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Database: PDB
Entry: 3AGL
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Original site: 3AGL 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       02-APR-10   3AGL              
TITLE     COMPLEX OF PKA WITH THE BISUBSTRATE PROTEIN KINASE INHIBITOR ARC-1039 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PKA C-ALPHA;                                                
COMPND   5 EC: 2.7.11.11;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PKACA, PRKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIL;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-285B(+)                               
KEYWDS    PKA, PROTEIN KINASE A, BISUBSTRATE INHIBITOR, ARC-1039, TRANSFERASE-  
KEYWDS   2 TRANSFERASE INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.PFLUG,J.RAGOZINA,A.URI,D.BOSSEMEYER,R.A.ENGH                        
REVDAT   2   13-JUL-11 3AGL    1       VERSN                                    
REVDAT   1   01-SEP-10 3AGL    0                                                
JRNL        AUTH   A.PFLUG,J.ROGOZINA,D.LAVOGINA,E.ENKVIST,A.URI,R.A.ENGH,      
JRNL        AUTH 2 D.BOSSEMEYER                                                 
JRNL        TITL   DIVERSITY OF BISUBSTRATE BINDING MODES OF ADENOSINE          
JRNL        TITL 2 ANALOGUE-OLIGOARGININE CONJUGATES IN PROTEIN KINASE A AND    
JRNL        TITL 3 IMPLICATIONS FOR PROTEIN SUBSTRATE INTERACTIONS.             
JRNL        REF    J.MOL.BIOL.                   V. 403    66 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20732331                                                     
JRNL        DOI    10.1016/J.JMB.2010.08.028                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 52.32                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 46179                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2459                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3351                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2220                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 185                          
REMARK   3   BIN FREE R VALUE                    : 0.2740                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5607                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 126                                     
REMARK   3   SOLVENT ATOMS            : 235                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.03000                                             
REMARK   3    B22 (A**2) : -0.15000                                             
REMARK   3    B33 (A**2) : 0.17000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.219         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.182         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.115         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.216         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5883 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7939 ; 1.258 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   676 ; 5.361 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   286 ;36.061 ;24.126       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1040 ;14.529 ;15.043       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;19.737 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   826 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4456 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3390 ; 0.697 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5478 ; 1.323 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2493 ; 2.020 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2461 ; 3.315 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   -10        A  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.0430   0.1720   7.8720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0221 T22:   0.0727                                     
REMARK   3      T33:   0.0281 T12:  -0.0036                                     
REMARK   3      T13:   0.0111 T23:   0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7220 L22:   2.2964                                     
REMARK   3      L33:   1.1376 L12:   0.0636                                     
REMARK   3      L13:   0.1115 L23:  -0.9219                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0228 S12:   0.0648 S13:   0.0415                       
REMARK   3      S21:  -0.0506 S22:  -0.0318 S23:  -0.1704                       
REMARK   3      S31:  -0.0971 S32:   0.0843 S33:   0.0547                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   -10        B  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.2590  50.0330 -25.2330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0209 T22:   0.0524                                     
REMARK   3      T33:   0.0313 T12:  -0.0018                                     
REMARK   3      T13:   0.0030 T23:   0.0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1787 L22:   2.4223                                     
REMARK   3      L33:   0.7760 L12:  -0.0045                                     
REMARK   3      L13:   0.2126 L23:  -0.4926                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0114 S12:   0.0987 S13:   0.1863                       
REMARK   3      S21:  -0.0641 S22:  -0.0147 S23:  -0.0565                       
REMARK   3      S31:  -0.0987 S32:   0.0097 S33:   0.0262                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3AGL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029227.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 6.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.23985                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48701                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 52.320                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : 0.09600                            
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) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.41300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1CDK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 80 MM MES-BISTRIS, 75 MM LICL, 1.5 MM    
REMARK 280  OCTANOYL-N-METHYLGLUCAMIDE; MIXED 2:1 WITH AND EQUILIBRATED         
REMARK 280  AGAINST 40%(V/V) MPD, PH 6.9, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  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       36.59000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.23500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.58500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.23500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.59000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.58500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     MET 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     MET B     0                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     SEP B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     GLN B    12                                                      
REMARK 465     GLU B    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   NH2  ARG A   336     O1P  SEP A   338              2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD1  ASP A   328     NH1  ARG B   194     4455     1.63            
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    THR A  37       97.23     88.92                                   
REMARK 500    ALA A  38      162.47    148.92                                   
REMARK 500    ASP A 166       37.28   -147.08                                   
REMARK 500    ASP A 184       83.52     64.25                                   
REMARK 500    LEU A 273       42.04    -85.08                                   
REMARK 500    LYS A 319       47.48   -103.03                                   
REMARK 500    ASP B 112     -158.79   -135.70                                   
REMARK 500    ASP B 166       36.91   -143.21                                   
REMARK 500    ASP B 184       88.92     64.04                                   
REMARK 500    ASN B 216     -162.57   -126.01                                   
REMARK 500    LEU B 273       41.15    -90.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: (10R,20R,23R)-1-[(2S,3S,4R,5R)-5-(6-AMINO-9H-PURIN-   
REMARK 630 9-YL)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL]-20,23-BIS(3-                
REMARK 630 CARBAMIMIDAMIDOPROPYL)-10-METHYL-1,8,11,18,21-PENTAOXO-2,9,12,19,    
REMARK 630 22-PENTAAZATETRACOSAN-24-AMIDE                                       
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     A03 A   351                                                      
REMARK 630     A03 B   351                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    44A ACA DAL ACA DAR DAR NH2                              
REMARK 630 DETAILS: NULL                                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A03 A 351                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A03 B 351                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3BWJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3AG9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3AGM   RELATED DB: PDB                                   
DBREF  3AGL A    0   350  UNP    P17612   KAPCA_HUMAN      1    351             
DBREF  3AGL B    0   350  UNP    P17612   KAPCA_HUMAN      1    351             
SEQRES   1 A  351  MET GLY ASN ALA ALA ALA ALA LYS LYS GLY SEP GLU GLN          
SEQRES   2 A  351  GLU SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP          
SEQRES   3 A  351  PHE LEU LYS LYS TRP GLU SER PRO ALA GLN ASN THR ALA          
SEQRES   4 A  351  HIS LEU ASP GLN PHE GLU ARG ILE LYS THR LEU GLY THR          
SEQRES   5 A  351  GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU          
SEQRES   6 A  351  THR GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN          
SEQRES   7 A  351  LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN          
SEQRES   8 A  351  GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU          
SEQRES   9 A  351  VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU          
SEQRES  10 A  351  TYR MET VAL MET GLU TYR VAL PRO GLY GLY GLU MET PHE          
SEQRES  11 A  351  SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS          
SEQRES  12 A  351  ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU          
SEQRES  13 A  351  TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS          
SEQRES  14 A  351  PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN          
SEQRES  15 A  351  VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG          
SEQRES  16 A  351  THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO          
SEQRES  17 A  351  GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP          
SEQRES  18 A  351  TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA          
SEQRES  19 A  351  GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE          
SEQRES  20 A  351  TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER          
SEQRES  21 A  351  HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU          
SEQRES  22 A  351  LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS          
SEQRES  23 A  351  ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA          
SEQRES  24 A  351  THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU          
SEQRES  25 A  351  ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR          
SEQRES  26 A  351  SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL          
SEQRES  27 A  351  SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE SER GLU PHE          
SEQRES   1 B  351  MET GLY ASN ALA ALA ALA ALA LYS LYS GLY SEP GLU GLN          
SEQRES   2 B  351  GLU SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP          
SEQRES   3 B  351  PHE LEU LYS LYS TRP GLU SER PRO ALA GLN ASN THR ALA          
SEQRES   4 B  351  HIS LEU ASP GLN PHE GLU ARG ILE LYS THR LEU GLY THR          
SEQRES   5 B  351  GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU          
SEQRES   6 B  351  THR GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN          
SEQRES   7 B  351  LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN          
SEQRES   8 B  351  GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU          
SEQRES   9 B  351  VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU          
SEQRES  10 B  351  TYR MET VAL MET GLU TYR VAL PRO GLY GLY GLU MET PHE          
SEQRES  11 B  351  SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS          
SEQRES  12 B  351  ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU          
SEQRES  13 B  351  TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS          
SEQRES  14 B  351  PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN          
SEQRES  15 B  351  VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG          
SEQRES  16 B  351  THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO          
SEQRES  17 B  351  GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP          
SEQRES  18 B  351  TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA          
SEQRES  19 B  351  GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE          
SEQRES  20 B  351  TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER          
SEQRES  21 B  351  HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU          
SEQRES  22 B  351  LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS          
SEQRES  23 B  351  ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA          
SEQRES  24 B  351  THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU          
SEQRES  25 B  351  ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR          
SEQRES  26 B  351  SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL          
SEQRES  27 B  351  SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE SER GLU PHE          
MODRES 3AGL SEP A   10  SER  PHOSPHOSERINE                                      
MODRES 3AGL TPO A  197  THR  PHOSPHOTHREONINE                                   
MODRES 3AGL SEP A  338  SER  PHOSPHOSERINE                                      
MODRES 3AGL TPO B  197  THR  PHOSPHOTHREONINE                                   
MODRES 3AGL SEP B  338  SER  PHOSPHOSERINE                                      
HET    SEP  A  10      10                                                       
HET    TPO  A 197      11                                                       
HET    SEP  A 338      10                                                       
HET    TPO  B 197      11                                                       
HET    SEP  B 338      10                                                       
HET    A03  A 351      63                                                       
HET    A03  B 351      63                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     A03 (10R,20R,23R)-1-[(2S,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-            
HETNAM   2 A03  YL)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL]-20,23-BIS(3-             
HETNAM   3 A03  CARBAMIMIDAMIDOPROPYL)-10-METHYL-1,8,11,18,21-                  
HETNAM   4 A03  PENTAOXO-2,9,12,19,22-PENTAAZATETRACOSAN-24-AMIDE               
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     A03 ARC-1039                                                         
FORMUL   1  SEP    3(C3 H8 N O6 P)                                              
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   3  A03    2(C37 H63 N17 O9)                                            
FORMUL   5  HOH   *235(H2 O)                                                    
HELIX    1   1 SEP A   10  SER A   32  1                                  23    
HELIX    2   2 HIS A   39  ASP A   41  5                                   3    
HELIX    3   3 LYS A   76  LEU A   82  1                                   7    
HELIX    4   4 GLN A   84  VAL A   98  1                                  15    
HELIX    5   5 GLU A  127  GLY A  136  1                                  10    
HELIX    6   6 SER 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  SER A  252  1                                  11    
HELIX   12  12 SER A  262  LEU A  273  1                                  12    
HELIX   13  13 ASP A  276  ARG A  280  5                                   5    
HELIX   14  14 VAL A  288  ASN A  293  1                                   6    
HELIX   15  15 HIS A  294  ALA A  298  5                                   5    
HELIX   16  16 ASP A  301  GLN A  307  1                                   7    
HELIX   17  17 SER B   14  SER B   32  1                                  19    
HELIX   18  18 HIS B   39  ASP B   41  5                                   3    
HELIX   19  19 LYS B   76  LEU B   82  1                                   7    
HELIX   20  20 GLN B   84  VAL B   98  1                                  15    
HELIX   21  21 GLU B  127  GLY B  136  1                                  10    
HELIX   22  22 SER B  139  LEU B  160  1                                  22    
HELIX   23  23 LYS B  168  GLU B  170  5                                   3    
HELIX   24  24 THR B  201  LEU B  205  5                                   5    
HELIX   25  25 ALA B  206  LEU B  211  1                                   6    
HELIX   26  26 LYS B  217  GLY B  234  1                                  18    
HELIX   27  27 GLN B  242  GLY B  253  1                                  12    
HELIX   28  28 SER B  262  LEU B  273  1                                  12    
HELIX   29  29 ASP B  276  ARG B  280  5                                   5    
HELIX   30  30 VAL B  288  ASN B  293  1                                   6    
HELIX   31  31 HIS B  294  ALA B  298  5                                   5    
HELIX   32  32 ASP B  301  GLN B  307  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  VAL A  57   N  LEU A  49           
SHEET    3   A 5 HIS A  68  ASP A  75 -1  O  MET A  71   N  MET A  58           
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           
SHEET    1   D 5 PHE B  43  THR B  51  0                                        
SHEET    2   D 5 GLY B  55  HIS B  62 -1  O  LYS B  61   N  GLU B  44           
SHEET    3   D 5 HIS B  68  ASP B  75 -1  O  MET B  71   N  MET B  58           
SHEET    4   D 5 ASN B 115  GLU B 121 -1  O  MET B 120   N  ALA B  70           
SHEET    5   D 5 LEU B 106  LYS B 111 -1  N  GLU B 107   O  VAL B 119           
SHEET    1   E 2 LEU B 162  ILE B 163  0                                        
SHEET    2   E 2 LYS B 189  ARG B 190 -1  O  LYS B 189   N  ILE B 163           
SHEET    1   F 2 LEU B 172  ILE B 174  0                                        
SHEET    2   F 2 ILE B 180  VAL B 182 -1  O  GLN B 181   N  LEU B 173           
LINK         C   SEP A  10                 N   GLU A  11     1555   1555  1.33  
LINK         C   TRP A 196                 N   TPO A 197     1555   1555  1.34  
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         C   TRP B 196                 N   TPO B 197     1555   1555  1.34  
LINK         C   TPO B 197                 N   LEU B 198     1555   1555  1.33  
LINK         C   VAL B 337                 N   SEP B 338     1555   1555  1.33  
LINK         C   SEP B 338                 N   ILE B 339     1555   1555  1.33  
CISPEP   1 ASN A   36    THR A   37          0         8.76                     
SITE     1 AC1 28 GLY A  52  SER A  53  PHE A  54  GLY A  55                    
SITE     2 AC1 28 VAL A  57  ALA A  70  VAL A 104  MET A 120                    
SITE     3 AC1 28 GLU A 121  TYR A 122  VAL A 123  GLU A 127                    
SITE     4 AC1 28 PHE A 129  ARG A 133  PRO A 169  GLU A 170                    
SITE     5 AC1 28 LEU A 173  THR A 183  GLU A 203  GLU A 230                    
SITE     6 AC1 28 PHE A 327  TYR A 330  HOH A 362  HOH A 370                    
SITE     7 AC1 28 HOH A 411  HOH A 447  HOH A 466  LYS B 192                    
SITE     1 AC2 27 LYS A 192  LEU B  49  THR B  51  GLY B  52                    
SITE     2 AC2 27 SER B  53  PHE B  54  GLY B  55  VAL B  57                    
SITE     3 AC2 27 ALA B  70  VAL B 104  GLU B 121  TYR B 122                    
SITE     4 AC2 27 VAL B 123  GLU B 127  PHE B 129  ARG B 133                    
SITE     5 AC2 27 PRO B 169  GLU B 170  LEU B 173  THR B 183                    
SITE     6 AC2 27 GLU B 230  PHE B 327  HOH B 375  HOH B 390                    
SITE     7 AC2 27 HOH B 401  HOH B 446  HOH B 448                               
CRYST1   73.180  105.170  106.470  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013665  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009508  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009392        0.00000                         
HETATM    1  N   SEP A  10       6.181 -23.207  -0.768  1.00 63.59           N  
HETATM    2  CA  SEP A  10       5.805 -22.979  -2.194  1.00 64.67           C  
HETATM    3  CB  SEP A  10       5.542 -24.309  -2.914  1.00 66.56           C  
HETATM    4  OG  SEP A  10       4.719 -24.115  -4.060  1.00 68.94           O  
HETATM    5  C   SEP A  10       4.590 -22.067  -2.294  1.00 62.04           C  
HETATM    6  O   SEP A  10       4.620 -21.042  -2.978  1.00 61.63           O  
HETATM    7  P   SEP A  10       5.390 -24.671  -5.427  1.00 75.51           P  
HETATM    8  O1P SEP A  10       6.189 -26.051  -5.155  1.00 77.04           O  
HETATM    9  O2P SEP A  10       6.405 -23.571  -6.028  1.00 75.98           O  
HETATM   10  O3P SEP A  10       4.225 -24.928  -6.516  1.00 75.44           O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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