  AUTH 2 S.S.TAYLOR,J.M.SOWADSKI                                      
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CYCLIC         
REMARK   1  TITL 2 ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN KINASE             
REMARK   1  REF    SCIENCE                       V. 253   407 1991              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   D.R.KNIGHTON,J.ZHENG,L.F.TENEYCK,N.-H.XUONG,S.S.TAYLOR,      
REMARK   1  AUTH 2 J.M.SOWADSKI                                                 
REMARK   1  TITL   STRUCTURE OF A PEPTIDE INHIBITOR BOUND TO THE CATALYTIC      
REMARK   1  TITL 2 SUBUNIT OF CYCLIC ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN  
REMARK   1  TITL 3 KINASE                                                       
REMARK   1  REF    SCIENCE                       V. 253   414 1991              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   L.W.SLICE,S.S.TAYLOR                                         
REMARK   1  TITL   EXPRESSION OF THE CATALYTIC SUBUNIT OF C/AMP-DEPENDENT       
REMARK   1  TITL 2 PROTEIN KINASE IN ESCHERICHIA COLI                           
REMARK   1  REF    J.BIOL.CHEM.                  V. 264 20940 1989              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
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  USING ALL DATA, NO SIGMA CUTOFF.                                    
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            : 2934                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 103                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : NULL  ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : NULL                                             
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ATP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000171245.                                   
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: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-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       36.79000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.29000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.14000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.29000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.79000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.14000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY E     1                                                      
REMARK 465     ASN E     2                                                      
REMARK 465     ALA E     3                                                      
REMARK 465     ALA E     4                                                      
REMARK 465     ALA E     5                                                      
REMARK 465     ALA E     6                                                      
REMARK 465     LYS E     7                                                      
REMARK 465     LYS E     8                                                      
REMARK 465     GLY E     9                                                      
REMARK 465     SER E    10                                                      
REMARK 465     GLU E    11                                                      
REMARK 465     GLN E    12                                                      
REMARK 465     GLU E    13                                                      
REMARK 465     SER E    14                                                      
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   O    TYR E   164     O    HOH E   424              1.14            
REMARK 500   O    ARG E   165     N    ASP E   166              1.78            
REMARK 500   ND2  ASN E   326     O    HOH E   605              1.95            
REMARK 500   C    TYR E   164     O    HOH E   424              2.10            
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    GLU E  17   CD    GLU E  17   OE2     0.073                       
REMARK 500    GLU E  24   CD    GLU E  24   OE2     0.068                       
REMARK 500    GLU E  31   CD    GLU E  31   OE1     0.067                       
REMARK 500    GLU E  64   CD    GLU E  64   OE2     0.069                       
REMARK 500    GLU E  91   CD    GLU E  91   OE2    -0.068                       
REMARK 500    GLU E 140   CD    GLU E 140   OE2     0.067                       
REMARK 500    ARG E 165   C     ASP E 166   N      -0.199                       
REMARK 500    GLU E 170   CD    GLU E 170   OE2     0.085                       
REMARK 500    GLU E 203   CD    GLU E 203   OE2     0.082                       
REMARK 500    GLU E 248   CD    GLU E 248   OE1     0.071                       
REMARK 500    GLU E 331   CD    GLU E 331   OE2     0.072                       
REMARK 500    GLU E 333   CD    GLU E 333   OE2     0.075                       
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    ASP E  44   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP E  44   CB  -  CG  -  OD2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ARG E  56   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ASP E  75   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP E 112   CB  -  CG  -  OD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG E 137   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ASP E 161   CB  -  CG  -  OD1 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ASP E 161   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG E 165   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG E 165   CA  -  C   -  N   ANGL. DEV. =  23.8 DEGREES          
REMARK 500    ARG E 165   O   -  C   -  N   ANGL. DEV. = -25.8 DEGREES          
REMARK 500    ASP E 166   CA  -  C   -  N   ANGL. DEV. = -13.9 DEGREES          
REMARK 500    ARG E 194   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP E 241   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ASP E 267   CB  -  CG  -  OD1 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    ASP E 290   CB  -  CG  -  OD1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    LYS E 317   N   -  CA  -  CB  ANGL. DEV. =  11.3 DEGREES          
REMARK 500    ARG I  18   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ASP I  24   CB  -  CG  -  OD1 ANGL. DEV. =  -5.9 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    ASN E  36       75.09     29.48                                   
REMARK 500    ILE E  46      -86.36   -107.73                                   
REMARK 500    ARG E 165       19.16     51.81                                   
REMARK 500    ASP E 166       76.02   -157.62                                   
REMARK 500    THR E 183     -165.60   -105.27                                   
REMARK 500    ASP E 184       87.06     48.73                                   
REMARK 500    PRO E 202      -60.76    -24.26                                   
REMARK 500    LEU E 273       45.13    -94.84                                   
REMARK 500    LEU E 277       -2.74    -55.75                                   
REMARK 500    GLU E 311       99.60    -64.65                                   
REMARK 500    LYS E 342      -60.79    -90.98                                   
REMARK 500    HIS I  23     -136.73   -144.46                                   
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    ARG E 165        -10.44                                           
REMARK 500    ASP E 166        -23.89                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 INHIBITOR RESIDUE NUMBERING CORRESPONDS TO NUMBERS FROM              
REMARK 600 THE SEQUENCE OF THE LARGER NATURALLY OCCURRING PKI PROTEIN           
REMARK 600 OF WHICH THE INHIBITOR IS A SYNTHETIC FRAGMENT.                      
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E 351  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP E 355   O1B                                                    
REMARK 620 2 HOH E 447   O   170.9                                              
REMARK 620 3 ATP E 355   O3G  91.2  95.1                                        
REMARK 620 4 HOH E 477   O    90.4  92.6 116.2                                  
REMARK 620 5 ASP E 184   OD2  80.7  92.7  89.9 152.7                            
REMARK 620 6 ASP E 184   OD1  80.5  90.8 149.1  93.7  59.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E 352  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP E 355   O2G                                                    
REMARK 620 2 HOH E 635   O    84.9                                              
REMARK 620 3 ATP E 355   O2A 127.3  88.4                                        
REMARK 620 4 ASP E 184   OD2  87.1 167.9  89.3                                  
REMARK 620 5 ASN E 171   OD1 116.5  96.1 116.2  95.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: NULL                                                  
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: NULL                                                  
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 351                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 352                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP E 355                 
DBREF  1ATP E    1   350  UNP    P05132   KAPCA_MOUSE      1    350             
DBREF  1ATP I    5    24  UNP    P63248   IPKA_MOUSE       5     24             
SEQRES   1 E  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU          
SEQRES   2 E  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 E  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 E  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 E  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 E  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 E  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 E  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 E  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 E  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 E  350  HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS ALA          
SEQRES  12 E  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 E  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 E  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 E  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 E  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 E  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 E  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 E  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 E  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 E  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 E  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN          
SEQRES  23 E  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 E  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 E  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 E  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 E  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE              
SEQRES   1 I   20  THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY          
SEQRES   2 I   20  ARG ARG ASN ALA ILE HIS ASP                                  
MODRES 1ATP TPO E  197  THR  PHOSPHOTHREONINE                                   
MODRES 1ATP SEP E  338  SER  PHOSPHOSERINE                                      
HET    TPO  E 197      11                                                       
HET    SEP  E 338      10                                                       
HET     MN  E 351       1                                                       
HET     MN  E 352       1                                                       
HET    ATP  E 355      31                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   5  ATP    C10 H16 N5 O13 P3                                            
FORMUL   6  HOH   *103(H2 O)                                                    
HELIX    1   A LYS E   16  GLU E   31  1                                  16    
HELIX    2  AB LEU E   40  GLN E   42  5NOT NOTED IN REF 3                 3    
HELIX    3   B LYS E   76  LYS E   81  1                                   6    
HELIX    4   C ILE E   85  ALA E   97  1                                  13    
HELIX    5   D MET E  128  ILE E  135  1                                   8    
HELIX    6   E GLU E  140  SER E  159  1                                  20    
HELIX    7 EF0 PRO E  169  ASN E  171  5NOT NOTED IN REF 3                 3    
HELIX    8 EF1 PRO E  202  TYR E  204  5NOT NOTED IN REF 3                 3    
HELIX    9 EF2 PRO E  207  ILE E  210  1NOT NOTED IN REF 3                 4    
HELIX   10   F ALA E  218  ALA E  233  1                                  16    
HELIX   11   G PRO E  243  SER E  252  1                                  10    
HELIX   12   H SER E  263  LEU E  272  1                                  10    
HELIX   13   I ASN E  289  LYS E  292  1                                   4    
HELIX   14  IJ LYS E  295  PHE E  297  5NOT NOTED IN REF 3                 3    
HELIX   15   J TRP E  302  TYR E  306  1                                   5    
HELIX   16  IA THR I    6  ILE I   11  1INHIBITOR N-TERMINAL HELIX         6    
SHEET    1   A 5 PHE E  43  THR E  51  0                                        
SHEET    2   A 5 ARG E  56  HIS E  62 -1                                        
SHEET    3   A 5 ASN E  67  ASP E  75 -1                                        
SHEET    4   A 5 ASN E 115  MET E 120 -1                                        
SHEET    5   A 5 LEU E 106  LYS E 111 -1                                        
SHEET    1   B 2 LEU E 162  ILE E 163  0                                        
SHEET    2   B 2 LEU E 172  ILE E 174 -1                                        
SHEET    1   C 2 ILE E 180  VAL E 182  0                                        
SHEET    2   C 2 LYS E 189  ARG E 190 -1                                        
LINK        MN    MN E 351                 O1B ATP E 355     1555   1555  2.18  
LINK        MN    MN E 351                 O   HOH E 447     1555   1555  2.15  
LINK        MN    MN E 351                 O3G ATP E 355     1555   1555  2.05  
LINK        MN    MN E 351                 O   HOH E 477     1555   1555  1.85  
LINK        MN    MN E 351                 OD2 ASP E 184     1555   1555  2.19  
LINK        MN    MN E 351                 OD1 ASP E 184     1555   1555  2.35  
LINK        MN    MN E 352                 O2G ATP E 355     1555   1555  2.21  
LINK        MN    MN E 352                 O   HOH E 635     1555   1555  2.08  
LINK        MN    MN E 352                 O2A ATP E 355     1555   1555  1.99  
LINK        MN    MN E 352                 OD2 ASP E 184     1555   1555  2.14  
LINK        MN    MN E 352                 OD1 ASN E 171     1555   1555  2.09  
LINK         C   TRP E 196                 N   TPO E 197     1555   1555  1.32  
LINK         C   TPO E 197                 N   LEU E 198     1555   1555  1.30  
LINK         C   VAL E 337                 N   SEP E 338     1555   1555  1.32  
LINK         C   SEP E 338                 N   ILE E 339     1555   1555  1.33  
SITE     1 AC4  5 HIS E  87  ARG E 165  LYS E 189  THR E 195                    
SITE     2 AC4  5 HOH E 450                                                     
SITE     1 AC5  2 ASN E 340  HOH E 588                                          
SITE     1 AC1  4 ASP E 184  ATP E 355  HOH E 447  HOH E 477                    
SITE     1 AC2  4 ASN E 171  ASP E 184  ATP E 355  HOH E 635                    
SITE     1 AC3 26 THR E  51  GLY E  52  SER E  53  PHE E  54                    
SITE     2 AC3 26 GLY E  55  VAL E  57  ALA E  70  LYS E  72                    
SITE     3 AC3 26 VAL E 104  GLU E 121  VAL E 123  GLU E 127                    
SITE     4 AC3 26 LYS E 168  GLU E 170  ASN E 171  LEU E 173                    
SITE     5 AC3 26 THR E 183  ASP E 184  PHE E 327   MN E 351                    
SITE     6 AC3 26  MN E 352  HOH E 447  HOH E 477  HOH E 635                    
SITE     7 AC3 26 ARG I  18  ALA I  21                                          
CRYST1   73.580   76.280   80.580  90.00  90.00  90.00 P 21 21 21    4          
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      0.013591  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013110  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012410        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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