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Database: PDB
Entry: 4O38
LinkDB: 4O38
Original site: 4O38 
HEADER    TRANSFERASE                             18-DEC-13   4O38              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN CYCLIN G ASSOCIATED KINASE (GAK)       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-G-ASSOCIATED KINASE;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: KINASE DOMAIN (11-347);                                    
COMPND   5 EC: 2.7.11.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GAK;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,             
KEYWDS   2 TRANSFERASE, PROTEIN KINASE, SERINE/THREONINE KINASE, CYCLIN G, P53, 
KEYWDS   3 CLATHRINE, MEMBRANE TRAFFICKING, PSI-2, PROTEIN STRUCTURE            
KEYWDS   4 INITIATIVE, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, ATP-       
KEYWDS   5 BINDING, CELL CYCLE, CELL JUNCTION, GOLGI APPARATUS, KINASE,         
KEYWDS   6 NUCLEOTIDE-BINDING, PHOSPHOPROTEIN                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.ZHANG,C.HATZOS-SKINTGES,A.WEGER,A.CHAIKUAD,J.ESWARAN,O.FEDOROV,     
AUTHOR   2 O.KING,F.VON DELFT,C.BOUNTRA,C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,     
AUTHOR   3 S.KNAPP,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG),  
AUTHOR   4 STRUCTURAL GENOMICS CONSORTIUM (SGC)                                 
REVDAT   2   22-NOV-17 4O38    1       REMARK                                   
REVDAT   1   01-JAN-14 4O38    0                                                
SPRSDE     01-JAN-14 4O38      3LL6                                             
JRNL        AUTH   R.ZHANG,C.HATZOS-SKINTGES,A.WEGER,A.CHAIKUAD,J.ESWARAN,      
JRNL        AUTH 2 O.FEDOROV,O.KING,F.VON DELFT,C.BOUNTRA,C.H.ARROWSMITH,       
JRNL        AUTH 3 J.WEIGELT,A.EDWARDS,S.KNAPP,A.JOACHIMIAK                     
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN CYCLIN G ASSOCIATED KINASE    
JRNL        TITL 2 (GAK)                                                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 74.11                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 45803                          
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) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2442                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3286                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.86                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2230                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 189                          
REMARK   3   BIN FREE R VALUE                    : 0.2500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4268                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 254                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.14000                                             
REMARK   3    B22 (A**2) : -0.14000                                             
REMARK   3    B33 (A**2) : 0.44000                                              
REMARK   3    B12 (A**2) : -0.07000                                             
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): 0.144         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.132         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.093         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.986         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4426 ; 0.016 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4294 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5988 ; 1.568 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9889 ; 1.010 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   555 ; 6.260 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   204 ;35.965 ;24.412       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   762 ;14.402 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;19.066 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   681 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4989 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   999 ; 0.004 ; 0.020       
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):  2184 ; 3.033 ; 3.097       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2183 ; 3.030 ; 3.095       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2724 ; 4.739 ; 4.606       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2725 ; 4.739 ; 4.607       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2242 ; 4.122 ; 3.584       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2240 ; 4.060 ; 3.581       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3255 ; 6.407 ; 5.172       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4955 ;10.411 ;25.267       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4956 ;10.410 ;25.276       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A    26    334       B    26    334   15976  0.10  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
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    68                          
REMARK   3    ORIGIN FOR THE GROUP (A):  64.5986  77.5480  12.2767              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3645 T22:   0.2451                                     
REMARK   3      T33:   0.1469 T12:   0.0280                                     
REMARK   3      T13:   0.0208 T23:  -0.0090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8968 L22:   3.5636                                     
REMARK   3      L33:   4.4851 L12:   0.9203                                     
REMARK   3      L13:   1.7144 L23:   0.8863                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0120 S12:   0.1789 S13:  -0.1029                       
REMARK   3      S21:  -0.2253 S22:  -0.1164 S23:   0.4270                       
REMARK   3      S31:   0.0604 S32:  -0.3458 S33:   0.1043                       
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    69        A   128                          
REMARK   3    ORIGIN FOR THE GROUP (A):  62.6364  68.6434  21.0942              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3033 T22:   0.2253                                     
REMARK   3      T33:   0.1458 T12:   0.0326                                     
REMARK   3      T13:   0.0674 T23:  -0.0431                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1611 L22:   0.9016                                     
REMARK   3      L33:   1.4020 L12:  -0.1049                                     
REMARK   3      L13:  -1.2230 L23:  -0.7136                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0149 S12:   0.1283 S13:   0.1701                       
REMARK   3      S21:   0.0657 S22:   0.1056 S23:  -0.0569                       
REMARK   3      S31:  -0.0654 S32:  -0.1910 S33:  -0.1205                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   129        A   334                          
REMARK   3    ORIGIN FOR THE GROUP (A):  71.7420  48.8926   8.8700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2604 T22:   0.1848                                     
REMARK   3      T33:   0.1572 T12:   0.0403                                     
REMARK   3      T13:   0.1151 T23:  -0.0954                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8120 L22:   1.3402                                     
REMARK   3      L33:   1.2994 L12:  -0.3337                                     
REMARK   3      L13:  -0.8767 L23:   0.6849                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0164 S12:   0.1251 S13:  -0.1594                       
REMARK   3      S21:  -0.0114 S22:  -0.1417 S23:   0.0780                       
REMARK   3      S31:   0.0050 S32:  -0.1203 S33:   0.1580                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    26        B    64                          
REMARK   3    ORIGIN FOR THE GROUP (A):  56.6273  31.2416  47.6705              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5825 T22:   0.0537                                     
REMARK   3      T33:   0.4752 T12:   0.0155                                     
REMARK   3      T13:   0.3031 T23:   0.0416                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9846 L22:  11.0687                                     
REMARK   3      L33:  13.6905 L12:  -0.3629                                     
REMARK   3      L13:  -1.6211 L23:   3.0736                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4679 S12:  -0.0243 S13:  -1.4195                       
REMARK   3      S21:   0.4437 S22:  -0.1112 S23:   0.1544                       
REMARK   3      S31:   1.7448 S32:  -0.6237 S33:   0.5792                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    65        B   169                          
REMARK   3    ORIGIN FOR THE GROUP (A):  53.0588  46.7804  44.3326              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3161 T22:   0.2328                                     
REMARK   3      T33:   0.1275 T12:   0.0540                                     
REMARK   3      T13:   0.0740 T23:  -0.0292                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9200 L22:   0.4999                                     
REMARK   3      L33:   1.9222 L12:   0.4201                                     
REMARK   3      L13:  -1.8884 L23:  -0.5100                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3056 S12:  -0.1103 S13:  -0.2976                       
REMARK   3      S21:  -0.1957 S22:  -0.0566 S23:  -0.0911                       
REMARK   3      S31:   0.3719 S32:   0.0721 S33:   0.3621                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   170        B   262                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.1182  58.6868  40.1171              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2601 T22:   0.2492                                     
REMARK   3      T33:   0.0774 T12:   0.0425                                     
REMARK   3      T13:   0.0100 T23:  -0.0532                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6523 L22:   0.7165                                     
REMARK   3      L33:   1.2104 L12:  -0.1761                                     
REMARK   3      L13:  -0.8460 L23:   0.0812                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0718 S12:   0.1025 S13:  -0.0728                       
REMARK   3      S21:  -0.1960 S22:  -0.1265 S23:  -0.0614                       
REMARK   3      S31:   0.0216 S32:  -0.0548 S33:   0.0548                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   263        B   337                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.0000  63.5814  50.1803              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2291 T22:   0.2489                                     
REMARK   3      T33:   0.1143 T12:   0.0462                                     
REMARK   3      T13:  -0.0068 T23:  -0.0680                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5832 L22:   0.6892                                     
REMARK   3      L33:   3.3693 L12:  -0.4919                                     
REMARK   3      L13:  -0.5198 L23:   0.1905                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0359 S12:   0.0554 S13:   0.0113                       
REMARK   3      S21:  -0.0192 S22:  -0.1239 S23:   0.0695                       
REMARK   3      S31:   0.0717 S32:  -0.1762 S33:   0.0880                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 4O38 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000083985.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794, 0.97912                    
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48245                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.097                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 74.110                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 14.50                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 36.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.95700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: HKL-3000                                              
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M SUCCINIC ACID, 0.1M BIS-TRIS        
REMARK 280  PROPANE, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE         
REMARK 280  289.0K                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       87.96733            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       43.98367            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       43.98367            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       87.96733            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE DIMERIC FORM IN THE ASYMMETRIC UNIT COULD OCCUR AT HIGH  
REMARK 300 CONCENTRATION, AND REPRESENT AN INACTIVE FORM OF THE KINASE.         
REMARK 300 MONOMERIC STATE IS THE ACTIVE FORM.                                  
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 589  LIES ON A SPECIAL POSITION.                          
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    10                                                      
REMARK 465     MSE A    11                                                      
REMARK 465     ALA A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     PRO A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     GLY A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     ARG A    23                                                      
REMARK 465     ASP A    24                                                      
REMARK 465     ASP A   203                                                      
REMARK 465     TYR A   204                                                      
REMARK 465     SER A   205                                                      
REMARK 465     TRP A   206                                                      
REMARK 465     SER A   207                                                      
REMARK 465     ALA A   208                                                      
REMARK 465     GLN A   209                                                      
REMARK 465     ARG A   210                                                      
REMARK 465     ARG A   211                                                      
REMARK 465     ALA A   212                                                      
REMARK 465     LEU A   213                                                      
REMARK 465     VAL A   214                                                      
REMARK 465     GLU A   215                                                      
REMARK 465     GLU A   216                                                      
REMARK 465     GLU A   217                                                      
REMARK 465     ILE A   218                                                      
REMARK 465     THR A   219                                                      
REMARK 465     ARG A   220                                                      
REMARK 465     ASN A   221                                                      
REMARK 465     THR A   222                                                      
REMARK 465     THR A   223                                                      
REMARK 465     PRO A   224                                                      
REMARK 465     MSE A   225                                                      
REMARK 465     TYR A   226                                                      
REMARK 465     ARG A   227                                                      
REMARK 465     THR A   228                                                      
REMARK 465     PRO A   229                                                      
REMARK 465     GLU A   230                                                      
REMARK 465     ILE A   231                                                      
REMARK 465     ILE A   232                                                      
REMARK 465     ASP A   233                                                      
REMARK 465     GLU A   264                                                      
REMARK 465     ASP A   265                                                      
REMARK 465     GLY A   266                                                      
REMARK 465     ALA A   267                                                      
REMARK 465     LYS A   268                                                      
REMARK 465     LEU A   269                                                      
REMARK 465     ARG A   270                                                      
REMARK 465     ILE A   271                                                      
REMARK 465     VAL A   272                                                      
REMARK 465     ASN A   273                                                      
REMARK 465     GLY A   274                                                      
REMARK 465     LYS A   275                                                      
REMARK 465     ASN A   335                                                      
REMARK 465     GLY A   336                                                      
REMARK 465     GLY A   337                                                      
REMARK 465     TYR A   338                                                      
REMARK 465     GLY A   339                                                      
REMARK 465     SER A   340                                                      
REMARK 465     ALA A   341                                                      
REMARK 465     THR A   342                                                      
REMARK 465     LEU A   343                                                      
REMARK 465     SER A   344                                                      
REMARK 465     ARG A   345                                                      
REMARK 465     GLY A   346                                                      
REMARK 465     PRO A   347                                                      
REMARK 465     SER B    10                                                      
REMARK 465     MSE B    11                                                      
REMARK 465     ALA B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     PRO B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     LEU B    17                                                      
REMARK 465     GLY B    18                                                      
REMARK 465     GLY B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     SER B    21                                                      
REMARK 465     GLY B    22                                                      
REMARK 465     ARG B    23                                                      
REMARK 465     ASP B    24                                                      
REMARK 465     GLN B    25                                                      
REMARK 465     TYR B   204                                                      
REMARK 465     SER B   205                                                      
REMARK 465     TRP B   206                                                      
REMARK 465     SER B   207                                                      
REMARK 465     ALA B   208                                                      
REMARK 465     GLN B   209                                                      
REMARK 465     ARG B   210                                                      
REMARK 465     ARG B   211                                                      
REMARK 465     ALA B   212                                                      
REMARK 465     LEU B   213                                                      
REMARK 465     VAL B   214                                                      
REMARK 465     GLU B   215                                                      
REMARK 465     GLU B   216                                                      
REMARK 465     GLU B   217                                                      
REMARK 465     ILE B   218                                                      
REMARK 465     THR B   219                                                      
REMARK 465     ARG B   220                                                      
REMARK 465     ASN B   221                                                      
REMARK 465     THR B   222                                                      
REMARK 465     THR B   223                                                      
REMARK 465     PRO B   224                                                      
REMARK 465     MSE B   225                                                      
REMARK 465     TYR B   226                                                      
REMARK 465     ARG B   227                                                      
REMARK 465     ASP B   265                                                      
REMARK 465     GLY B   266                                                      
REMARK 465     ALA B   267                                                      
REMARK 465     LYS B   268                                                      
REMARK 465     LEU B   269                                                      
REMARK 465     ARG B   270                                                      
REMARK 465     ILE B   271                                                      
REMARK 465     VAL B   272                                                      
REMARK 465     ASN B   273                                                      
REMARK 465     GLY B   274                                                      
REMARK 465     LYS B   275                                                      
REMARK 465     TYR B   276                                                      
REMARK 465     TYR B   338                                                      
REMARK 465     GLY B   339                                                      
REMARK 465     SER B   340                                                      
REMARK 465     ALA B   341                                                      
REMARK 465     THR B   342                                                      
REMARK 465     LEU B   343                                                      
REMARK 465     SER B   344                                                      
REMARK 465     ARG B   345                                                      
REMARK 465     GLY B   346                                                      
REMARK 465     PRO B   347                                                      
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     GLN A  25    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  34    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  37    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  39    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  41    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  48    CG   CD   OE1  OE2                                  
REMARK 470     PHE B  51    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE B  53    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 111    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 233    CG   OD1  OD2                                       
REMARK 470     LEU B 234    CG   CD1  CD2                                       
REMARK 470     TYR B 235    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER B 290   CB    SER B 290   OG     -0.079                       
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    ARG A  80   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ASP A 191   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 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    ARG A 172       -0.63     74.73                                   
REMARK 500    ASP A 173       40.73   -142.25                                   
REMARK 500    SER A 277      129.11   -172.94                                   
REMARK 500    ARG B 172       -3.06     73.13                                   
REMARK 500    ASP B 173       38.80   -141.13                                   
REMARK 500    CYS B 190       -2.71   -142.92                                   
REMARK 500    LEU B 234       -4.78    -54.42                                   
REMARK 500    TYR B 235       44.03    -95.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PHE A   51     ALA A   52                 -149.99                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN B 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4C57   RELATED DB: PDB                                   
REMARK 900 GAK-NANOBODY1                                                        
REMARK 900 RELATED ID: 4C58   RELATED DB: PDB                                   
REMARK 900 GAK-NANOBODY4                                                        
REMARK 900 RELATED ID: 4C59   RELATED DB: PDB                                   
REMARK 900 GAK-NANOBODY4                                                        
DBREF  4O38 A   12   347  UNP    O14976   GAK_HUMAN       12    347             
DBREF  4O38 B   12   347  UNP    O14976   GAK_HUMAN       12    347             
SEQADV 4O38 SER A   10  UNP  O14976              EXPRESSION TAG                 
SEQADV 4O38 MSE A   11  UNP  O14976              EXPRESSION TAG                 
SEQADV 4O38 SER B   10  UNP  O14976              EXPRESSION TAG                 
SEQADV 4O38 MSE B   11  UNP  O14976              EXPRESSION TAG                 
SEQRES   1 A  338  SER MSE ALA GLY PRO GLY SER LEU GLY GLY ALA SER GLY          
SEQRES   2 A  338  ARG ASP GLN SER ASP PHE VAL GLY GLN THR VAL GLU LEU          
SEQRES   3 A  338  GLY GLU LEU ARG LEU ARG VAL ARG ARG VAL LEU ALA GLU          
SEQRES   4 A  338  GLY GLY PHE ALA PHE VAL TYR GLU ALA GLN ASP VAL GLY          
SEQRES   5 A  338  SER GLY ARG GLU TYR ALA LEU LYS ARG LEU LEU SER ASN          
SEQRES   6 A  338  GLU GLU GLU LYS ASN ARG ALA ILE ILE GLN GLU VAL CYS          
SEQRES   7 A  338  PHE MSE LYS LYS LEU SER GLY HIS PRO ASN ILE VAL GLN          
SEQRES   8 A  338  PHE CYS SER ALA ALA SER ILE GLY LYS GLU GLU SER ASP          
SEQRES   9 A  338  THR GLY GLN ALA GLU PHE LEU LEU LEU THR GLU LEU CYS          
SEQRES  10 A  338  LYS GLY GLN LEU VAL GLU PHE LEU LYS LYS MSE GLU SER          
SEQRES  11 A  338  ARG GLY PRO LEU SER CYS ASP THR VAL LEU LYS ILE PHE          
SEQRES  12 A  338  TYR GLN THR CYS ARG ALA VAL GLN HIS MSE HIS ARG GLN          
SEQRES  13 A  338  LYS PRO PRO ILE ILE HIS ARG ASP LEU LYS VAL GLU ASN          
SEQRES  14 A  338  LEU LEU LEU SER ASN GLN GLY THR ILE LYS LEU CYS ASP          
SEQRES  15 A  338  PHE GLY SER ALA THR THR ILE SER HIS TYR PRO ASP TYR          
SEQRES  16 A  338  SER TRP SER ALA GLN ARG ARG ALA LEU VAL GLU GLU GLU          
SEQRES  17 A  338  ILE THR ARG ASN THR THR PRO MSE TYR ARG THR PRO GLU          
SEQRES  18 A  338  ILE ILE ASP LEU TYR SER ASN PHE PRO ILE GLY GLU LYS          
SEQRES  19 A  338  GLN ASP ILE TRP ALA LEU GLY CYS ILE LEU TYR LEU LEU          
SEQRES  20 A  338  CYS PHE ARG GLN HIS PRO PHE GLU ASP GLY ALA LYS LEU          
SEQRES  21 A  338  ARG ILE VAL ASN GLY LYS TYR SER ILE PRO PRO HIS ASP          
SEQRES  22 A  338  THR GLN TYR THR VAL PHE HIS SER LEU ILE ARG ALA MSE          
SEQRES  23 A  338  LEU GLN VAL ASN PRO GLU GLU ARG LEU SER ILE ALA GLU          
SEQRES  24 A  338  VAL VAL HIS GLN LEU GLN GLU ILE ALA ALA ALA ARG ASN          
SEQRES  25 A  338  VAL ASN PRO LYS SER PRO ILE THR GLU LEU LEU GLU GLN          
SEQRES  26 A  338  ASN GLY GLY TYR GLY SER ALA THR LEU SER ARG GLY PRO          
SEQRES   1 B  338  SER MSE ALA GLY PRO GLY SER LEU GLY GLY ALA SER GLY          
SEQRES   2 B  338  ARG ASP GLN SER ASP PHE VAL GLY GLN THR VAL GLU LEU          
SEQRES   3 B  338  GLY GLU LEU ARG LEU ARG VAL ARG ARG VAL LEU ALA GLU          
SEQRES   4 B  338  GLY GLY PHE ALA PHE VAL TYR GLU ALA GLN ASP VAL GLY          
SEQRES   5 B  338  SER GLY ARG GLU TYR ALA LEU LYS ARG LEU LEU SER ASN          
SEQRES   6 B  338  GLU GLU GLU LYS ASN ARG ALA ILE ILE GLN GLU VAL CYS          
SEQRES   7 B  338  PHE MSE LYS LYS LEU SER GLY HIS PRO ASN ILE VAL GLN          
SEQRES   8 B  338  PHE CYS SER ALA ALA SER ILE GLY LYS GLU GLU SER ASP          
SEQRES   9 B  338  THR GLY GLN ALA GLU PHE LEU LEU LEU THR GLU LEU CYS          
SEQRES  10 B  338  LYS GLY GLN LEU VAL GLU PHE LEU LYS LYS MSE GLU SER          
SEQRES  11 B  338  ARG GLY PRO LEU SER CYS ASP THR VAL LEU LYS ILE PHE          
SEQRES  12 B  338  TYR GLN THR CYS ARG ALA VAL GLN HIS MSE HIS ARG GLN          
SEQRES  13 B  338  LYS PRO PRO ILE ILE HIS ARG ASP LEU LYS VAL GLU ASN          
SEQRES  14 B  338  LEU LEU LEU SER ASN GLN GLY THR ILE LYS LEU CYS ASP          
SEQRES  15 B  338  PHE GLY SER ALA THR THR ILE SER HIS TYR PRO ASP TYR          
SEQRES  16 B  338  SER TRP SER ALA GLN ARG ARG ALA LEU VAL GLU GLU GLU          
SEQRES  17 B  338  ILE THR ARG ASN THR THR PRO MSE TYR ARG THR PRO GLU          
SEQRES  18 B  338  ILE ILE ASP LEU TYR SER ASN PHE PRO ILE GLY GLU LYS          
SEQRES  19 B  338  GLN ASP ILE TRP ALA LEU GLY CYS ILE LEU TYR LEU LEU          
SEQRES  20 B  338  CYS PHE ARG GLN HIS PRO PHE GLU ASP GLY ALA LYS LEU          
SEQRES  21 B  338  ARG ILE VAL ASN GLY LYS TYR SER ILE PRO PRO HIS ASP          
SEQRES  22 B  338  THR GLN TYR THR VAL PHE HIS SER LEU ILE ARG ALA MSE          
SEQRES  23 B  338  LEU GLN VAL ASN PRO GLU GLU ARG LEU SER ILE ALA GLU          
SEQRES  24 B  338  VAL VAL HIS GLN LEU GLN GLU ILE ALA ALA ALA ARG ASN          
SEQRES  25 B  338  VAL ASN PRO LYS SER PRO ILE THR GLU LEU LEU GLU GLN          
SEQRES  26 B  338  ASN GLY GLY TYR GLY SER ALA THR LEU SER ARG GLY PRO          
MODRES 4O38 MSE A   89  MET  SELENOMETHIONINE                                   
MODRES 4O38 MSE A  137  MET  SELENOMETHIONINE                                   
MODRES 4O38 MSE A  162  MET  SELENOMETHIONINE                                   
MODRES 4O38 MSE A  295  MET  SELENOMETHIONINE                                   
MODRES 4O38 MSE B   89  MET  SELENOMETHIONINE                                   
MODRES 4O38 MSE B  137  MET  SELENOMETHIONINE                                   
MODRES 4O38 MSE B  162  MET  SELENOMETHIONINE                                   
MODRES 4O38 MSE B  295  MET  SELENOMETHIONINE                                   
HET    MSE  A  89      13                                                       
HET    MSE  A 137       8                                                       
HET    MSE  A 162       8                                                       
HET    MSE  A 295       8                                                       
HET    MSE  B  89      13                                                       
HET    MSE  B 137       8                                                       
HET    MSE  B 162       8                                                       
HET    MSE  B 295       8                                                       
HET    SIN  A 401       8                                                       
HET    GOL  B 401       6                                                       
HET    GOL  B 402       6                                                       
HET    SIN  B 403       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SIN SUCCINIC ACID                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    8(C5 H11 N O2 SE)                                            
FORMUL   3  SIN    2(C4 H6 O4)                                                  
FORMUL   4  GOL    2(C3 H8 O3)                                                  
FORMUL   7  HOH   *254(H2 O)                                                    
HELIX    1   1 GLU A   75  SER A   93  1                                  19    
HELIX    2   2 LEU A  130  SER A  139  1                                  10    
HELIX    3   3 SER A  144  ARG A  164  1                                  21    
HELIX    4   4 LYS A  175  ASN A  178  5                                   4    
HELIX    5   5 GLY A  241  ARG A  259  1                                  19    
HELIX    6   6 TYR A  285  VAL A  287  5                                   3    
HELIX    7   7 PHE A  288  LEU A  296  1                                   9    
HELIX    8   8 ASN A  299  ARG A  303  5                                   5    
HELIX    9   9 SER A  305  ARG A  320  1                                  16    
HELIX   10  10 ILE A  328  GLU A  333  1                                   6    
HELIX   11  11 GLU B   75  SER B   93  1                                  19    
HELIX   12  12 LEU B  130  GLU B  138  1                                   9    
HELIX   13  13 SER B  144  ARG B  164  1                                  21    
HELIX   14  14 LYS B  175  ASN B  178  5                                   4    
HELIX   15  15 GLY B  241  ARG B  259  1                                  19    
HELIX   16  16 TYR B  285  VAL B  287  5                                   3    
HELIX   17  17 PHE B  288  LEU B  296  1                                   9    
HELIX   18  18 ASN B  299  ARG B  303  5                                   5    
HELIX   19  19 SER B  305  ARG B  320  1                                  16    
HELIX   20  20 ILE B  328  GLU B  333  1                                   6    
SHEET    1   A 7 THR A  32  LEU A  35  0                                        
SHEET    2   A 7 LEU A  38  ALA A  47 -1  O  LEU A  40   N  VAL A  33           
SHEET    3   A 7 ALA A  52  ASP A  59 -1  O  VAL A  54   N  LEU A  46           
SHEET    4   A 7 GLU A  65  SER A  73 -1  O  LEU A  68   N  TYR A  55           
SHEET    5   A 7 ALA A 117  GLU A 124 -1  O  THR A 123   N  ALA A  67           
SHEET    6   A 7 PHE A 101  ILE A 107 -1  N  SER A 103   O  LEU A 122           
SHEET    7   A 7 GLU B 230  ILE B 231 -1  O  GLU B 230   N  SER A 106           
SHEET    1   B 3 GLY A 128  GLN A 129  0                                        
SHEET    2   B 3 LEU A 180  LEU A 181 -1  O  LEU A 181   N  GLY A 128           
SHEET    3   B 3 ILE A 187  LYS A 188 -1  O  LYS A 188   N  LEU A 180           
SHEET    1   C 6 THR B  32  LEU B  35  0                                        
SHEET    2   C 6 LEU B  38  ALA B  47 -1  O  LEU B  40   N  VAL B  33           
SHEET    3   C 6 ALA B  52  ASP B  59 -1  O  VAL B  54   N  LEU B  46           
SHEET    4   C 6 GLU B  65  SER B  73 -1  O  LEU B  68   N  TYR B  55           
SHEET    5   C 6 ALA B 117  GLU B 124 -1  O  LEU B 121   N  LYS B  69           
SHEET    6   C 6 PHE B 101  ILE B 107 -1  N  SER B 103   O  LEU B 122           
SHEET    1   D 3 GLY B 128  GLN B 129  0                                        
SHEET    2   D 3 LEU B 180  LEU B 181 -1  O  LEU B 181   N  GLY B 128           
SHEET    3   D 3 ILE B 187  LYS B 188 -1  O  LYS B 188   N  LEU B 180           
LINK         C   PHE A  88                 N   MSE A  89     1555   1555  1.33  
LINK         C   MSE A  89                 N   LYS A  90     1555   1555  1.32  
LINK         C   LYS A 136                 N   MSE A 137     1555   1555  1.33  
LINK         C   MSE A 137                 N   GLU A 138     1555   1555  1.33  
LINK         C   HIS A 161                 N   MSE A 162     1555   1555  1.34  
LINK         C   MSE A 162                 N   HIS A 163     1555   1555  1.32  
LINK         C   ALA A 294                 N   MSE A 295     1555   1555  1.33  
LINK         C   MSE A 295                 N   LEU A 296     1555   1555  1.34  
LINK         C   PHE B  88                 N   MSE B  89     1555   1555  1.33  
LINK         C   MSE B  89                 N   LYS B  90     1555   1555  1.32  
LINK         C   LYS B 136                 N   MSE B 137     1555   1555  1.34  
LINK         C   MSE B 137                 N   GLU B 138     1555   1555  1.34  
LINK         C   HIS B 161                 N   MSE B 162     1555   1555  1.33  
LINK         C   MSE B 162                 N   HIS B 163     1555   1555  1.33  
LINK         C   ALA B 294                 N   MSE B 295     1555   1555  1.33  
LINK         C   MSE B 295                 N   LEU B 296     1555   1555  1.33  
CISPEP   1 LYS A  166    PRO A  167          0         2.80                     
CISPEP   2 LYS B  166    PRO B  167          0         0.66                     
SITE     1 AC1  3 CYS A 126  LYS A 127  GLY A 128                               
SITE     1 AC2  3 GLY B  94  PRO B  96  ASP B 203                               
SITE     1 AC3  3 PRO B  96  ARG B 157  HOH B 535                               
SITE     1 AC4  4 CYS B 126  LYS B 127  GLY B 128  GLY B 337                    
CRYST1  103.425  103.425  131.951  90.00  90.00 120.00 P 32 2 1     12          
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      0.009669  0.005582  0.000000        0.00000                         
SCALE2      0.000000  0.011165  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007579        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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