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Database: PDB
Entry: 1U59
LinkDB: 1U59
Original site: 1U59 
HEADER    TRANSFERASE                             27-JUL-04   1U59              
TITLE     CRYSTAL STRUCTURE OF THE ZAP-70 KINASE DOMAIN IN COMPLEX WITH         
TITLE    2 STAUROSPORINE                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE ZAP-70;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN;                                             
COMPND   5 SYNONYM: 70 KDA ZETA-ASSOCIATED PROTEIN, SYK-RELATED TYROSINE KINASE;
COMPND   6 EC: 2.7.1.112;                                                       
COMPND   7 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: ZAP70, SRK;                                                    
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF+;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PTRIEX AND BACVECTOR                      
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.JIN,S.PLUSKEY,E.C.PETRELLA,S.M.CANTIN,J.C.GORGA,M.J.RYNKIEWICZ,     
AUTHOR   2 P.PANDEY,J.E.STRICKLER,R.E.BABINE,D.T.WEAVER,K.J.SEIDL               
REVDAT   4   11-OCT-17 1U59    1       REMARK                                   
REVDAT   3   24-FEB-09 1U59    1       VERSN                                    
REVDAT   2   12-OCT-04 1U59    1       JRNL                                     
REVDAT   1   17-AUG-04 1U59    0                                                
JRNL        AUTH   L.JIN,S.PLUSKEY,E.C.PETRELLA,S.M.CANTIN,J.C.GORGA,           
JRNL        AUTH 2 M.J.RYNKIEWICZ,P.PANDEY,J.E.STRICKLER,R.E.BABINE,D.T.WEAVER, 
JRNL        AUTH 3 K.J.SEIDL                                                    
JRNL        TITL   THE THREE-DIMENSIONAL STRUCTURE OF THE ZAP-70 KINASE DOMAIN  
JRNL        TITL 2 IN COMPLEX WITH STAUROSPORINE: IMPLICATIONS FOR THE DESIGN   
JRNL        TITL 3 OF SELECTIVE INHIBITORS                                      
JRNL        REF    J.BIOL.CHEM.                  V. 279 42818 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15292186                                                     
JRNL        DOI    10.1074/JBC.M407096200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 498101.360                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 13783                          
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) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.200                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1400                            
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) : 14312                
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.38                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1138                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3220                       
REMARK   3   BIN FREE R VALUE                    : 0.3510                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 11.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 140                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.030                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2281                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 54                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 29.02000                                             
REMARK   3    B22 (A**2) : -12.90000                                            
REMARK   3    B33 (A**2) : -16.12000                                            
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) : 0.30                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.35                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.39                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.39                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.200                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.730                           
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) : 1.360 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.320 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.980 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.910 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 48.18                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : STO.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER_REP.TOP                                  
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : STO.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1U59 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000023261.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-DEC-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 113                                
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 RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : BLUE OSMIC MIRRORS                 
REMARK 200  OPTICS                         : BLUE OSMIC MIRRORS                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14304                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.700                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.500                              
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 1MQB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, DL-MALIC ACID, PH 7.0, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
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       21.52800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.56650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.53200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.56650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.52800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       28.53200            
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: MONOMERIC                         
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 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     ASP A   327                                                      
REMARK 465     MET A   359                                                      
REMARK 465     ARG A   360                                                      
REMARK 465     LYS A   361                                                      
REMARK 465     HIS A   613                                                      
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 341       49.48    -91.12                                   
REMARK 500    CYS A 346     -144.87   -156.97                                   
REMARK 500    LYS A 372      152.56    -49.53                                   
REMARK 500    ALA A 407     -116.75   -133.81                                   
REMARK 500    ARG A 460      -36.80     82.30                                   
REMARK 500    ASP A 479       79.94     60.68                                   
REMARK 500    LYS A 504       -7.44    -59.55                                   
REMARK 500    LYS A 542      -17.21    111.33                                   
REMARK 500    LYS A 544      155.02    179.43                                   
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 STU A 100                 
DBREF  1U59 A  327   606  UNP    P43403   ZAP70_HUMAN    327    606             
SEQADV 1U59 HIS A  607  UNP  P43403              EXPRESSION TAG                 
SEQADV 1U59 HIS A  608  UNP  P43403              EXPRESSION TAG                 
SEQADV 1U59 HIS A  609  UNP  P43403              EXPRESSION TAG                 
SEQADV 1U59 HIS A  610  UNP  P43403              EXPRESSION TAG                 
SEQADV 1U59 HIS A  611  UNP  P43403              EXPRESSION TAG                 
SEQADV 1U59 HIS A  612  UNP  P43403              EXPRESSION TAG                 
SEQADV 1U59 HIS A  613  UNP  P43403              EXPRESSION TAG                 
SEQRES   1 A  287  ASP LYS LYS LEU PHE LEU LYS ARG ASP ASN LEU LEU ILE          
SEQRES   2 A  287  ALA ASP ILE GLU LEU GLY CYS GLY ASN PHE GLY SER VAL          
SEQRES   3 A  287  ARG GLN GLY VAL TYR ARG MET ARG LYS LYS GLN ILE ASP          
SEQRES   4 A  287  VAL ALA ILE LYS VAL LEU LYS GLN GLY THR GLU LYS ALA          
SEQRES   5 A  287  ASP THR GLU GLU MET MET ARG GLU ALA GLN ILE MET HIS          
SEQRES   6 A  287  GLN LEU ASP ASN PRO TYR ILE VAL ARG LEU ILE GLY VAL          
SEQRES   7 A  287  CYS GLN ALA GLU ALA LEU MET LEU VAL MET GLU MET ALA          
SEQRES   8 A  287  GLY GLY GLY PRO LEU HIS LYS PHE LEU VAL GLY LYS ARG          
SEQRES   9 A  287  GLU GLU ILE PRO VAL SER ASN VAL ALA GLU LEU LEU HIS          
SEQRES  10 A  287  GLN VAL SER MET GLY MET LYS TYR LEU GLU GLU LYS ASN          
SEQRES  11 A  287  PHE VAL HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU LEU          
SEQRES  12 A  287  VAL ASN ARG HIS TYR ALA LYS ILE SER ASP PHE GLY LEU          
SEQRES  13 A  287  SER LYS ALA LEU GLY ALA ASP ASP SER TYR TYR THR ALA          
SEQRES  14 A  287  ARG SER ALA GLY LYS TRP PRO LEU LYS TRP TYR ALA PRO          
SEQRES  15 A  287  GLU CYS ILE ASN PHE ARG LYS PHE SER SER ARG SER ASP          
SEQRES  16 A  287  VAL TRP SER TYR GLY VAL THR MET TRP GLU ALA LEU SER          
SEQRES  17 A  287  TYR GLY GLN LYS PRO TYR LYS LYS MET LYS GLY PRO GLU          
SEQRES  18 A  287  VAL MET ALA PHE ILE GLU GLN GLY LYS ARG MET GLU CYS          
SEQRES  19 A  287  PRO PRO GLU CYS PRO PRO GLU LEU TYR ALA LEU MET SER          
SEQRES  20 A  287  ASP CYS TRP ILE TYR LYS TRP GLU ASP ARG PRO ASP PHE          
SEQRES  21 A  287  LEU THR VAL GLU GLN ARG MET ARG ALA CYS TYR TYR SER          
SEQRES  22 A  287  LEU ALA SER LYS VAL GLU GLY HIS HIS HIS HIS HIS HIS          
SEQRES  23 A  287  HIS                                                          
HET    STU  A 100      35                                                       
HETNAM     STU STAUROSPORINE                                                    
FORMUL   2  STU    C28 H26 N4 O3                                                
FORMUL   3  HOH   *54(H2 O)                                                     
HELIX    1   1 LYS A  333  ASP A  335  5                                   3    
HELIX    2   2 GLU A  376  LEU A  393  1                                  18    
HELIX    3   3 LEU A  422  VAL A  427  1                                   6    
HELIX    4   4 PRO A  434  LYS A  455  1                                  22    
HELIX    5   5 ALA A  463  ARG A  465  5                                   3    
HELIX    6   6 PRO A  502  TYR A  506  5                                   5    
HELIX    7   7 ALA A  507  ARG A  514  1                                   8    
HELIX    8   8 SER A  517  SER A  534  1                                  18    
HELIX    9   9 GLY A  545  GLN A  554  1                                  10    
HELIX   10  10 PRO A  565  CYS A  575  1                                  11    
HELIX   11  11 LYS A  579  ARG A  583  5                                   5    
HELIX   12  12 ASP A  585  SER A  602  1                                  18    
SHEET    1   A 5 LEU A 337  GLY A 345  0                                        
SHEET    2   A 5 GLY A 350  TYR A 357 -1  O  VAL A 356   N  LEU A 338           
SHEET    3   A 5 ILE A 364  LEU A 371 -1  O  ILE A 368   N  ARG A 353           
SHEET    4   A 5 LEU A 410  GLU A 415 -1  O  MET A 414   N  ALA A 367           
SHEET    5   A 5 LEU A 401  GLN A 406 -1  N  ILE A 402   O  VAL A 413           
SHEET    1   B 3 GLY A 420  PRO A 421  0                                        
SHEET    2   B 3 VAL A 467  ASN A 471 -1  O  LEU A 469   N  GLY A 420           
SHEET    3   B 3 TYR A 474  ILE A 477 -1  O  LYS A 476   N  LEU A 468           
SHEET    1   C 2 PHE A 457  VAL A 458  0                                        
SHEET    2   C 2 LYS A 484  ALA A 485 -1  O  LYS A 484   N  VAL A 458           
SHEET    1   D 2 TYR A 492  TYR A 493  0                                        
SHEET    2   D 2 LYS A 515  PHE A 516 -1  O  PHE A 516   N  TYR A 492           
SITE     1 AC1 15 HOH A  36  LEU A 344  GLY A 345  VAL A 352                    
SITE     2 AC1 15 ALA A 367  MET A 414  GLU A 415  MET A 416                    
SITE     3 AC1 15 ALA A 417  GLY A 420  ARG A 465  ASN A 466                    
SITE     4 AC1 15 LEU A 468  SER A 478  ASP A 479                               
CRYST1   43.056   57.064  125.133  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      0.023226  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017524  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007991        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system