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Database: PDB
Entry: 4NTS
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HEADER    TRANSFERASE                             02-DEC-13   4NTS              
TITLE     APO STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN      
TITLE    2 KINASE                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PKA C-ALPHA;                                                
COMPND   5 EC: 2.7.11.11;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PRKACA, PKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN KINASE FOLD, PHOSPHORYL TRANSFERASE, KINASE, REGULATORY       
KEYWDS   2 SUBUNIT OF PKA, PKI, PHOSPHORYLATION, TRANSFERASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.BASTIDAS,J.WU,S.S.TAYLOR                                          
REVDAT   2   28-JAN-15 4NTS    1       JRNL                                     
REVDAT   1   15-OCT-14 4NTS    0                                                
JRNL        AUTH   A.C.BASTIDAS,J.WU,S.S.TAYLOR                                 
JRNL        TITL   MOLECULAR FEATURES OF PRODUCT RELEASE FOR THE PKA CATALYTIC  
JRNL        TITL 2 CYCLE.                                                       
JRNL        REF    BIOCHEMISTRY                  V.  54     2 2015              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   25077557                                                     
JRNL        DOI    10.1021/BI500684C                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.38                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 18013                          
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) : 0.247                           
REMARK   3   R VALUE            (WORKING SET) : 0.244                           
REMARK   3   FREE R VALUE                     : 0.292                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 967                             
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1354                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.28                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3650                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 75                           
REMARK   3   BIN FREE R VALUE                    : 0.3800                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5223                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 10.43000                                             
REMARK   3    B22 (A**2) : -5.38000                                             
REMARK   3    B33 (A**2) : -3.80000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.64000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.088         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.468         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.454         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 54.421        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.924                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.890                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5361 ; 0.006 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7300 ; 1.013 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   684 ; 4.972 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   238 ;39.089 ;23.739       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   771 ;17.373 ;15.039       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;21.362 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   797 ; 0.067 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4157 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     10       A     126      6                      
REMARK   3           1     B     10       B     126      6                      
REMARK   3           2     A    327       A     350      6                      
REMARK   3           2     B    327       B     350      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   1    A    (A):    989 ; 0.560 ; 5.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    127       A     326      4                      
REMARK   3           1     B    127       B     326      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):   1540 ; 0.450 ; 0.500           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     8        A   126                          
REMARK   3    RESIDUE RANGE :   A   327        A   350                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.7985  56.5646  62.7462              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4658 T22:   0.3499                                     
REMARK   3      T33:   0.4422 T12:   0.0533                                     
REMARK   3      T13:   0.1346 T23:  -0.0027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3390 L22:   3.6724                                     
REMARK   3      L33:   5.9288 L12:   0.1922                                     
REMARK   3      L13:   1.0381 L23:   0.3431                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1503 S12:  -0.1029 S13:   0.0819                       
REMARK   3      S21:   0.6323 S22:   0.1873 S23:   0.3200                       
REMARK   3      S31:   0.2651 S32:  -0.3445 S33:  -0.0371                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     8        B   126                          
REMARK   3    RESIDUE RANGE :   B   327        B   350                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0126  11.6738  23.5274              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6974 T22:   0.3572                                     
REMARK   3      T33:   0.3630 T12:   0.0660                                     
REMARK   3      T13:   0.0904 T23:   0.0085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0498 L22:   6.4690                                     
REMARK   3      L33:   5.0177 L12:   0.3812                                     
REMARK   3      L13:  -0.6180 L23:  -1.8665                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0425 S12:  -0.0135 S13:   0.0871                       
REMARK   3      S21:   1.1849 S22:   0.1880 S23:   0.5525                       
REMARK   3      S31:  -0.7621 S32:  -0.3625 S33:  -0.2305                       
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   127        A   300                          
REMARK   3    RESIDUE RANGE :   A   301        A   326                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6262  44.1736  40.9759              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2030 T22:   0.4706                                     
REMARK   3      T33:   0.3153 T12:  -0.1154                                     
REMARK   3      T13:  -0.0826 T23:  -0.0052                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0185 L22:   6.6809                                     
REMARK   3      L33:   5.2057 L12:  -1.1002                                     
REMARK   3      L13:  -0.5023 L23:   1.4189                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0477 S12:   0.3395 S13:  -0.2595                       
REMARK   3      S21:  -0.1330 S22:  -0.1183 S23:   0.4855                       
REMARK   3      S31:   0.8882 S32:  -0.4588 S33:   0.1661                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   127        B   300                          
REMARK   3    RESIDUE RANGE :   B   301        B   326                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.3916  23.9983   1.8924              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0600 T22:   0.3045                                     
REMARK   3      T33:   0.2854 T12:  -0.0759                                     
REMARK   3      T13:  -0.0433 T23:  -0.0493                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3451 L22:   8.8958                                     
REMARK   3      L33:   3.4095 L12:  -1.1263                                     
REMARK   3      L13:   1.1241 L23:  -2.8589                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1519 S12:  -0.0143 S13:   0.0306                       
REMARK   3      S21:   0.1019 S22:  -0.0863 S23:   0.1224                       
REMARK   3      S31:  -0.1332 S32:  -0.0598 S33:  -0.0656                       
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 4NTS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB083646.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19014                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 61.380                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1J3H                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% MPD, 0.1 M BICINE, 150 MM AMMONIUM    
REMARK 280  ACETATE, 10 MM DTT, 9% METHANOL ADDED TO THE WELL SOLUTION, PH      
REMARK 280  8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.15K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       71.30500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     GLY A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     CYS A     7                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     CYS B     7                                                      
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     LYS A   8    CG   CD   CE   NZ                                   
REMARK 470     GLU A  11    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  12    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  13    CG   CD   OE1  OE2                                  
REMARK 470     SER A  14    OG                                                  
REMARK 470     LYS A  16    CG   CD   CE   NZ                                   
REMARK 470     GLU A  17    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  21    CG   CD   CE   NZ                                   
REMARK 470     GLU A  24    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  29    CG   CD   CE   NZ                                   
REMARK 470     ASP A  44    CG   OD1  OD2                                       
REMARK 470     ARG A  45    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A  46    CD1                                                 
REMARK 470     LYS A  47    CG   CD   CE   NZ                                   
REMARK 470     THR A  51    OG1  CG2                                            
REMARK 470     VAL A  60    CG1  CG2                                            
REMARK 470     LYS A  61    CG   CD   CE   NZ                                   
REMARK 470     LYS A  63    CG   CD   CE   NZ                                   
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  73    CD1                                                 
REMARK 470     LYS A  78    CG   CD   CE   NZ                                   
REMARK 470     LYS A  81    CE   NZ                                             
REMARK 470     LEU A  82    CG   CD1  CD2                                       
REMARK 470     LYS A  83    CG   CD   CE   NZ                                   
REMARK 470     GLU A  86    CG   CD   OE1  OE2                                  
REMARK 470     SER A 114    OG                                                  
REMARK 470     GLU A 127    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 135    CD1                                                 
REMARK 470     VAL A 191    CG1  CG2                                            
REMARK 470     ILE A 210    CD1                                                 
REMARK 470     LYS A 213    CG   CD   CE   NZ                                   
REMARK 470     ILE A 228    CD1                                                 
REMARK 470     GLN A 242    CD   OE1  NE2                                       
REMARK 470     ILE A 246    CD1                                                 
REMARK 470     LYS A 249    CG   CD   CE   NZ                                   
REMARK 470     SER A 252    OG                                                  
REMARK 470     VAL A 255    CG1  CG2                                            
REMARK 470     ARG A 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 263    OG                                                  
REMARK 470     ARG A 270    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 275    CG1  CG2                                            
REMARK 470     LYS A 285    CG   CD   CE   NZ                                   
REMARK 470     ILE A 291    CD1                                                 
REMARK 470     LYS A 295    CG   CD   CE   NZ                                   
REMARK 470     ILE A 303    CD1                                                 
REMARK 470     GLU A 311    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 315    CD1                                                 
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     PHE A 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 319    CG   CD   CE   NZ                                   
REMARK 470     PRO A 321    CG   CD                                             
REMARK 470     ASP A 323    CG   OD1  OD2                                       
REMARK 470     THR A 324    OG1  CG2                                            
REMARK 470     SER A 325    OG                                                  
REMARK 470     ASN A 326    CG   OD1  ND2                                       
REMARK 470     PHE A 327    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP A 328    CG   OD1  OD2                                       
REMARK 470     ASP A 329    CG   OD1  OD2                                       
REMARK 470     TYR A 330    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 331    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 332    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 334    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 335    CD1                                                 
REMARK 470     VAL A 337    CG1  CG2                                            
REMARK 470     LYS B   8    CG   CD   CE   NZ                                   
REMARK 470     SER B  10    OG                                                  
REMARK 470     GLU B  11    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  12    CG   CD   OE1  NE2                                  
REMARK 470     SER B  14    OG                                                  
REMARK 470     VAL B  15    CG1  CG2                                            
REMARK 470     LYS B  16    CG   CD   CE   NZ                                   
REMARK 470     GLU B  17    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  21    CG   CD   CE   NZ                                   
REMARK 470     ASP B  25    CG   OD1  OD2                                       
REMARK 470     LYS B  29    CG   CD   CE   NZ                                   
REMARK 470     ARG B  45    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B  46    CD1                                                 
REMARK 470     LYS B  47    CG   CD   CE   NZ                                   
REMARK 470     THR B  51    OG1  CG2                                            
REMARK 470     SER B  53    OG                                                  
REMARK 470     ARG B  56    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B  57    CG1  CG2                                            
REMARK 470     LEU B  59    CG   CD1  CD2                                       
REMARK 470     VAL B  60    CG1  CG2                                            
REMARK 470     GLU B  64    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  72    CG   CD   CE   NZ                                   
REMARK 470     GLN B  77    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  78    CG   CD   CE   NZ                                   
REMARK 470     VAL B  79    CG1  CG2                                            
REMARK 470     LYS B  81    CG   CD   CE   NZ                                   
REMARK 470     LEU B  82    CG   CD1  CD2                                       
REMARK 470     LYS B  83    CG   CD   CE   NZ                                   
REMARK 470     GLU B  86    CG   CD   OE1  OE2                                  
REMARK 470     SER B 109    OG                                                  
REMARK 470     SER B 114    OG                                                  
REMARK 470     ARG B 133    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 135    CD1                                                 
REMARK 470     ILE B 150    CD1                                                 
REMARK 470     GLN B 176    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 198    CG   CD1  CD2                                       
REMARK 470     ILE B 210    CD1                                                 
REMARK 470     SER B 212    OG                                                  
REMARK 470     LYS B 213    CG   CD   CE   NZ                                   
REMARK 470     ILE B 244    CG1  CG2  CD1                                       
REMARK 470     GLN B 245    CG   CD   OE1  NE2                                  
REMARK 470     ILE B 246    CD1                                                 
REMARK 470     LYS B 249    CG   CD   CE   NZ                                   
REMARK 470     ILE B 250    CD1                                                 
REMARK 470     SER B 252    OG                                                  
REMARK 470     VAL B 255    CG1  CG2                                            
REMARK 470     SER B 263    OG                                                  
REMARK 470     LEU B 268    CD1  CD2                                            
REMARK 470     THR B 278    OG1  CG2                                            
REMARK 470     LYS B 285    CG   CD   CE   NZ                                   
REMARK 470     LYS B 295    CD   CE   NZ                                        
REMARK 470     ILE B 303    CD1                                                 
REMARK 470     LYS B 309    CG   CD   CE   NZ                                   
REMARK 470     GLU B 311    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 315    CD1                                                 
REMARK 470     LYS B 317    CG   CD   CE   NZ                                   
REMARK 470     LYS B 319    CG   CD   CE   NZ                                   
REMARK 470     PRO B 321    CG   CD                                             
REMARK 470     ASP B 323    CG   OD1  OD2                                       
REMARK 470     THR B 324    OG1  CG2                                            
REMARK 470     SER B 325    OG                                                  
REMARK 470     ASN B 326    CG   OD1  ND2                                       
REMARK 470     PHE B 327    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP B 328    CG   OD1  OD2                                       
REMARK 470     ASP B 329    CG   OD1  OD2                                       
REMARK 470     TYR B 330    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B 331    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 332    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 334    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 335    CG1  CG2  CD1                                       
REMARK 470     ILE B 339    CG1  CG2  CD1                                       
REMARK 470     GLU B 341    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 342    CG   CD   CE   NZ                                   
REMARK 470     LYS B 345    CG   CD   CE   NZ                                   
REMARK 470     GLU B 349    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   O    LEU B   132     O    ILE B   135              2.05            
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    SER A  10      -30.18     84.32                                   
REMARK 500    ASP A 166       38.99   -151.53                                   
REMARK 500    ASN A 216     -157.37   -153.59                                   
REMARK 500    ASN A 283       52.03   -114.28                                   
REMARK 500    LEU A 284     -160.72   -125.51                                   
REMARK 500    LYS A 317       52.24    -98.87                                   
REMARK 500    THR A 324     -132.79     45.45                                   
REMARK 500    ASP A 328     -112.44     44.50                                   
REMARK 500    ASP A 329      -93.46   -126.99                                   
REMARK 500    GLU A 331     -160.85   -125.41                                   
REMARK 500    GLU A 333      125.58   -174.87                                   
REMARK 500    ILE B  46       75.01   -116.50                                   
REMARK 500    LYS B  47      157.30     80.74                                   
REMARK 500    ASP B 112     -164.97   -123.31                                   
REMARK 500    ARG B 165        4.32     58.73                                   
REMARK 500    ASP B 166       54.85   -149.40                                   
REMARK 500    ASN B 216     -159.04   -145.91                                   
REMARK 500    LEU B 273       35.06    -76.93                                   
REMARK 500    PHE B 318     -171.88     73.44                                   
REMARK 500    LYS B 319       -6.54     91.65                                   
REMARK 500    ASP B 328     -169.56    -69.38                                   
REMARK 500    GLU B 331       43.54    -69.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     MYR A  401                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR A 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1J3H   RELATED DB: PDB                                   
REMARK 900 PREVIOUS APO STRUCTURE OF THE C-SUBUNIT                              
REMARK 900 RELATED ID: 1ATP   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE C-SUBUNIT WITH ATP AND IP20                         
REMARK 900 RELATED ID: 1CMK   RELATED DB: PDB                                   
REMARK 900 OPEN STRUCTURE OF THE C-SUBUNIT BOUND TO IP20                        
REMARK 900 RELATED ID: 1SYK   RELATED DB: PDB                                   
REMARK 900 APO STRUCTURE OF THE C-SUBUNIT WITH E230Q MUTATION                   
REMARK 900 RELATED ID: 4DFY   RELATED DB: PDB                                   
REMARK 900 APO STRUCTURE OF THE C-SUBUNIT LACKING PHOSPHORYLATION ON            
REMARK 900 THE ACTIVATION LOOP                                                  
DBREF  4NTS A    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  4NTS B    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
SEQADV 4NTS CYS A    7  UNP  P05132    LYS     8 ENGINEERED MUTATION            
SEQADV 4NTS CYS B    7  UNP  P05132    LYS     8 ENGINEERED MUTATION            
SEQRES   1 A  350  GLY ASN ALA ALA ALA ALA CYS LYS GLY SER GLU GLN GLU          
SEQRES   2 A  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 A  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 A  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 A  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 A  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 A  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 A  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 A  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 A  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 A  350  HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS ALA          
SEQRES  12 A  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 A  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 A  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 A  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 A  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 A  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 A  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 A  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 A  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 A  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 A  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN          
SEQRES  23 A  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 A  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 A  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 A  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 A  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE              
SEQRES   1 B  350  GLY ASN ALA ALA ALA ALA CYS LYS GLY SER GLU GLN GLU          
SEQRES   2 B  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 B  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 B  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 B  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 B  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 B  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 B  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 B  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 B  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 B  350  HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS ALA          
SEQRES  12 B  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 B  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 B  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 B  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 B  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 B  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 B  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 B  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 B  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 B  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 B  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN          
SEQRES  23 B  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 B  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 B  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 B  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 B  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE              
MODRES 4NTS TPO A  197  THR  PHOSPHOTHREONINE                                   
MODRES 4NTS SEP A  338  SER  PHOSPHOSERINE                                      
MODRES 4NTS TPO B  197  THR  PHOSPHOTHREONINE                                   
MODRES 4NTS SEP B  338  SER  PHOSPHOSERINE                                      
HET    TPO  A 197      11                                                       
HET    SEP  A 338      10                                                       
HET    TPO  B 197      11                                                       
HET    SEP  B 338      10                                                       
HET    MYR  A 401       4                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     MYR MYRISTIC ACID                                                    
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   3  MYR    C14 H28 O2                                                   
HELIX    1   1 GLU A   13  THR A   32  1                                  20    
HELIX    2   2 GLN A   39  ASP A   41  5                                   3    
HELIX    3   3 LYS A   76  LYS A   83  1                                   8    
HELIX    4   4 GLN A   84  VAL A   98  1                                  15    
HELIX    5   5 GLU A  127  GLY A  136  1                                  10    
HELIX    6   6 SER A  139  LEU A  160  1                                  22    
HELIX    7   7 LYS A  168  GLU A  170  5                                   3    
HELIX    8   8 THR A  201  LEU A  205  5                                   5    
HELIX    9   9 ALA A  206  SER A  212  1                                   7    
HELIX   10  10 LYS A  217  GLY A  234  1                                  18    
HELIX   11  11 GLN A  242  SER A  252  1                                  11    
HELIX   12  12 SER A  262  LEU A  273  1                                  12    
HELIX   13  13 VAL A  288  ASN A  293  1                                   6    
HELIX   14  14 HIS A  294  ALA A  298  5                                   5    
HELIX   15  15 ASP A  301  ARG A  308  1                                   8    
HELIX   16  16 GLU B   13  THR B   32  1                                  20    
HELIX   17  17 GLN B   39  ASP B   41  5                                   3    
HELIX   18  18 LYS B   76  LEU B   82  1                                   7    
HELIX   19  19 GLN B   84  VAL B   98  1                                  15    
HELIX   20  20 GLU B  127  ILE B  135  1                                   9    
HELIX   21  21 SER B  139  LEU B  160  1                                  22    
HELIX   22  22 LYS B  168  GLU B  170  5                                   3    
HELIX   23  23 THR B  201  LEU B  205  5                                   5    
HELIX   24  24 ALA B  206  LEU B  211  1                                   6    
HELIX   25  25 ALA B  218  GLY B  234  1                                  17    
HELIX   26  26 GLN B  242  GLY B  253  1                                  12    
HELIX   27  27 SER B  262  LEU B  273  1                                  12    
HELIX   28  28 VAL B  288  ASN B  293  1                                   6    
HELIX   29  29 HIS B  294  ALA B  298  5                                   5    
HELIX   30  30 ASP B  301  GLN B  307  1                                   7    
SHEET    1   A 5 PHE A  43  THR A  51  0                                        
SHEET    2   A 5 GLY A  55  HIS A  62 -1  O  VAL A  57   N  GLY A  50           
SHEET    3   A 5 HIS A  68  ASP A  75 -1  O  ILE A  73   N  ARG A  56           
SHEET    4   A 5 ASN A 115  GLU A 121 -1  O  MET A 120   N  ALA A  70           
SHEET    5   A 5 LEU A 106  LYS A 111 -1  N  PHE A 110   O  TYR A 117           
SHEET    1   B 2 LEU A 162  ILE A 163  0                                        
SHEET    2   B 2 LYS A 189  ARG A 190 -1  O  LYS A 189   N  ILE A 163           
SHEET    1   C 2 LEU A 172  ILE A 174  0                                        
SHEET    2   C 2 ILE A 180  VAL A 182 -1  O  GLN A 181   N  LEU A 173           
SHEET    1   D 5 PHE B  43  THR B  51  0                                        
SHEET    2   D 5 GLY B  55  HIS B  62 -1  O  LYS B  61   N  ASP B  44           
SHEET    3   D 5 HIS B  68  ASP B  75 -1  O  ILE B  73   N  ARG B  56           
SHEET    4   D 5 ASN B 115  GLU B 121 -1  O  LEU B 116   N  LEU B  74           
SHEET    5   D 5 LEU B 106  LYS B 111 -1  N  PHE B 110   O  TYR B 117           
SHEET    1   E 2 LEU B 162  ILE B 163  0                                        
SHEET    2   E 2 LYS B 189  ARG B 190 -1  O  LYS B 189   N  ILE B 163           
SHEET    1   F 2 LEU B 172  ILE B 174  0                                        
SHEET    2   F 2 ILE B 180  VAL B 182 -1  O  GLN B 181   N  LEU B 173           
LINK         C   TRP A 196                 N   TPO A 197     1555   1555  1.33  
LINK         C   TPO A 197                 N   LEU A 198     1555   1555  1.33  
LINK         C   VAL A 337                 N   SEP A 338     1555   1555  1.33  
LINK         C   SEP A 338                 N   ILE A 339     1555   1555  1.33  
LINK         C   TRP B 196                 N   TPO B 197     1555   1555  1.34  
LINK         C   TPO B 197                 N   LEU B 198     1555   1555  1.33  
LINK         C   VAL B 337                 N   SEP B 338     1555   1555  1.33  
LINK         C   SEP B 338                 N   ILE B 339     1555   1555  1.33  
SITE     1 AC1  2 PHE A  18  GLU A 155                                          
CRYST1   50.960  142.610   63.160  90.00 103.65  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019623  0.000000  0.004765        0.00000                         
SCALE2      0.000000  0.007012  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016293        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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