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Database: PDB
Entry: 2J7T
LinkDB: 2J7T
Original site: 2J7T 
HEADER    TRANSFERASE                             17-OCT-06   2J7T              
TITLE     CRYSTAL STRUCTURE OF HUMAN SERINE THREONINE KINASE-10 BOUND TO SU11274
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE 10;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN, RESIDUES 18-317;                            
COMPND   5 SYNONYM: LYMPHOCYTE-ORIENTED KINASE, SERINE-THREONINE PROTEIN KINASE-
COMPND   6 10;                                                                  
COMPND   7 EC: 2.7.11.1;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    KINASE, TRANSFERASE, ATP-BINDING, CELL CYCLE PROGRESSION,             
KEYWDS   2 PHOSPHORYLATION, DISEASE MUTATION, NUCLEOTIDE- BINDING, LYMPHOCYTE   
KEYWDS   3 ORIENTED KINASE (LOK), SERINE/THREONINE- PROTEIN KINASE,             
KEYWDS   4 SERINE/THREONINE KINASE (STK10A)                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.W.PIKE,P.RELLOS,O.FEDOROV,S.DAS,J.DEBRECZENI,F.SOBOTT,S.WATT,     
AUTHOR   2 P.SAVITSKY,J.ESWARAN,A.P.TURNBULL,E.PAPAGRIGORIOU,E.UGOCHUKWA,       
AUTHOR   3 F.GORREC,C.C.UMEANO,F.VON DELFT,C.H.ARROWSMITH,A.EDWARDS,J.WEIGELT,  
AUTHOR   4 M.SUNDSTROM,S.KNAPP                                                  
REVDAT   4   27-JUN-18 2J7T    1       LINK                                     
REVDAT   3   13-JUL-11 2J7T    1       VERSN                                    
REVDAT   2   24-FEB-09 2J7T    1       VERSN                                    
REVDAT   1   07-NOV-06 2J7T    0                                                
JRNL        AUTH   A.C.W.PIKE,P.RELLOS,F.H.NIESEN,A.TURNBULL,A.W.OLIVER,        
JRNL        AUTH 2 S.A.PARKER,B.E.TURK,L.H.PEARL,S.KNAPP                        
JRNL        TITL   ACTIVATION SEGMENT DIMERIZATION: A MECHANISM FOR KINASE      
JRNL        TITL 2 AUTOPHOSPHORYLATION OF NON-CONSENSUS SITES.                  
JRNL        REF    EMBO J.                       V.  27   704 2008              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   18239682                                                     
JRNL        DOI    10.1038/EMBOJ.2008.8                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 24339                          
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) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1308                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1768                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2610                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 113                          
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2148                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 130                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 28.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.63000                                             
REMARK   3    B22 (A**2) : 2.17000                                              
REMARK   3    B33 (A**2) : -1.55000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.164         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.148         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.110         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.399         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2254 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1455 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3074 ; 1.236 ; 2.000       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3547 ; 1.329 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   281 ; 5.740 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    87 ;29.822 ;24.828       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   357 ;13.425 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;25.418 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   348 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2490 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   409 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   466 ; 0.197 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1500 ; 0.178 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1101 ; 0.169 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1093 ; 0.084 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   111 ; 0.131 ; 0.200       
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):    13 ; 0.508 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    45 ; 0.246 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.139 ; 0.200       
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):  1463 ; 0.567 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2276 ; 0.878 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   927 ; 1.413 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   798 ; 2.232 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    25        A   114                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.6824  45.0702  18.9690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4333 T22:  -0.1861                                     
REMARK   3      T33:   0.0649 T12:   0.2131                                     
REMARK   3      T13:   0.0273 T23:   0.0228                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1009 L22:   4.4656                                     
REMARK   3      L33:   6.3464 L12:  -0.4803                                     
REMARK   3      L13:   0.4614 L23:  -1.2544                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0184 S12:   0.2518 S13:   0.8882                       
REMARK   3      S21:  -0.4543 S22:  -0.0563 S23:  -0.1357                       
REMARK   3      S31:  -1.8438 S32:  -0.3946 S33:   0.0747                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   193        A   212                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.4301  21.1705  -2.5168              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1795 T22:   0.1016                                     
REMARK   3      T33:  -0.1831 T12:  -0.0396                                     
REMARK   3      T13:  -0.0408 T23:   0.0170                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.0572 L22:   3.4439                                     
REMARK   3      L33:  15.1814 L12:   0.1638                                     
REMARK   3      L13:  11.4642 L23:   1.3747                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3818 S12:  -1.3126 S13:   0.7671                       
REMARK   3      S21:   0.4308 S22:   0.0870 S23:  -0.1915                       
REMARK   3      S31:  -0.4614 S32:   0.0719 S33:   0.2949                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   115        A   188                          
REMARK   3    RESIDUE RANGE :   A   213        A   317                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.3276  19.9270  19.1323              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2863 T22:  -0.1979                                     
REMARK   3      T33:  -0.2407 T12:   0.0293                                     
REMARK   3      T13:  -0.0179 T23:  -0.0234                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4371 L22:   1.3964                                     
REMARK   3      L33:   5.2451 L12:   0.1696                                     
REMARK   3      L13:   0.3048 L23:   0.2861                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0410 S12:   0.1901 S13:  -0.1331                       
REMARK   3      S21:  -0.0141 S22:  -0.0377 S23:   0.0432                       
REMARK   3      S31:   0.2289 S32:  -0.3311 S33:  -0.0033                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2J7T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-OCT-06.                  
REMARK 100 THE DEPOSITION ID IS D_1290030248.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-SEP-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.999                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25648                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.520                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.82000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2J51                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 45% PEG300, 0.24M CALCIUM ACETATE,       
REMARK 280  0.1M SODIUM CACODYLATE PH6.5, PH 6.50                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       24.59600            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.48000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       66.90850            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       24.59600            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.48000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       66.90850            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       24.59600            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       56.48000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       66.90850            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       24.59600            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       56.48000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       66.90850            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -49.19200            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     SER A    16                                                      
REMARK 465     MET A    17                                                      
REMARK 465     ARG A    18                                                      
REMARK 465     LYS A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     ARG A    21                                                      
REMARK 465     GLU A    22                                                      
REMARK 465     TYR A    23                                                      
REMARK 465     GLU A    24                                                      
REMARK 465     THR A    69                                                      
REMARK 465     LYS A    70                                                      
REMARK 465     SER A    71                                                      
REMARK 465     GLU A    72                                                      
REMARK 465     ARG A   189                                                      
REMARK 465     ASP A   190                                                      
REMARK 465     SER A   191                                                      
REMARK 465     PHE A   192                                                      
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     VAL A  26    CG1  CG2                                            
REMARK 470     ARG A  27    CD   NE   CZ   NH1  NH2                             
REMARK 470     LEU A  30    CD1  CD2                                            
REMARK 470     GLU A  34    CG   CD   OE1  OE2                                  
REMARK 470     VAL A  35    CG1  CG2                                            
REMARK 470     VAL A  39    CG1  CG2                                            
REMARK 470     GLU A  41    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  49    CG   CD   CE   NZ                                   
REMARK 470     LYS A  54    CD   CE   NZ                                        
REMARK 470     LYS A  56    CG   CD   CE   NZ                                   
REMARK 470     GLU A  57    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  65    NZ                                                  
REMARK 470     GLU A  73    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  74    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  79    CD1                                                 
REMARK 470     ILE A  82    CD1                                                 
REMARK 470     GLU A  83    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  95    CD   CE   NZ                                        
REMARK 470     HIS A 102    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP A 103    CG   OD1  OD2                                       
REMARK 470     GLY A 104    C    O                                              
REMARK 470     LEU A 123    CD1  CD2                                            
REMARK 470     ARG A 152    CD   NE   CZ   NH1  NH2                             
REMARK 470     ILE A 154    CD1                                                 
REMARK 470     LYS A 181    CE   NZ                                             
REMARK 470     LYS A 184    CG   CD   CE   NZ                                   
REMARK 470     LYS A 188    CG   CD   CE   NZ                                   
REMARK 470     ILE A 193    N    CB   CG1  CG2  CD1                             
REMARK 470     MET A 205    CE                                                  
REMARK 470     LYS A 210    CD   CE   NZ                                        
REMARK 470     ASP A 211    CG   OD1  OD2                                       
REMARK 470     MET A 243    CG   SD   CE                                        
REMARK 470     LEU A 247    CD1  CD2                                            
REMARK 470     LYS A 248    NZ                                                  
REMARK 470     LYS A 251    CD   CE   NZ                                        
REMARK 470     LYS A 272    CE   NZ                                             
REMARK 470     GLU A 280    CG   CD   OE1  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   OE1  GLU A   313     O    HOH A  2125              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  29   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A  29   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 157       41.43   -144.62                                   
REMARK 500    ASP A 175       79.65     61.18                                   
REMARK 500    ILE A 233      -44.69     69.89                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1322  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 124   O                                                      
REMARK 620 2 GLU A 313   OE2  78.2                                              
REMARK 620 3 HOH A2028   O    79.9 142.7                                        
REMARK 620 4 HOH A2126   O   143.0  81.7  98.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1320  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 234   OE1                                                    
REMARK 620 2 GLU A 234   OE2  46.7                                              
REMARK 620 3 HOH A2079   O   112.1  67.3                                        
REMARK 620 4 HOH A2029   O    89.5  83.8  66.7                                  
REMARK 620 5 HOH A2078   O    74.4 120.3 152.4  87.0                            
REMARK 620 6 HOH A2080   O    71.4  94.5 135.8 154.4  71.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1319  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 313   OE1                                                    
REMARK 620 2 GLU A 313   OE2  47.9                                              
REMARK 620 3 GLU A 316   OE1  94.0  89.6                                        
REMARK 620 4 GLU A 316   OE2  60.1  88.5  46.2                                  
REMARK 620 5 HOH A2128   O    74.5 120.9 108.7  70.0                            
REMARK 620 6 HOH A2055   O   133.5 162.7  73.2  81.1  68.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1318  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 316   OE2                                                    
REMARK 620 2 HOH A2128   O    88.5                                              
REMARK 620 3 HOH A2125   O    71.7  86.5                                        
REMARK 620 4 HOH A2127   O    70.8 155.3  74.5                                  
REMARK 620 5 GLU A 168   OE1  87.7 112.9  30.3  54.7                            
REMARK 620 6 GLU A 168   OE2  91.8 116.2  35.2  53.4   5.2                      
REMARK 620 7 HOH A2054   O   147.6 120.6  94.6  77.3  68.8  63.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 332  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2016   O                                                      
REMARK 620 2 HOH A2013   O    85.2                                              
REMARK 620 3 HOH A2014   O   108.2  72.6                                        
REMARK 620 4 HOH A2058   O    64.6 134.6  85.1                                  
REMARK 620 5 HOH A2019   O   128.3 146.5  93.7  71.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 333  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2020   O                                                      
REMARK 620 2 HOH A2059   O    59.8                                              
REMARK 620 3 HOH A2129   O   102.3  87.2                                        
REMARK 620 4 HOH A2130   O    71.6 124.0  77.0                                  
REMARK 620 5 HOH A2051   O   156.6 121.9 101.1 113.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1321  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2108   O                                                      
REMARK 620 2 HOH A2039   O   164.2                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 332                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 333                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1318                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1319                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1320                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1321                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1322                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1323                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 274 A1324                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEQUENCE DISCREPANCIES DUE TO CLONING ARTEFACTS                      
DBREF  2J7T A   16    17  PDB    2J7T     2J7T            16     17             
DBREF  2J7T A   18   317  UNP    O94804   STK10_HUMAN     18    317             
SEQRES   1 A  302  SER MET ARG LYS SER ARG GLU TYR GLU HIS VAL ARG ARG          
SEQRES   2 A  302  ASP LEU ASP PRO ASN GLU VAL TRP GLU ILE VAL GLY GLU          
SEQRES   3 A  302  LEU GLY ASP GLY ALA PHE GLY LYS VAL TYR LYS ALA LYS          
SEQRES   4 A  302  ASN LYS GLU THR GLY ALA LEU ALA ALA ALA LYS VAL ILE          
SEQRES   5 A  302  GLU THR LYS SER GLU GLU GLU LEU GLU ASP TYR ILE VAL          
SEQRES   6 A  302  GLU ILE GLU ILE LEU ALA THR CYS ASP HIS PRO TYR ILE          
SEQRES   7 A  302  VAL LYS LEU LEU GLY ALA TYR TYR HIS ASP GLY LYS LEU          
SEQRES   8 A  302  TRP ILE MET ILE GLU PHE CYS PRO GLY GLY ALA VAL ASP          
SEQRES   9 A  302  ALA ILE MET LEU GLU LEU ASP ARG GLY LEU THR GLU PRO          
SEQRES  10 A  302  GLN ILE GLN VAL VAL CYS ARG GLN MET LEU GLU ALA LEU          
SEQRES  11 A  302  ASN PHE LEU HIS SER LYS ARG ILE ILE HIS ARG ASP LEU          
SEQRES  12 A  302  LYS ALA GLY ASN VAL LEU MET THR LEU GLU GLY ASP ILE          
SEQRES  13 A  302  ARG LEU ALA ASP PHE GLY VAL SER ALA LYS ASN LEU LYS          
SEQRES  14 A  302  THR LEU GLN LYS ARG ASP SER PHE ILE GLY THR PRO TYR          
SEQRES  15 A  302  TRP MET ALA PRO GLU VAL VAL MET CYS GLU THR MET LYS          
SEQRES  16 A  302  ASP THR PRO TYR ASP TYR LYS ALA ASP ILE TRP SER LEU          
SEQRES  17 A  302  GLY ILE THR LEU ILE GLU MET ALA GLN ILE GLU PRO PRO          
SEQRES  18 A  302  HIS HIS GLU LEU ASN PRO MET ARG VAL LEU LEU LYS ILE          
SEQRES  19 A  302  ALA LYS SER ASP PRO PRO THR LEU LEU THR PRO SER LYS          
SEQRES  20 A  302  TRP SER VAL GLU PHE ARG ASP PHE LEU LYS ILE ALA LEU          
SEQRES  21 A  302  ASP LYS ASN PRO GLU THR ARG PRO SER ALA ALA GLN LEU          
SEQRES  22 A  302  LEU GLU HIS PRO PHE VAL SER SER ILE THR SER ASN LYS          
SEQRES  23 A  302  ALA LEU ARG GLU LEU VAL ALA GLU ALA LYS ALA GLU VAL          
SEQRES  24 A  302  MET GLU GLU                                                  
HET     CA  A 332       1                                                       
HET     CA  A 333       1                                                       
HET     CA  A1318       1                                                       
HET     CA  A1319       1                                                       
HET     CA  A1320       1                                                       
HET     CA  A1321       1                                                       
HET     CA  A1322       1                                                       
HET    ACT  A1323       4                                                       
HET    274  A1324      46                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     ACT ACETATE ION                                                      
HETNAM     274 (3Z)-N-(3-CHLOROPHENYL)-3-({3,5-DIMETHYL-4-[(4-                  
HETNAM   2 274  METHYLPIPERAZIN-1-YL)CARBONYL]-1H-PYRROL-2-                     
HETNAM   3 274  YL}METHYLENE)-N-METHYL-2-OXOINDOLINE-5-SULFONAMIDE              
HETSYN     274 MET KINASE INHIBITOR                                             
FORMUL   2   CA    7(CA 2+)                                                     
FORMUL   9  ACT    C2 H3 O2 1-                                                  
FORMUL  10  274    C28 H30 CL N5 O4 S                                           
FORMUL  11  HOH   *130(H2 O)                                                    
HELIX    1   1 ASP A   31  GLU A   34  5                                   4    
HELIX    2   2 GLU A   74  CYS A   88  1                                  15    
HELIX    3   3 VAL A  118  ASP A  126  1                                   9    
HELIX    4   4 THR A  130  LYS A  151  1                                  22    
HELIX    5   5 LYS A  159  GLY A  161  5                                   3    
HELIX    6   6 PHE A  176  LYS A  188  1                                  13    
HELIX    7   7 THR A  195  MET A  199  5                                   5    
HELIX    8   8 ALA A  200  MET A  209  1                                  10    
HELIX    9   9 TYR A  216  ILE A  233  1                                  18    
HELIX   10  10 ASN A  241  SER A  252  1                                  12    
HELIX   11  11 THR A  259  TRP A  263  5                                   5    
HELIX   12  12 SER A  264  LEU A  275  1                                  12    
HELIX   13  13 SER A  284  LEU A  289  1                                   6    
HELIX   14  14 ASN A  300  MET A  315  1                                  16    
SHEET    1  AA 5 TRP A  36  GLY A  43  0                                        
SHEET    2  AA 5 VAL A  50  ASN A  55 -1  O  VAL A  50   N  LEU A  42           
SHEET    3  AA 5 LEU A  61  ILE A  67 -1  O  ALA A  62   N  ALA A  53           
SHEET    4  AA 5 LEU A 106  GLU A 111 -1  O  LEU A 106   N  ILE A  67           
SHEET    5  AA 5 LEU A  96  TYR A 101 -1  N  LEU A  97   O  MET A 109           
SHEET    1  AB 3 GLY A 116  ALA A 117  0                                        
SHEET    2  AB 3 VAL A 163  MET A 165 -1  N  MET A 165   O  GLY A 116           
SHEET    3  AB 3 ILE A 171  LEU A 173 -1  O  ARG A 172   N  LEU A 164           
SSBOND   1 CYS A  206    CYS A  206                          1555   3455  2.06  
LINK         O   GLU A 124                CA    CA A1322     1555   1555  2.68  
LINK         OE1 GLU A 234                CA    CA A1320     1555   1555  2.76  
LINK         OE2 GLU A 234                CA    CA A1320     1555   1555  2.77  
LINK         OE1 GLU A 313                CA    CA A1319     1555   1555  2.88  
LINK         OE2 GLU A 313                CA    CA A1322     1555   1555  3.20  
LINK         OE2 GLU A 313                CA    CA A1319     1555   1555  2.40  
LINK         OE1 GLU A 316                CA    CA A1319     1555   1555  2.71  
LINK         OE2 GLU A 316                CA    CA A1319     1555   1555  2.86  
LINK         OE2 GLU A 316                CA    CA A1318     1555   1555  2.20  
LINK        CA    CA A 332                 O   HOH A2016     1555   1555  2.53  
LINK        CA    CA A 332                 O   HOH A2013     1555   1555  2.51  
LINK        CA    CA A 332                 O   HOH A2014     1555   1555  2.56  
LINK        CA    CA A 332                 O   HOH A2058     1555   1555  2.56  
LINK        CA    CA A 332                 O   HOH A2019     1555   1555  2.48  
LINK        CA    CA A 333                 O   HOH A2020     1555   1555  2.39  
LINK        CA    CA A 333                 O   HOH A2059     1555   1555  3.07  
LINK        CA    CA A 333                 O   HOH A2129     1555   1555  2.43  
LINK        CA    CA A 333                 O   HOH A2130     1555   1555  2.61  
LINK        CA    CA A 333                 O   HOH A2051     1555   1555  2.32  
LINK        CA    CA A1318                 O   HOH A2128     1555   1555  2.61  
LINK        CA    CA A1318                 O   HOH A2125     1555   1555  2.43  
LINK        CA    CA A1318                 O   HOH A2127     1555   1555  2.49  
LINK        CA    CA A1319                 O   HOH A2128     1555   1555  3.01  
LINK        CA    CA A1320                 O   HOH A2079     1555   1555  2.98  
LINK        CA    CA A1320                 O   HOH A2029     1555   1555  3.12  
LINK        CA    CA A1320                 O   HOH A2078     1555   1555  2.78  
LINK        CA    CA A1320                 O   HOH A2080     1555   1555  2.49  
LINK        CA    CA A1321                 O   HOH A2108     1555   1555  2.12  
LINK        CA    CA A1321                 O   HOH A2039     1555   1555  2.20  
LINK        CA    CA A1322                 O   HOH A2028     1555   1555  2.27  
LINK        CA    CA A1322                 O   HOH A2126     1555   1555  2.23  
LINK         OE1 GLU A 168                CA    CA A1318     1555   8455  2.50  
LINK         OE2 GLU A 168                CA    CA A1318     1555   8455  2.68  
LINK        CA    CA A1318                 O   HOH A2054     1555   8555  2.37  
LINK        CA    CA A1319                 O   HOH A2055     1555   8555  2.44  
CISPEP   1 THR A  212    PRO A  213          0        -5.00                     
SITE     1 AC1  5 HOH A2013  HOH A2014  HOH A2016  HOH A2019                    
SITE     2 AC1  5 HOH A2058                                                     
SITE     1 AC2  5 HOH A2020  HOH A2051  HOH A2059  HOH A2129                    
SITE     2 AC2  5 HOH A2130                                                     
SITE     1 AC3  6 GLU A 168  GLU A 316  HOH A2054  HOH A2125                    
SITE     2 AC3  6 HOH A2127  HOH A2128                                          
SITE     1 AC4  4 GLU A 313  GLU A 316  HOH A2055  HOH A2128                    
SITE     1 AC5  4 GLU A 234  HOH A2078  HOH A2079  HOH A2080                    
SITE     1 AC6  3 GLN A 135  HOH A2039  HOH A2108                               
SITE     1 AC7  4 GLU A 124  GLU A 313  HOH A2028  HOH A2126                    
SITE     1 AC8  2 THR A 298  VAL A 314                                          
SITE     1 AC9 14 LEU A  42  ALA A  63  GLU A  81  ILE A 108                    
SITE     2 AC9 14 ILE A 110  GLU A 111  PHE A 112  CYS A 113                    
SITE     3 AC9 14 GLY A 116  ALA A 117  LEU A 164  ASP A 175                    
SITE     4 AC9 14 HOH A2007  HOH A2129                                          
CRYST1   49.192  112.960  133.817  90.00  90.00  90.00 I 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020329  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008853  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007473        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system