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Database: PDB
Entry: 4IAC
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Original site: 4IAC 
HEADER    TRANSFERASE/PEPTIDE                     06-DEC-12   4IAC              
TITLE     X-RAY STRUCTURE OF CAMP DEPENDENT PROTEIN KINASE A IN COMPLEX WITH    
TITLE    2 HIGH MG2+ CONCENTRATION, AMP-PCP AND PSEUDO-SUBSTRATE PEPTIDE SP20   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PKA C-ALPHA;                                                
COMPND   5 EC: 2.7.11.11;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PEPTIDE SP20;                                              
COMPND   9 CHAIN: S;                                                            
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PRKACA, PKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    KINASE, PHOSPHORYLATION, AUTO-PHOSPHORYLATED, TRANSFERASE-PEPTIDE     
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.GERLITS,A.KOVALEVSKY                                                
REVDAT   3   21-SEP-16 4IAC    1       TITLE                                    
REVDAT   2   18-DEC-13 4IAC    1       JRNL                                     
REVDAT   1   12-JUN-13 4IAC    0                                                
JRNL        AUTH   O.GERLITS,M.J.WALTMAN,S.TAYLOR,P.LANGAN,A.KOVALEVSKY         
JRNL        TITL   INSIGHTS INTO THE PHOSPHORYL TRANSFER CATALYZED BY           
JRNL        TITL 2 CAMP-DEPENDENT PROTEIN KINASE: AN X-RAY CRYSTALLOGRAPHIC     
JRNL        TITL 3 STUDY OF COMPLEXES WITH VARIOUS METALS AND PEPTIDE SUBSTRATE 
JRNL        TITL 4 SP20.                                                        
JRNL        REF    BIOCHEMISTRY                  V.  52  3721 2013              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   23672593                                                     
JRNL        DOI    10.1021/BI400066A                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 21951                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1110                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2936                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 339                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : 1.165                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4IAC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB076503.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-APR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NONE                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21951                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.400                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.0                               
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.5, 5 MM DTT, 15-20%      
REMARK 280  PEG 4000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K           
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       28.40450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.97700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.83900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       48.97700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.40450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.83900            
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: 3260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, S                                  
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     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     GLY A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     GLN A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  38     -179.57   -178.87                                   
REMARK 500    ILE A  46      -63.55   -101.97                                   
REMARK 500    ASP A 166       43.45   -149.21                                   
REMARK 500    ASP A 184       78.08     59.80                                   
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 A  45         0.26    SIDE CHAIN                              
REMARK 500    ARG A 134         0.09    SIDE CHAIN                              
REMARK 500    ARG A 144         0.17    SIDE CHAIN                              
REMARK 500    ARG A 190         0.17    SIDE CHAIN                              
REMARK 500    ARG A 256         0.19    SIDE CHAIN                              
REMARK 500    ARG A 270         0.15    SIDE CHAIN                              
REMARK 500    ARG A 308         0.21    SIDE CHAIN                              
REMARK 500    ARG A 336         0.08    SIDE CHAIN                              
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    ARG A 165        21.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1076        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH A1090        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH A1101        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH A1123        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH A1192        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH A1206        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH A1208        DISTANCE =  5.43 ANGSTROMS                       
REMARK 525    HOH A1214        DISTANCE =  6.19 ANGSTROMS                       
REMARK 525    HOH A1239        DISTANCE =  6.52 ANGSTROMS                       
REMARK 525    HOH A1247        DISTANCE =  7.18 ANGSTROMS                       
REMARK 525    HOH A1250        DISTANCE =  9.37 ANGSTROMS                       
REMARK 525    HOH S 707        DISTANCE =  5.46 ANGSTROMS                       
REMARK 525    HOH S 711        DISTANCE =  5.42 ANGSTROMS                       
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                              MG A 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1001   O                                                      
REMARK 620 2 HOH A1003   O    97.5                                              
REMARK 620 3 ACP A 403   O1B  97.5 164.9                                        
REMARK 620 4 ACP A 403   O3G 111.2  94.0  78.4                                  
REMARK 620 5 ASP A 184   OD2 151.5  86.7  81.2  96.5                            
REMARK 620 6 ASP A 184   OD1  96.0  95.4  85.3 149.7  55.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ACP A 403   O2A                                                    
REMARK 620 2 ASN A 171   OD1 100.1                                              
REMARK 620 3 ACP A 403   O2G 127.7 131.8                                        
REMARK 620 4 ASP A 184   OD2  88.0  95.5  92.5                                  
REMARK 620 5 HOH A1002   O    83.4  88.1  91.2 171.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP A 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4IAD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IAF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IAI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IAK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IAY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IAZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IB0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IB1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IB3   RELATED DB: PDB                                   
DBREF  4IAC A    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  4IAC S  605   624  PDB    4IAC     4IAC           605    624             
SEQADV 4IAC HIS A   -5  UNP  P05132              EXPRESSION TAG                 
SEQADV 4IAC HIS A   -4  UNP  P05132              EXPRESSION TAG                 
SEQADV 4IAC HIS A   -3  UNP  P05132              EXPRESSION TAG                 
SEQADV 4IAC HIS A   -2  UNP  P05132              EXPRESSION TAG                 
SEQADV 4IAC HIS A   -1  UNP  P05132              EXPRESSION TAG                 
SEQADV 4IAC HIS A    0  UNP  P05132              EXPRESSION TAG                 
SEQRES   1 A  356  HIS HIS HIS HIS HIS HIS GLY ASN ALA ALA ALA ALA LYS          
SEQRES   2 A  356  LYS GLY SER GLU GLN GLU SER VAL LYS GLU PHE LEU ALA          
SEQRES   3 A  356  LYS ALA LYS GLU ASP PHE LEU LYS LYS TRP GLU THR PRO          
SEQRES   4 A  356  SER GLN ASN THR ALA GLN LEU ASP GLN PHE ASP ARG ILE          
SEQRES   5 A  356  LYS THR LEU GLY THR GLY SER PHE GLY ARG VAL MET LEU          
SEQRES   6 A  356  VAL LYS HIS LYS GLU SER GLY ASN HIS TYR ALA MET LYS          
SEQRES   7 A  356  ILE LEU ASP LYS GLN LYS VAL VAL LYS LEU LYS GLN ILE          
SEQRES   8 A  356  GLU HIS THR LEU ASN GLU LYS ARG ILE LEU GLN ALA VAL          
SEQRES   9 A  356  ASN PHE PRO PHE LEU VAL LYS LEU GLU PHE SER PHE LYS          
SEQRES  10 A  356  ASP ASN SER ASN LEU TYR MET VAL MET GLU TYR VAL ALA          
SEQRES  11 A  356  GLY GLY GLU MET PHE SER HIS LEU ARG ARG ILE GLY ARG          
SEQRES  12 A  356  PHE SEP GLU PRO HIS ALA ARG PHE TYR ALA ALA GLN ILE          
SEQRES  13 A  356  VAL LEU THR PHE GLU TYR LEU HIS SER LEU ASP LEU ILE          
SEQRES  14 A  356  TYR ARG ASP LEU LYS PRO GLU ASN LEU LEU ILE ASP GLN          
SEQRES  15 A  356  GLN GLY TYR ILE GLN VAL THR ASP PHE GLY PHE ALA LYS          
SEQRES  16 A  356  ARG VAL LYS GLY ARG THR TRP TPO LEU CYS GLY THR PRO          
SEQRES  17 A  356  GLU TYR LEU ALA PRO GLU ILE ILE LEU SER LYS GLY TYR          
SEQRES  18 A  356  ASN LYS ALA VAL ASP TRP TRP ALA LEU GLY VAL LEU ILE          
SEQRES  19 A  356  TYR GLU MET ALA ALA GLY TYR PRO PRO PHE PHE ALA ASP          
SEQRES  20 A  356  GLN PRO ILE GLN ILE TYR GLU LYS ILE VAL SER GLY LYS          
SEQRES  21 A  356  VAL ARG PHE PRO SER HIS PHE SER SER ASP LEU LYS ASP          
SEQRES  22 A  356  LEU LEU ARG ASN LEU LEU GLN VAL ASP LEU THR LYS ARG          
SEQRES  23 A  356  PHE GLY ASN LEU LYS ASN GLY VAL ASN ASP ILE LYS ASN          
SEQRES  24 A  356  HIS LYS TRP PHE ALA THR THR ASP TRP ILE ALA ILE TYR          
SEQRES  25 A  356  GLN ARG LYS VAL GLU ALA PRO PHE ILE PRO LYS PHE LYS          
SEQRES  26 A  356  GLY PRO GLY ASP THR SER ASN PHE ASP ASP TYR GLU GLU          
SEQRES  27 A  356  GLU GLU ILE ARG VAL SEP ILE ASN GLU LYS CYS GLY LYS          
SEQRES  28 A  356  GLU PHE THR GLU PHE                                          
SEQRES   1 S   20  THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY          
SEQRES   2 S   20  ARG ARG ALA SER ILE HIS ASP                                  
MODRES 4IAC SEP A  139  SER  PHOSPHOSERINE                                      
MODRES 4IAC TPO A  197  THR  PHOSPHOTHREONINE                                   
MODRES 4IAC SEP A  338  SER  PHOSPHOSERINE                                      
HET    SEP  A 139      10                                                       
HET    TPO  A 197      11                                                       
HET    SEP  A 338      10                                                       
HET     MG  A 401       1                                                       
HET     MG  A 402       1                                                       
HET    ACP  A 403      31                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER                     
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE                 
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  ACP    C11 H18 N5 O12 P3                                            
FORMUL   6  HOH   *339(H2 O)                                                    
HELIX    1   1 VAL A   15  THR A   32  1                                  18    
HELIX    2   2 GLN A   39  ASP A   41  5                                   3    
HELIX    3   3 LYS A   76  LEU A   82  1                                   7    
HELIX    4   4 GLN A   84  GLN A   96  1                                  13    
HELIX    5   5 GLU A  127  GLY A  136  1                                  10    
HELIX    6   6 SEP A  139  LEU A  160  1                                  22    
HELIX    7   7 LYS A  168  GLU A  170  5                                   3    
HELIX    8   8 THR A  201  LEU A  205  5                                   5    
HELIX    9   9 ALA A  206  LEU A  211  1                                   6    
HELIX   10  10 LYS A  217  GLY A  234  1                                  18    
HELIX   11  11 GLN A  242  GLY A  253  1                                  12    
HELIX   12  12 SER A  262  LEU A  273  1                                  12    
HELIX   13  13 VAL A  288  ASN A  293  1                                   6    
HELIX   14  14 HIS A  294  ALA A  298  5                                   5    
HELIX   15  15 ASP A  301  GLN A  307  1                                   7    
HELIX   16  16 THR S  606  ALA S  612  1                                   7    
SHEET    1   A 5 PHE A  43  THR A  51  0                                        
SHEET    2   A 5 GLY A  55  HIS A  62 -1  O  LEU A  59   N  LYS A  47           
SHEET    3   A 5 HIS A  68  ASP A  75 -1  O  ILE A  73   N  ARG A  56           
SHEET    4   A 5 ASN A 115  GLU A 121 -1  O  MET A 120   N  ALA A  70           
SHEET    5   A 5 LEU A 106  LYS A 111 -1  N  PHE A 110   O  TYR A 117           
SHEET    1   B 2 LEU A 162  ILE A 163  0                                        
SHEET    2   B 2 LYS A 189  ARG A 190 -1  O  LYS A 189   N  ILE A 163           
SHEET    1   C 2 LEU A 172  ILE A 174  0                                        
SHEET    2   C 2 ILE A 180  VAL A 182 -1  O  GLN A 181   N  LEU A 173           
LINK         C   PHE A 138                 N   SEP A 139     1555   1555  1.33  
LINK         C   SEP A 139                 N   GLU A 140     1555   1555  1.33  
LINK         C   TRP A 196                 N   TPO A 197     1555   1555  1.33  
LINK         C   TPO A 197                 N   LEU A 198     1555   1555  1.33  
LINK         C   VAL A 337                 N   SEP A 338     1555   1555  1.33  
LINK         C   SEP A 338                 N   ILE A 339     1555   1555  1.33  
LINK        MG    MG A 401                 O   HOH A1001     1555   1555  2.16  
LINK        MG    MG A 401                 O   HOH A1003     1555   1555  2.17  
LINK        MG    MG A 402                 O2A ACP A 403     1555   1555  2.18  
LINK         OD1 ASN A 171                MG    MG A 402     1555   1555  2.19  
LINK        MG    MG A 402                 O2G ACP A 403     1555   1555  2.19  
LINK        MG    MG A 401                 O1B ACP A 403     1555   1555  2.20  
LINK         OD2 ASP A 184                MG    MG A 402     1555   1555  2.22  
LINK        MG    MG A 401                 O3G ACP A 403     1555   1555  2.25  
LINK        MG    MG A 402                 O   HOH A1002     1555   1555  2.27  
LINK         OD2 ASP A 184                MG    MG A 401     1555   1555  2.29  
LINK         OD1 ASP A 184                MG    MG A 401     1555   1555  2.40  
SITE     1 AC1  3 ASP A 184  HOH A1001  HOH A1003                               
SITE     1 AC2  3 ASN A 171  ASP A 184  HOH A1002                               
SITE     1 AC3 25 GLY A  52  VAL A  57  ALA A  70  LYS A  72                    
SITE     2 AC3 25 VAL A 104  MET A 120  GLU A 121  VAL A 123                    
SITE     3 AC3 25 GLU A 127  LYS A 168  GLU A 170  ASN A 171                    
SITE     4 AC3 25 LEU A 173  THR A 183  ASP A 184  PHE A 327                    
SITE     5 AC3 25  MG A 401   MG A 402  HOH A1002  HOH A1089                    
SITE     6 AC3 25 HOH A1270  HOH A1271  ARG S 618  ALA S 620                    
SITE     7 AC3 25 SER S 621                                                     
CRYST1   56.809   79.678   97.954  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      0.017603  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012551  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010209        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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