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Database: PDB
Entry: 4XW6
LinkDB: 4XW6
Original site: 4XW6 
HEADER    TRANSFERASE                             28-JAN-15   4XW6              
TITLE     X-RAY STRUCTURE OF PKAC WITH ADP, FREE PHOSPHATE ION, CP20, MAGNESIUM 
TITLE    2 IONS                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 15-351;                                       
COMPND   5 SYNONYM: PKA C-ALPHA;                                                
COMPND   6 EC: 2.7.11.11;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA;             
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: PKI-ALPHA,CAMP-DEPENDENT PROTEIN KINASE INHIBITOR,          
COMPND  12 MUSCLE/BRAIN ISOFORM;                                                
COMPND  13 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: ORYCTOLAGUS CUNICULUS;                          
SOURCE  11 ORGANISM_COMMON: RABBIT;                                             
SOURCE  12 ORGANISM_TAXID: 9986                                                 
KEYWDS    PROTEIN KINASE A, ATP HYDROLYSIS, CATALYTIC SUBUNIT, ATPASE,          
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.GERLITS,J.TIAN,A.DAS,S.TAYLOR,P.LANGAN,T.W.HELLER,A.KOVALEVSKY      
REVDAT   3   01-JUL-15 4XW6    1       JRNL                                     
REVDAT   2   13-MAY-15 4XW6    1       JRNL                                     
REVDAT   1   06-MAY-15 4XW6    0                                                
JRNL        AUTH   O.GERLITS,J.TIAN,A.DAS,P.LANGAN,W.T.HELLER,A.KOVALEVSKY      
JRNL        TITL   PHOSPHORYL TRANSFER REACTION SNAPSHOTS IN CRYSTALS: INSIGHTS 
JRNL        TITL 2 INTO THE MECHANISM OF PROTEIN KINASE A CATALYTIC SUBUNIT.    
JRNL        REF    J.BIOL.CHEM.                  V. 290 15538 2015              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   25925954                                                     
JRNL        DOI    10.1074/JBC.M115.643213                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELX                                                
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.9                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R-VALUE                   
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.190                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.186                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.265                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 1595                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.174                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.170                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.248                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 1390                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 27860                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 2942                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 34                                            
REMARK   3   SOLVENT ATOMS      : 377                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 3302.2                  
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 6                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 11842                   
REMARK   3   NUMBER OF RESTRAINTS                     : 12515                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.015                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.032                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.031                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.095                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.096                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.147                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.080                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4XW6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-FEB-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206406.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-MAR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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                  : NULL                               
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   : 32017                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.04200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.1500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER, SHELX                                         
REMARK 200 STARTING MODEL: 4DH3                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
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       28.65200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.91000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.61400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       48.91000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.65200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.61400            
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: 3380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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 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   SG   CYS B   621     O1   PO4 A   404              0.86            
REMARK 500   O    GLY A   253     O    HOH A   818              1.98            
REMARK 500   O    HOH A   796     O    HOH A   797              2.14            
REMARK 500   O    HOH A   719     O    HOH A   724              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 144   CD  -  NE  -  CZ  ANGL. DEV. =  12.7 DEGREES          
REMARK 500    ARG A 144   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A 144   NE  -  CZ  -  NH2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ASP A 166   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    LYS A 217   N   -  CA  -  C   ANGL. DEV. =  16.6 DEGREES          
REMARK 500    LYS A 217   N   -  CA  -  C   ANGL. DEV. =  16.6 DEGREES          
REMARK 500    LYS A 217   CA  -  C   -  N   ANGL. DEV. = -14.7 DEGREES          
REMARK 500    LYS A 217   CA  -  C   -  N   ANGL. DEV. = -14.3 DEGREES          
REMARK 500    ASP A 241   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG A 270   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    PRO A 321   C   -  N   -  CA  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    GLY A 322   C   -  N   -  CA  ANGL. DEV. =  17.2 DEGREES          
REMARK 500    GLY A 322   C   -  N   -  CA  ANGL. DEV. =  17.7 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    ASP A 166       36.74   -144.89                                   
REMARK 500    ASP A 184       84.15     65.03                                   
REMARK 500    ASN A 216     -161.74   -129.08                                   
REMARK 500    LEU A 273       49.65    -81.79                                   
REMARK 500    LYS A 285      -80.75    -10.84                                   
REMARK 500    PRO A 321      -74.23    -16.50                                   
REMARK 500    SEP A 338      163.56    -48.14                                   
REMARK 500    ILE B 622     -121.61    -98.50                                   
REMARK 500    HIS B 623      -22.68   -160.16                                   
REMARK 500    HIS B 623      -34.37    111.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 HIS B  623     ASP B  624                  138.70                    
REMARK 500 HIS B  623     ASP B  624                  130.87                    
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    LEU A 284         10.99                                           
REMARK 500    ALA B 620        -10.39                                           
REMARK 500    ALA B 620        -10.99                                           
REMARK 500    HIS B 623        -11.18                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 171   OD1                                                    
REMARK 620 2 ASP A 184   OD2  93.4                                              
REMARK 620 3 PO4 A 404   O3   85.7  78.0                                        
REMARK 620 4 ADP A 403   O3B 179.3  86.1  93.7                                  
REMARK 620 5 ADP A 403   O2A  93.3  91.8 169.6  87.2                            
REMARK 620 6 HOH A 712   O    83.2 168.2  90.5  97.2  99.7                      
REMARK 620 N                    1     2     3     4     5                       
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 ASP A 184   OD1                                                    
REMARK 620 2 ASP A 184   OD2  50.1                                              
REMARK 620 3 HOH A 714   O    70.0  87.6                                        
REMARK 620 4 ADP A 403   O1B  70.5  71.6 140.0                                  
REMARK 620 5 PO4 A 404   O2  139.8  89.7 115.0  99.0                            
REMARK 620 6 HOH A 713   O    84.1 133.6  82.9  87.5 135.2                      
REMARK 620 N                    1     2     3     4     5                       
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 ADP A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 404                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4XW4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4XW5   RELATED DB: PDB                                   
DBREF  4XW6 A   14   350  UNP    P05132   KAPCA_MOUSE     15    351             
DBREF  4XW6 B  605   624  PDB    4XW6     4XW6           605    624             
SEQADV 4XW6 HIS A   -5  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 HIS A   -4  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 HIS A   -3  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 HIS A   -2  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 HIS A   -1  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 HIS A    0  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 GLY A    1  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 ASN A    2  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 ALA A    3  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 ALA A    4  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 ALA A    5  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 ALA A    6  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 LYS A    7  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 LYS A    8  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 GLY A    9  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 SER A   10  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 GLU A   11  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 GLN A   12  UNP  P05132              EXPRESSION TAG                 
SEQADV 4XW6 GLU A   13  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 B   20  THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY          
SEQRES   2 B   20  ARG ARG ALA CYS ILE HIS ASP                                  
MODRES 4XW6 SEP A  139  SER  MODIFIED RESIDUE                                   
MODRES 4XW6 TPO A  197  THR  MODIFIED RESIDUE                                   
MODRES 4XW6 SEP A  338  SER  MODIFIED RESIDUE                                   
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    ADP  A 403      27                                                       
HET    PO4  A 404       5                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     TPO PHOSPHONOTHREONINE                                               
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  ADP    C10 H15 N5 O10 P2                                            
FORMUL   6  PO4    O4 P 3-                                                      
FORMUL   7  HOH   *377(H2 O)                                                    
HELIX    1 AA1 SER A   14  THR A   32  1                                  19    
HELIX    2 AA2 GLN A   39  ASP A   41  5                                   3    
HELIX    3 AA3 LYS A   76  LEU A   82  1                                   7    
HELIX    4 AA4 GLN A   84  GLN A   96  1                                  13    
HELIX    5 AA5 GLU A  127  GLY A  136  1                                  10    
HELIX    6 AA6 SEP A  139  LEU A  160  1                                  22    
HELIX    7 AA7 LYS A  168  GLU A  170  5                                   3    
HELIX    8 AA8 THR A  201  LEU A  205  5                                   5    
HELIX    9 AA9 ALA A  206  LEU A  211  1                                   6    
HELIX   10 AB1 LYS A  217  GLY A  234  1                                  18    
HELIX   11 AB2 GLN A  242  GLY A  253  1                                  12    
HELIX   12 AB3 SER A  262  LEU A  273  1                                  12    
HELIX   13 AB4 VAL A  288  ASN A  293  1                                   6    
HELIX   14 AB5 HIS A  294  ALA A  298  5                                   5    
HELIX   15 AB6 ASP A  301  GLN A  307  1                                   7    
HELIX   16 AB7 THR B  606  ALA B  612  1                                   7    
SHEET    1 AA1 5 PHE A  43  THR A  51  0                                        
SHEET    2 AA1 5 ARG A  56  HIS A  62 -1  O  LEU A  59   N  LYS A  47           
SHEET    3 AA1 5 HIS A  68  ASP A  75 -1  O  MET A  71   N  MET A  58           
SHEET    4 AA1 5 ASN A 115  GLU A 121 -1  O  LEU A 116   N  LEU A  74           
SHEET    5 AA1 5 LEU A 106  LYS A 111 -1  N  PHE A 108   O  VAL A 119           
SHEET    1 AA2 2 LEU A 162  ILE A 163  0                                        
SHEET    2 AA2 2 LYS A 189  ARG A 190 -1  O  LYS A 189   N  ILE A 163           
SHEET    1 AA3 2 LEU A 172  ILE A 174  0                                        
SHEET    2 AA3 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  1.32  
LINK         OD1 ASN A 171                MG    MG A 402     1555   1555  2.20  
LINK         OD1 ASP A 184                MG    MG A 401     1555   1555  2.73  
LINK         OD2 ASP A 184                MG    MG A 402     1555   1555  2.29  
LINK         OD2 ASP A 184                MG    MG A 401     1555   1555  2.25  
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  1.32  
LINK         C   SEP A 338                 N   ILE A 339     1555   1555  1.33  
LINK        MG    MG A 401                 O   HOH A 714     1555   1555  2.19  
LINK        MG    MG A 401                 O1B ADP A 403     1555   1555  2.37  
LINK        MG    MG A 401                 O2  PO4 A 404     1555   1555  2.13  
LINK        MG    MG A 401                 O   HOH A 713     1555   1555  2.34  
LINK        MG    MG A 402                 O3  PO4 A 404     1555   1555  2.48  
LINK        MG    MG A 402                 O3B ADP A 403     1555   1555  2.07  
LINK        MG    MG A 402                 O2A ADP A 403     1555   1555  1.92  
LINK        MG    MG A 402                 O   HOH A 712     1555   1555  2.35  
SITE     1 AC1  5 ASP A 184  ADP A 403  PO4 A 404  HOH A 713                    
SITE     2 AC1  5 HOH A 714                                                     
SITE     1 AC2  5 ASN A 171  ASP A 184  ADP A 403  PO4 A 404                    
SITE     2 AC2  5 HOH A 712                                                     
SITE     1 AC3 25 LEU A  49  GLY A  50  GLY A  52  SER A  53                    
SITE     2 AC3 25 PHE A  54  VAL A  57  ALA A  70  LYS A  72                    
SITE     3 AC3 25 MET A 120  GLU A 121  TYR A 122  VAL A 123                    
SITE     4 AC3 25 GLU A 127  GLU A 170  ASN A 171  LEU A 173                    
SITE     5 AC3 25 THR A 183  ASP A 184  PHE A 327   MG A 401                    
SITE     6 AC3 25  MG A 402  PO4 A 404  HOH A 691  HOH A 712                    
SITE     7 AC3 25 ARG B 618                                                     
SITE     1 AC4  9 SER A  53  ASP A 166  LYS A 168  ASN A 171                    
SITE     2 AC4  9 ASP A 184   MG A 401   MG A 402  ADP A 403                    
SITE     3 AC4  9 CYS B 621                                                     
CRYST1   57.304   79.228   97.820  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      0.017451  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012622  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010223        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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