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Database: PDB
Entry: 2ERZ
LinkDB: 2ERZ
Original site: 2ERZ 
HEADER    TRANSFERASE                             25-OCT-05   2ERZ              
TITLE     CRYSTAL STRUCTURE OF C-AMP DEPENDENT KINASE (PKA) BOUND TO            
TITLE    2 HYDROXYFASUDIL                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC             
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: E;                                                            
COMPND   5 SYNONYM: PKA C-ALPHA;                                                
COMPND   6 EC: 2.7.1.37;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA             
COMPND  10 FORM;                                                                
COMPND  11 CHAIN: I;                                                            
COMPND  12 FRAGMENT: RESIDUES 5-24;                                             
COMPND  13 SYNONYM: PKI-ALPHA, CAMP- DEPENDENT PROTEIN KINASE                   
COMPND  14 INHIBITOR, MUSCLE/BRAIN ISOFORM;                                     
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 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 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN                     
SOURCE  11 ORYCTOLAGUS CUNICULUS (RABBIT)                                       
KEYWDS    FASUDIL KINASE, TRANSFERASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.JACOBS                                                              
REVDAT   3   24-FEB-09 2ERZ    1       VERSN                                    
REVDAT   2   24-JAN-06 2ERZ    1       JRNL   AUTHOR                            
REVDAT   1   08-NOV-05 2ERZ    0                                                
JRNL        AUTH   M.JACOBS,K.HAYAKAWA,L.SWENSON,S.BELLON,M.FLEMING,            
JRNL        AUTH 2 P.TASLIMI,J.DORAN                                            
JRNL        TITL   THE STRUCTURE OF DIMERIC ROCK I REVEALS THE                  
JRNL        TITL 2 MECHANISM FOR LIGAND SELECTIVITY.                            
JRNL        REF    J.BIOL.CHEM.                  V. 281   260 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16249185                                                     
JRNL        DOI    10.1074/JBC.M508847200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2002                                             
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN,ACCELRYS                   
REMARK   3               : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,            
REMARK   3               : YIP,DZAKULA)                                         
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 139000.516                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 22170                          
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) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.287                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1525                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 23695                
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3047                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3360                       
REMARK   3   BIN FREE R VALUE                    : 0.3700                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 229                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.024                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2934                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 61                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.49000                                              
REMARK   3    B22 (A**2) : 3.48000                                              
REMARK   3    B33 (A**2) : -5.97000                                             
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.70                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.670 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.000 ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 5.720 ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 7.320 ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 44.03                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN.TOP                                    
REMARK   3  PARAMETER FILE  2  : INHIB.RTF                                      
REMARK   3  PARAMETER FILE  3  : MASS1.DAT                                      
REMARK   3  PARAMETER FILE  4  : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  1   : PROTEIN_REP.PARAM                              
REMARK   3  TOPOLOGY FILE  2   : WATER_REP.PARAM                                
REMARK   3  TOPOLOGY FILE  3   : MISSING.DAT                                    
REMARK   3  TOPOLOGY FILE  4   : PARMXRAY.XPL                                   
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2ERZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB035019.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAR-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC MIRRORS                      
REMARK 200  OPTICS                         : OSMIC                              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR (MSC/RIGAKU)          
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22293                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.510                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 4.870                              
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1ATP                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: BICINE, PH 7.0, 2% MPD, VAPOR            
REMARK 280  DIFFUSION, HANGING 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       36.39700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.02400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.87550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.02400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.39700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.87550            
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 300 REMARK: BIOLOGICAL ASSEMBLY IS SAME AS ASYM. UNIT: ONE PROTEIN       
REMARK 300 MOLECULE (PKA), ONE INHIBITOR PEPTIDE (PKI), ONE LIGAND              
REMARK 300 (HYDROXYFASUDIL)                                                     
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: 2720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET E     0                                                      
REMARK 465     GLY E     1                                                      
REMARK 465     ASN E     2                                                      
REMARK 465     ALA E     3                                                      
REMARK 465     ALA E     4                                                      
REMARK 465     ALA E     5                                                      
REMARK 465     ALA E     6                                                      
REMARK 465     LYS E     7                                                      
REMARK 465     LYS E     8                                                      
REMARK 465     GLY E     9                                                      
REMARK 465     SER E    10                                                      
REMARK 465     GLU E    11                                                      
REMARK 465     GLN E    12                                                      
REMARK 465     GLU E    13                                                      
REMARK 465     SER E    14                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH I    31     O    HOH I    35              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN E  99      101.48   -164.64                                   
REMARK 500    ASP E 166       40.60   -148.03                                   
REMARK 500    ASP E 184       90.43     70.07                                   
REMARK 500    LEU E 273       45.60    -79.95                                   
REMARK 500    LYS E 319       29.11    -77.39                                   
REMARK 500    HIS I  23      -81.00    -90.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HFS E 351                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ESM   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ROCK 1 BOUND TO FASUDIL                         
REMARK 900 RELATED ID: 2ETR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ROCK I BOUND TO Y-27632                         
REMARK 900 RELATED ID: 2ETO   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ROCK I BOUND TO H-1152P-A DI-                   
REMARK 900 METHYLATED VARIANT OF FASUDIL                                        
REMARK 900 RELATED ID: 2ETK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ROCK 1 BOUND TO HYDROXYFASUDIL                  
DBREF  2ERZ E    0   350  UNP    P05132   KAPCA_MOUSE      0    350             
DBREF  2ERZ I    5    24  UNP    P61926   IPKA_RABIT       5     24             
SEQADV 2ERZ TPO E  197  UNP  P05132    THR   197 MODIFIED RESIDUE               
SEQADV 2ERZ SEP E  338  UNP  P05132    SER   338 MODIFIED RESIDUE               
SEQRES   1 E  351  MET GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN          
SEQRES   2 E  351  GLU SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP          
SEQRES   3 E  351  PHE LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA          
SEQRES   4 E  351  GLN LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR          
SEQRES   5 E  351  GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU          
SEQRES   6 E  351  SER GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN          
SEQRES   7 E  351  LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN          
SEQRES   8 E  351  GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU          
SEQRES   9 E  351  VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU          
SEQRES  10 E  351  TYR MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE          
SEQRES  11 E  351  SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS          
SEQRES  12 E  351  ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU          
SEQRES  13 E  351  TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS          
SEQRES  14 E  351  PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN          
SEQRES  15 E  351  VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG          
SEQRES  16 E  351  THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO          
SEQRES  17 E  351  GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP          
SEQRES  18 E  351  TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA          
SEQRES  19 E  351  GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE          
SEQRES  20 E  351  TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER          
SEQRES  21 E  351  HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU          
SEQRES  22 E  351  LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS          
SEQRES  23 E  351  ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA          
SEQRES  24 E  351  THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU          
SEQRES  25 E  351  ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR          
SEQRES  26 E  351  SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL          
SEQRES  27 E  351  SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE          
SEQRES   1 I   20  THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY          
SEQRES   2 I   20  ARG ARG ASN ALA ILE HIS ASP                                  
MODRES 2ERZ TPO E  197  THR  PHOSPHOTHREONINE                                   
MODRES 2ERZ SEP E  338  SER  PHOSPHOSERINE                                      
HET    TPO  E 197      11                                                       
HET    SEP  E 338      10                                                       
HET    HFS  E 351      21                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     HFS 1-(1-HYDROXY-5-ISOQUINOLINESULFONYL)HOMOPIPERAZINE               
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     HFS HYDROXYFASUDIL                                                   
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   3  HFS    C14 H17 N3 O3 S                                              
FORMUL   4  HOH   *61(H2 O)                                                     
HELIX    1   1 VAL E   15  THR E   32  1                                  18    
HELIX    2   2 GLN E   39  ASP E   41  5                                   3    
HELIX    3   3 LYS E   76  LEU E   82  1                                   7    
HELIX    4   4 GLN E   84  GLN E   96  1                                  13    
HELIX    5   5 GLU E  127  GLY E  136  1                                  10    
HELIX    6   6 SER E  139  LEU E  160  1                                  22    
HELIX    7   7 LYS E  168  GLU E  170  5                                   3    
HELIX    8   8 THR E  201  LEU E  205  5                                   5    
HELIX    9   9 ALA E  206  LEU E  211  1                                   6    
HELIX   10  10 LYS E  217  GLY E  234  1                                  18    
HELIX   11  11 GLN E  242  SER E  252  1                                  11    
HELIX   12  12 SER E  262  LEU E  273  1                                  12    
HELIX   13  13 ASP E  276  ARG E  280  5                                   5    
HELIX   14  14 VAL E  288  ASN E  293  1                                   6    
HELIX   15  15 HIS E  294  ALA E  298  5                                   5    
HELIX   16  16 ASP E  301  GLN E  307  1                                   7    
HELIX   17  17 GLY E  344  THR E  348  5                                   5    
HELIX   18  18 THR I    5  SER I   13  1                                   9    
SHEET    1   A 5 PHE E  43  THR E  51  0                                        
SHEET    2   A 5 ARG E  56  HIS E  62 -1  O  LEU E  59   N  LYS E  47           
SHEET    3   A 5 ASN E  67  ASP E  75 -1  O  ASN E  67   N  HIS E  62           
SHEET    4   A 5 ASN E 115  GLU E 121 -1  O  MET E 120   N  ALA E  70           
SHEET    5   A 5 LEU E 106  LYS E 111 -1  N  PHE E 110   O  TYR E 117           
SHEET    1   B 2 LEU E 162  ILE E 163  0                                        
SHEET    2   B 2 LYS E 189  ARG E 190 -1  O  LYS E 189   N  ILE E 163           
SHEET    1   C 2 LEU E 172  ILE E 174  0                                        
SHEET    2   C 2 ILE E 180  VAL E 182 -1  O  GLN E 181   N  LEU E 173           
LINK         C   TRP E 196                 N   TPO E 197     1555   1555  1.33  
LINK         C   TPO E 197                 N   LEU E 198     1555   1555  1.33  
LINK         C   VAL E 337                 N   SEP E 338     1555   1555  1.33  
LINK         C   SEP E 338                 N   ILE E 339     1555   1555  1.33  
SITE     1 AC1 12 THR E  51  VAL E  57  ALA E  70  GLU E 121                    
SITE     2 AC1 12 TYR E 122  VAL E 123  ASN E 171  LEU E 173                    
SITE     3 AC1 12 THR E 183  ASP E 184  PHE E 327  ARG I  18                    
CRYST1   72.794   75.751   80.048  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      0.013737  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013201  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012493        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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