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Database: PDB
Entry: 3AC5
LinkDB: 3AC5
Original site: 3AC5 
HEADER    TRANSFERASE                             28-DEC-09   3AC5              
TITLE     CRYSTAL STRUCTURE OF TRIAZOLO PYRIMIDINE DERIVATIVE BOUND TO THE      
TITLE    2 KINASE DOMAIN OF HUMAN LCK, (AUTO-PHOSPHORYLATED ON TYR394)          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE LCK;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 225-509;                                      
COMPND   5 SYNONYM: LYMPHOCYTE KINASE, LCK, LYMPHOCYTE CELL-SPECIFIC PROTEIN-   
COMPND   6 TYROSINE KINASE, P56-LCK, LSK, T CELL-SPECIFIC PROTEIN-TYROSINE      
COMPND   7 KINASE;                                                              
COMPND   8 EC: 2.7.10.2;                                                        
COMPND   9 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: LCK;                                                           
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET-19B                                    
KEYWDS    TYROSINE-PROTEIN KINASE, ATP-BINDING, PHOSPHORYLATION, SIGNAL         
KEYWDS   2 TRANSDUCTION, KINASE, SH2 DOMAIN, SH3 DOMAIN, TRANSFERASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.TSUJI                                                               
REVDAT   1   30-JUN-10 3AC5    0                                                
JRNL        AUTH   M.OZAWA,T.OZAWA,E.TSUJI,K.OKAZAKI,K.TAKEDA                   
JRNL        TITL   AB INITIO MOLECULAR ORBITAL STUDY OF LIGAND BINDING TO       
JRNL        TITL 2 LEUKOCYTE-SPECIFIC PROTEIN TYROSINE (LCK) KINASE             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 9219                           
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) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1005                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 631                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.86                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2030                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 73                           
REMARK   3   BIN FREE R VALUE                    : 0.3570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2210                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 176                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.88000                                             
REMARK   3    B22 (A**2) : 0.73000                                              
REMARK   3    B33 (A**2) : 0.15000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.357         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.219         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.589         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.854                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2317 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3148 ; 1.119 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.479 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   109 ;35.858 ;23.761       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   395 ;15.950 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;16.546 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   335 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1759 ; 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):  1354 ; 0.985 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2194 ; 1.832 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   963 ; 2.920 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   954 ; 4.556 ; 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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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: NULL                                      
REMARK   4                                                                      
REMARK   4 3AC5 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-JAN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029071.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUL-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL32B2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU JUPITER 210                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10437                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.480                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : 0.07600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.13400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.15200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 10.700                             
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 3LCK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M (NH4)2SO4, 0.1M SODIUM              
REMARK 280  CACODYLATE, 30% PEG 8000, 0.2% MPD, PH 6.5, VAPOR DIFFUSION,        
REMARK 280  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       21.15150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.30150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.90450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       46.30150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.15150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.90450            
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 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 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     GLN A   225                                                      
REMARK 465     THR A   226                                                      
REMARK 465     GLN A   227                                                      
REMARK 465     LYS A   228                                                      
REMARK 465     PRO A   229                                                      
REMARK 465     GLN A   230                                                      
REMARK 465     GLY A   503                                                      
REMARK 465     GLN A   504                                                      
REMARK 465     TYR A   505                                                      
REMARK 465     GLN A   506                                                      
REMARK 465     PRO A   507                                                      
REMARK 465     GLN A   508                                                      
REMARK 465     PRO A   509                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 502    CA   C    O    CB   CG   CD   OE1                   
REMARK 470     GLU A 502    OE2                                                 
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   NH1  ARG A   438     O    HOH A   176              1.88            
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    VAL A 248      -62.81   -102.81                                   
REMARK 500    ASN A 265       44.80     39.55                                   
REMARK 500    LEU A 295       63.35   -114.59                                   
REMARK 500    ARG A 363       -8.64     77.33                                   
REMARK 500    ASP A 382       72.52     59.74                                   
REMARK 500    ASP A 391       59.77   -111.47                                   
REMARK 500    ASN A 392      -29.16     66.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 160        DISTANCE =  6.66 ANGSTROMS                       
REMARK 525    HOH A 165        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH A 170        DISTANCE =  6.98 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KZM A 513                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3LCK   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL BASIS FOR ACTIVATION OF HUMAN LYMPHOCYTE KINASE           
REMARK 900 LCK UPON TYROSINE PHOSPHORYLATION NATURE VOL. 384, 484, 1996         
REMARK 900 RELATED ID: 3AC1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3AC2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3AC3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3AC4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3AC8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3ACJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3ACK   RELATED DB: PDB                                   
DBREF  3AC5 A  225   509  UNP    P06239   LCK_HUMAN      225    509             
SEQRES   1 A  285  GLN THR GLN LYS PRO GLN LYS PRO TRP TRP GLU ASP GLU          
SEQRES   2 A  285  TRP GLU VAL PRO ARG GLU THR LEU LYS LEU VAL GLU ARG          
SEQRES   3 A  285  LEU GLY ALA GLY GLN PHE GLY GLU VAL TRP MET GLY TYR          
SEQRES   4 A  285  TYR ASN GLY HIS THR LYS VAL ALA VAL LYS SER LEU LYS          
SEQRES   5 A  285  GLN GLY SER MET SER PRO ASP ALA PHE LEU ALA GLU ALA          
SEQRES   6 A  285  ASN LEU MET LYS GLN LEU GLN HIS GLN ARG LEU VAL ARG          
SEQRES   7 A  285  LEU TYR ALA VAL VAL THR GLN GLU PRO ILE TYR ILE ILE          
SEQRES   8 A  285  THR GLU TYR MET GLU ASN GLY SER LEU VAL ASP PHE LEU          
SEQRES   9 A  285  LYS THR PRO SER GLY ILE LYS LEU THR ILE ASN LYS LEU          
SEQRES  10 A  285  LEU ASP MET ALA ALA GLN ILE ALA GLU GLY MET ALA PHE          
SEQRES  11 A  285  ILE GLU GLU ARG ASN TYR ILE HIS ARG ASP LEU ARG ALA          
SEQRES  12 A  285  ALA ASN ILE LEU VAL SER ASP THR LEU SER CYS LYS ILE          
SEQRES  13 A  285  ALA ASP PHE GLY LEU ALA ARG LEU ILE GLU ASP ASN GLU          
SEQRES  14 A  285  PTR THR ALA ARG GLU GLY ALA LYS PHE PRO ILE LYS TRP          
SEQRES  15 A  285  THR ALA PRO GLU ALA ILE ASN TYR GLY THR PHE THR ILE          
SEQRES  16 A  285  LYS SER ASP VAL TRP SER PHE GLY ILE LEU LEU THR GLU          
SEQRES  17 A  285  ILE VAL THR HIS GLY ARG ILE PRO TYR PRO GLY MET THR          
SEQRES  18 A  285  ASN PRO GLU VAL ILE GLN ASN LEU GLU ARG GLY TYR ARG          
SEQRES  19 A  285  MET VAL ARG PRO ASP ASN CYS PRO GLU GLU LEU TYR GLN          
SEQRES  20 A  285  LEU MET ARG LEU CYS TRP LYS GLU ARG PRO GLU ASP ARG          
SEQRES  21 A  285  PRO THR PHE ASP TYR LEU ARG SER VAL LEU GLU ASP PHE          
SEQRES  22 A  285  PHE THR ALA THR GLU GLY GLN TYR GLN PRO GLN PRO              
MODRES 3AC5 PTR A  394  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  A 394      16                                                       
HET    SO4  A 510       5                                                       
HET    SO4  A 511       5                                                       
HET    DMS  A 512       4                                                       
HET    KZM  A 513      38                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     KZM 5-{[(1R,2S)-2-AMINOCYCLOHEXYL]AMINO}-7-[(3,5-                    
HETNAM   2 KZM  DIMETHOXYPHENYL)AMINO]-2-(3-HYDROXYPHENYL)[1,2,                 
HETNAM   3 KZM  4]TRIAZOLO[1,5-C]PYRIMIDINE-8-CARBOXAMIDE                       
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  PTR    C9 H12 N O6 P                                                
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4  DMS    C2 H6 O S                                                    
FORMUL   5  KZM    C26 H30 N8 O4                                                
FORMUL   6  HOH   *176(H2 O)                                                    
HELIX    1   1 PRO A  241  GLU A  243  5                                   3    
HELIX    2   2 SER A  281  LEU A  295  1                                  15    
HELIX    3   3 SER A  323  LEU A  328  1                                   6    
HELIX    4   4 THR A  330  LYS A  335  1                                   6    
HELIX    5   5 THR A  337  ARG A  358  1                                  22    
HELIX    6   6 ARG A  366  ALA A  368  5                                   3    
HELIX    7   7 ALA A  408  GLY A  415  1                                   8    
HELIX    8   8 THR A  418  THR A  435  1                                  18    
HELIX    9   9 THR A  445  ARG A  455  1                                  11    
HELIX   10  10 PRO A  466  TRP A  477  1                                  12    
HELIX   11  11 ARG A  480  ARG A  484  5                                   5    
HELIX   12  12 THR A  486  THR A  501  1                                  16    
SHEET    1   A 5 LEU A 245  GLY A 254  0                                        
SHEET    2   A 5 GLY A 257  TYR A 264 -1  O  MET A 261   N  GLU A 249           
SHEET    3   A 5 THR A 268  LEU A 275 -1  O  SER A 274   N  GLU A 258           
SHEET    4   A 5 TYR A 313  GLU A 317 -1  O  ILE A 314   N  LYS A 273           
SHEET    5   A 5 LEU A 303  VAL A 307 -1  N  TYR A 304   O  ILE A 315           
SHEET    1   B 2 TYR A 360  ILE A 361  0                                        
SHEET    2   B 2 ARG A 387  LEU A 388 -1  O  ARG A 387   N  ILE A 361           
SHEET    1   C 2 ILE A 370  VAL A 372  0                                        
SHEET    2   C 2 CYS A 378  ILE A 380 -1  O  LYS A 379   N  LEU A 371           
SHEET    1   D 2 PTR A 394  THR A 395  0                                        
SHEET    2   D 2 THR A 416  PHE A 417 -1  O  PHE A 417   N  PTR A 394           
LINK         C   GLU A 393                 N   PTR A 394     1555   1555  1.33  
LINK         C   PTR A 394                 N   THR A 395     1555   1555  1.33  
CISPEP   1 GLU A  310    PRO A  311          0         0.10                     
SITE     1 AC1  9 HOH A  65  HOH A 108  GLN A 298  ARG A 299                    
SITE     2 AC1  9 SER A 377  LYS A 379  TYR A 457  ARG A 458                    
SITE     3 AC1  9 ARG A 474                                                     
SITE     1 AC2  4 TYR A 263  GLY A 266  HIS A 267  TYR A 489                    
SITE     1 AC3  4 HOH A  63  TRP A 233  GLU A 239  GLN A 309                    
SITE     1 AC4 12 HOH A 100  LEU A 251  GLU A 288  ILE A 314                    
SITE     2 AC4 12 THR A 316  GLU A 317  TYR A 318  MET A 319                    
SITE     3 AC4 12 GLU A 320  GLY A 322  LEU A 371  ASP A 382                    
CRYST1   42.303   73.809   92.603  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      0.023639  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013549  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010799        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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