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Database: PDB
Entry: 2QCS
LinkDB: 2QCS
Original site: 2QCS 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       19-JUN-07   2QCS              
TITLE     A COMPLEX STRUCTURE BETWEEN THE CATALYTIC AND REGULATORY SUBUNIT OF   
TITLE    2 PROTEIN KINASE A THAT REPRESENTS THE INHIBITED STATE                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT;    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC SUBUNIT;                                         
COMPND   5 SYNONYM: PKA C-ALPHA;                                                
COMPND   6 EC: 2.7.11.11;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE TYPE I-ALPHA REGULATORY      
COMPND  10 SUBUNIT;                                                             
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: REGULATORY SUBUNIT;                                        
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PRKACA, PKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  12 ORGANISM_COMMON: CATTLE;                                             
SOURCE  13 ORGANISM_TAXID: 9913;                                                
SOURCE  14 GENE: PRKAR1A;                                                       
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    CYCLIC ADENOSINE MONOPHOSPHATE, CAMP-DEPENDENT PROTEIN KINASE, PKA    
KEYWDS   2 HOLOENZYME, CYCLIC NUCLEOTIDE BINDING DOMAIN, PROTEIN-PROTEIN        
KEYWDS   3 INTERACTION, CONFORMATIONAL CHANGE, PROTEIN BINDING, TRANSFERASE-    
KEYWDS   4 TRANSFERASE INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.KIM,C.Y.CHENG,A.S.SALDANHA,S.S.TAYLOR                               
REVDAT   4   18-OCT-17 2QCS    1       REMARK                                   
REVDAT   3   13-JUL-11 2QCS    1       VERSN                                    
REVDAT   2   24-FEB-09 2QCS    1       VERSN                                    
REVDAT   1   06-NOV-07 2QCS    0                                                
JRNL        AUTH   C.KIM,C.Y.CHENG,S.A.SALDANHA,S.S.TAYLOR                      
JRNL        TITL   PKA-I HOLOENZYME STRUCTURE REVEALS A MECHANISM FOR           
JRNL        TITL 2 CAMP-DEPENDENT ACTIVATION.                                   
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 130  1032 2007              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   17889648                                                     
JRNL        DOI    10.1016/J.CELL.2007.07.018                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 59282                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3160                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2864                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 62.88                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2890                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 150                          
REMARK   3   BIN FREE R VALUE                    : 0.3090                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5059                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 96                                      
REMARK   3   SOLVENT ATOMS            : 289                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.88000                                              
REMARK   3    B22 (A**2) : 0.88000                                              
REMARK   3    B33 (A**2) : -1.32000                                             
REMARK   3    B12 (A**2) : 0.44000                                              
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): 0.165         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.154         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.111         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.201         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5197 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3580 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7034 ; 1.439 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8653 ; 0.945 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   627 ; 6.515 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   244 ;36.645 ;23.934       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   878 ;16.235 ;15.034       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;15.281 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   755 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5720 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1096 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   933 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3697 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2466 ; 0.176 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2750 ; 0.088 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   293 ; 0.161 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    27 ; 0.191 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    63 ; 0.283 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.201 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3416 ; 0.708 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1275 ; 0.142 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5033 ; 1.052 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2297 ; 1.576 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2001 ; 2.259 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
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    13        A   128                          
REMARK   3    ORIGIN FOR THE GROUP (A):  82.9942 -24.4065 -24.1771              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0824 T22:   0.0047                                     
REMARK   3      T33:  -0.0941 T12:   0.1383                                     
REMARK   3      T13:   0.1168 T23:   0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0830 L22:   1.7531                                     
REMARK   3      L33:   2.8580 L12:  -0.4111                                     
REMARK   3      L13:  -0.4736 L23:   0.5941                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2136 S12:   0.2177 S13:   0.0908                       
REMARK   3      S21:  -0.3443 S22:  -0.1702 S23:  -0.3641                       
REMARK   3      S31:  -0.0308 S32:   0.3806 S33:  -0.0434                       
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   129        A   350                          
REMARK   3    ORIGIN FOR THE GROUP (A):  70.3818 -30.3568 -10.9260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0335 T22:  -0.0659                                     
REMARK   3      T33:  -0.1254 T12:   0.0780                                     
REMARK   3      T13:   0.0086 T23:  -0.0259                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2124 L22:   1.4534                                     
REMARK   3      L33:   1.4257 L12:  -0.1155                                     
REMARK   3      L13:  -0.0444 L23:   0.1015                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1156 S12:   0.0737 S13:  -0.0221                       
REMARK   3      S21:  -0.0882 S22:  -0.1550 S23:  -0.0561                       
REMARK   3      S31:   0.1634 S32:   0.0886 S33:   0.0395                       
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 :   B    90        B   255                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.6568  -4.3599  -3.8600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0017 T22:  -0.1476                                     
REMARK   3      T33:  -0.0823 T12:   0.0209                                     
REMARK   3      T13:   0.0004 T23:  -0.0337                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8289 L22:   1.3670                                     
REMARK   3      L33:   0.6609 L12:  -0.5729                                     
REMARK   3      L13:   0.1247 L23:  -0.4591                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0892 S12:   0.0644 S13:   0.0779                       
REMARK   3      S21:   0.0170 S22:  -0.0565 S23:   0.0976                       
REMARK   3      S31:  -0.2442 S32:   0.0609 S33:   0.1457                       
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   256        B   376                          
REMARK   3    ORIGIN FOR THE GROUP (A):  75.0095 -18.7050  26.1392              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0400 T22:  -0.1007                                     
REMARK   3      T33:  -0.1429 T12:   0.0116                                     
REMARK   3      T13:  -0.0489 T23:   0.0396                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5301 L22:   2.8598                                     
REMARK   3      L33:   2.5368 L12:   0.0042                                     
REMARK   3      L13:  -0.1570 L23:   0.3735                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0157 S12:  -0.0091 S13:  -0.0219                       
REMARK   3      S21:   0.0660 S22:   0.0422 S23:  -0.0207                       
REMARK   3      S31:  -0.2455 S32:   0.0338 S33:  -0.0580                       
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 :   A   400        A   402                          
REMARK   3    ORIGIN FOR THE GROUP (A):  72.7041 -26.2170 -24.0498              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0187 T22:   0.0531                                     
REMARK   3      T33:  -0.1450 T12:   0.1243                                     
REMARK   3      T13:   0.0509 T23:   0.0076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0788 L22:   7.1148                                     
REMARK   3      L33:  21.1749 L12:  -6.0224                                     
REMARK   3      L13:  -5.9565 L23:  10.0979                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2788 S12:   0.3423 S13:   0.0419                       
REMARK   3      S21:   0.2027 S22:  -0.3686 S23:   0.2835                       
REMARK   3      S31:   0.1765 S32:   0.3132 S33:   0.0898                       
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 2QCS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000043435.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-FEB-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
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) : 1.00                               
REMARK 200  MONOCHROMATOR                  : SI 111 ROSENBAUM-ROCK HIGH         
REMARK 200                                   -RESOLUTION DOUBLE-CRYSTAL         
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62263                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.4000                            
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: PHASES                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1U7E                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M(NH4)2SO4, 0.1M CITRATE, PH 5.5,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                     
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       93.96067            
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       46.98033            
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       46.98033            
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       93.96067            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7900 ANGSTROM**2                          
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 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     LYS A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     GLN A    12                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  13    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 105    CD   CE   NZ                                        
REMARK 470     LYS A 254    CD   CE   NZ                                        
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     LYS A 319    CG   CD   CE   NZ                                   
REMARK 470     GLU A 331    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 334    CG   CD   OE1                                       
REMARK 470     LYS A 345    CG   CD   CE   NZ                                   
REMARK 470     GLN B 177    CD   OE1  NE2                                       
REMARK 470     LYS B 279    CE   NZ                                             
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A   16   CD   CE   NZ                                        
REMARK 480     LYS A   21   CE   NZ                                             
REMARK 480     LYS A   28   CD   CE   NZ                                        
REMARK 480     GLU A   31   CD   OE1  OE2                                       
REMARK 480     LYS A   81   CD   CE   NZ                                        
REMARK 480     ARG A   93   CZ   NH1  NH2                                       
REMARK 480     LYS A  192   CE   NZ                                             
REMARK 480     ARG A  256   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS A  309   CE   NZ                                             
REMARK 480     PHE A  318   CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 480     GLU B  106   CD   OE1  OE2                                       
REMARK 480     LYS B  114   CD   CE   NZ                                        
REMARK 480     LYS B  121   CD   CE   NZ                                        
REMARK 480     LYS B  128   CE   NZ                                             
REMARK 480     ARG B  304   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLU B  306   CG   CD   OE1  OE2                                  
REMARK 480     ASN B  307   CB   CG   OD1  ND2                                  
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    LYS A  21   CG  -  CD  -  CE  ANGL. DEV. =  27.7 DEGREES          
REMARK 500    LYS A  21   CD  -  CE  -  NZ  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    ARG A  93   CD  -  NE  -  CZ  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    ARG A  93   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG A  93   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    LYS A 192   CD  -  CE  -  NZ  ANGL. DEV. =  19.0 DEGREES          
REMARK 500    PHE A 318   CA  -  CB  -  CG  ANGL. DEV. =  23.6 DEGREES          
REMARK 500    PHE A 318   CB  -  CG  -  CD2 ANGL. DEV. = -14.7 DEGREES          
REMARK 500    PHE A 318   CB  -  CG  -  CD1 ANGL. DEV. =  12.5 DEGREES          
REMARK 500    ARG B  93   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B  93   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    LYS B 114   CB  -  CG  -  CD  ANGL. DEV. =  18.0 DEGREES          
REMARK 500    ARG B 304   CG  -  CD  -  NE  ANGL. DEV. =  21.9 DEGREES          
REMARK 500    ARG B 304   CD  -  NE  -  CZ  ANGL. DEV. =  10.4 DEGREES          
REMARK 500    ASN B 307   CB  -  CA  -  C   ANGL. DEV. = -19.2 DEGREES          
REMARK 500    ARG B 340   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 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    THR A  32       78.84   -117.97                                   
REMARK 500    ASP A 112     -161.32   -120.24                                   
REMARK 500    SEP A 139      141.96    -38.33                                   
REMARK 500    ASP A 166       44.40   -150.15                                   
REMARK 500    ASP A 184       77.31     65.56                                   
REMARK 500    ASN B 185       43.38     38.41                                   
REMARK 500    ASN B 186       -2.25     72.82                                   
REMARK 500    ASP B 276      123.02    -38.54                                   
REMARK 500    ASN B 307       60.08   -100.91                                   
REMARK 500    SER B 319      -19.50     87.56                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  93         0.08    SIDE CHAIN                              
REMARK 500    PHE A 318         0.09    SIDE CHAIN                              
REMARK 500    ARG B 304         0.15    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 171   OD1                                                    
REMARK 620 2 ASP A 184   OD2  94.0                                              
REMARK 620 3 HOH A 555   O    92.3 173.4                                        
REMARK 620 4 ANP A 400   O2A  96.3  87.3  90.1                                  
REMARK 620 5 ANP A 400   O2G 118.2  84.8  94.0 144.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 184   OD1                                                    
REMARK 620 2 ASP A 184   OD2  55.3                                              
REMARK 620 3 ANP A 400   O1G 149.6  95.4                                        
REMARK 620 4 ANP A 400   O2B  86.0  86.1  84.0                                  
REMARK 620 5 HOH A 564   O    94.5 149.5 113.6  87.6                            
REMARK 620 6 HOH A 527   O    89.9  87.1  97.0 173.2  98.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 408                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1APM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1RGS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1NE6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1NE4   RELATED DB: PDB                                   
DBREF  2QCS A    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  2QCS B   90   379  UNP    P00514   KAP0_BOVIN      91    380             
SEQADV 2QCS SEP A  139  UNP  P05132    SER   140 MODIFIED RESIDUE               
SEQADV 2QCS TPO A  197  UNP  P05132    THR   198 MODIFIED RESIDUE               
SEQADV 2QCS SEP A  338  UNP  P05132    SER   339 MODIFIED RESIDUE               
SEQADV 2QCS LYS B  333  UNP  P00514    ARG   334 ENGINEERED                     
SEQADV 2QCS ALA B  380  UNP  P00514              EXPRESSION TAG                 
SEQRES   1 A  350  GLY ASN ALA ALA ALA ALA LYS 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 SEP 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  291  LYS GLY ARG ARG ARG ARG GLY ALA ILE SER ALA GLU VAL          
SEQRES   2 B  291  TYR THR GLU GLU ASP ALA ALA SER TYR VAL ARG LYS VAL          
SEQRES   3 B  291  ILE PRO LYS ASP TYR LYS THR MET ALA ALA LEU ALA LYS          
SEQRES   4 B  291  ALA ILE GLU LYS ASN VAL LEU PHE SER HIS LEU ASP ASP          
SEQRES   5 B  291  ASN GLU ARG SER ASP ILE PHE ASP ALA MET PHE PRO VAL          
SEQRES   6 B  291  SER PHE ILE ALA GLY GLU THR VAL ILE GLN GLN GLY ASP          
SEQRES   7 B  291  GLU GLY ASP ASN PHE TYR VAL ILE ASP GLN GLY GLU MET          
SEQRES   8 B  291  ASP VAL TYR VAL ASN ASN GLU TRP ALA THR SER VAL GLY          
SEQRES   9 B  291  GLU GLY GLY SER PHE GLY GLU LEU ALA LEU ILE TYR GLY          
SEQRES  10 B  291  THR PRO ARG ALA ALA THR VAL LYS ALA LYS THR ASN VAL          
SEQRES  11 B  291  LYS LEU TRP GLY ILE ASP ARG ASP SER TYR ARG ARG ILE          
SEQRES  12 B  291  LEU MET GLY SER THR LEU ARG LYS ARG LYS MET TYR GLU          
SEQRES  13 B  291  GLU PHE LEU SER LYS VAL SER ILE LEU GLU SER LEU ASP          
SEQRES  14 B  291  LYS TRP GLU ARG LEU THR VAL ALA ASP ALA LEU GLU PRO          
SEQRES  15 B  291  VAL GLN PHE GLU ASP GLY GLN LYS ILE VAL VAL GLN GLY          
SEQRES  16 B  291  GLU PRO GLY ASP GLU PHE PHE ILE ILE LEU GLU GLY SER          
SEQRES  17 B  291  ALA ALA VAL LEU GLN ARG ARG SER GLU ASN GLU GLU PHE          
SEQRES  18 B  291  VAL GLU VAL GLY ARG LEU GLY PRO SER ASP TYR PHE GLY          
SEQRES  19 B  291  GLU ILE ALA LEU LEU MET ASN ARG PRO LYS ALA ALA THR          
SEQRES  20 B  291  VAL VAL ALA ARG GLY PRO LEU LYS CYS VAL LYS LEU ASP          
SEQRES  21 B  291  ARG PRO ARG PHE GLU ARG VAL LEU GLY PRO CYS SER ASP          
SEQRES  22 B  291  ILE LEU LYS ARG ASN ILE GLN GLN TYR ASN SER PHE VAL          
SEQRES  23 B  291  SER LEU SER VAL ALA                                          
MODRES 2QCS SEP A  139  SER  PHOSPHOSERINE                                      
MODRES 2QCS TPO A  197  THR  PHOSPHOTHREONINE                                   
MODRES 2QCS SEP A  338  SER  PHOSPHOSERINE                                      
HET    SEP  A 139      10                                                       
HET    TPO  A 197      11                                                       
HET    SEP  A 338      10                                                       
HET     MN  A 401       1                                                       
HET     MN  A 402       1                                                       
HET    SO4  A 403       5                                                       
HET    ACT  A 412       4                                                       
HET    ANP  A 400      31                                                       
HET    TAM  A 406      11                                                       
HET    GOL  A 407       6                                                       
HET    GOL  A 410       6                                                       
HET    SO4  B 400       5                                                       
HET    SO4  B 403       5                                                       
HET    SO4  B 401       5                                                       
HET    SO4  B 404       5                                                       
HET    SO4  B 405       5                                                       
HET    GOL  B 408       6                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ACT ACETATE ION                                                      
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM     TAM TRIS(HYDROXYETHYL)AMINOMETHANE                                   
HETNAM     GOL GLYCEROL                                                         
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   5  SO4    6(O4 S 2-)                                                   
FORMUL   6  ACT    C2 H3 O2 1-                                                  
FORMUL   7  ANP    C10 H17 N6 O12 P3                                            
FORMUL   8  TAM    C7 H17 N O3                                                  
FORMUL   9  GOL    3(C3 H8 O3)                                                  
FORMUL  17  HOH   *289(H2 O)                                                    
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  LEU A   82  1                                   7    
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 SEP 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  LEU A  211  1                                   6    
HELIX   10  10 ALA A  218  GLY A  234  1                                  17    
HELIX   11  11 GLN A  242  GLY A  253  1                                  12    
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  GLN A  307  1                                   7    
HELIX   16  16 THR B  104  SER B  110  1                                   7    
HELIX   17  17 ASP B  119  ILE B  130  1                                  12    
HELIX   18  18 ASN B  133  HIS B  138  1                                   6    
HELIX   19  19 ASP B  140  MET B  151  1                                  12    
HELIX   20  20 GLY B  199  ILE B  204  5                                   6    
HELIX   21  21 ARG B  226  LYS B  250  1                                  25    
HELIX   22  22 VAL B  251  GLU B  255  5                                   5    
HELIX   23  23 ASP B  258  LEU B  269  1                                  12    
HELIX   24  24 GLU B  324  LEU B  328  5                                   5    
HELIX   25  25 ARG B  350  GLY B  358  1                                   9    
HELIX   26  26 PRO B  359  LYS B  365  1                                   7    
HELIX   27  27 ASN B  367  VAL B  375  1                                   9    
SHEET    1   A 5 PHE A  43  THR A  51  0                                        
SHEET    2   A 5 ARG A  56  HIS A  62 -1  O  VAL A  57   N  LEU A  49           
SHEET    3   A 5 HIS A  68  ASP A  75 -1  O  MET A  71   N  MET A  58           
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 108   O  VAL A 119           
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 2 CYS A 199  GLY A 200  0                                        
SHEET    2   D 2 ILE B  98  SER B  99 -1  O  ILE B  98   N  GLY A 200           
SHEET    1   E 4 PHE B 152  PHE B 156  0                                        
SHEET    2   E 4 VAL B 219  ASP B 225 -1  O  LEU B 221   N  VAL B 154           
SHEET    3   E 4 ASN B 171  GLN B 177 -1  N  PHE B 172   O  ILE B 224           
SHEET    4   E 4 SER B 197  PHE B 198 -1  O  PHE B 198   N  TYR B 173           
SHEET    1   F 4 THR B 161  ILE B 163  0                                        
SHEET    2   F 4 THR B 212  ALA B 215 -1  O  VAL B 213   N  VAL B 162           
SHEET    3   F 4 MET B 180  VAL B 184 -1  N  TYR B 183   O  THR B 212           
SHEET    4   F 4 GLU B 187  VAL B 192 -1  O  THR B 190   N  VAL B 182           
SHEET    1   G 4 GLU B 270  PHE B 274  0                                        
SHEET    2   G 4 THR B 336  ASP B 349 -1  O  LYS B 347   N  GLU B 270           
SHEET    3   G 4 GLU B 289  ARG B 303 -1  N  LEU B 294   O  LYS B 344           
SHEET    4   G 4 PHE B 310  LEU B 316 -1  O  GLY B 314   N  VAL B 300           
SHEET    1   H 4 LYS B 279  VAL B 281  0                                        
SHEET    2   H 4 THR B 336  ASP B 349 -1  O  VAL B 337   N  ILE B 280           
SHEET    3   H 4 GLU B 289  ARG B 303 -1  N  LEU B 294   O  LYS B 344           
SHEET    4   H 4 TYR B 321  PHE B 322 -1  O  PHE B 322   N  PHE B 291           
LINK         OD1 ASN A 171                MN    MN A 401     1555   1555  2.20  
LINK         OD1 ASP A 184                MN    MN A 402     1555   1555  2.40  
LINK         OD2 ASP A 184                MN    MN A 401     1555   1555  2.26  
LINK         OD2 ASP A 184                MN    MN A 402     1555   1555  2.32  
LINK        MN    MN A 401                 O   HOH A 555     1555   1555  2.15  
LINK        MN    MN A 401                 O2A ANP A 400     1555   1555  2.11  
LINK        MN    MN A 401                 O2G ANP A 400     1555   1555  2.22  
LINK        MN    MN A 402                 O1G ANP A 400     1555   1555  2.14  
LINK        MN    MN A 402                 O2B ANP A 400     1555   1555  2.07  
LINK        MN    MN A 402                 O   HOH A 564     1555   1555  2.04  
LINK        MN    MN A 402                 O   HOH A 527     1555   1555  2.20  
LINK         C   PHE A 138                 N   SEP A 139     1555   1555  1.31  
LINK         C   SEP A 139                 N   GLU A 140     1555   1555  1.33  
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  
CISPEP   1 LYS B   90    GLY B   91          0       -18.01                     
SITE     1 AC1  4 ASN A 171  ASP A 184  ANP A 400  HOH A 555                    
SITE     1 AC2  4 ASP A 184  ANP A 400  HOH A 527  HOH A 564                    
SITE     1 AC3  3 ARG A 137  HIS A 260  HOH A 454                               
SITE     1 AC4  4 HIS A 131  ARG A 134  ILE A 135  PHE A 314                    
SITE     1 AC5 10 GLY B 323  GLU B 324  ILE B 325  HOH B 410                    
SITE     2 AC5 10 HOH B 417  HOH B 428  HOH B 431  HOH B 452                    
SITE     3 AC5 10 HOH B 454  HOH B 502                                          
SITE     1 AC6  8 PHE A 257  PRO A 258  SER A 259  GLN B 283                    
SITE     2 AC6  8 GLY B 284  ARG B 303  HOH B 463  HOH B 495                    
SITE     1 AC7  5 ASP B 170  ASN B 171  TYR B 173  ARG B 209                    
SITE     2 AC7  5 HOH B 499                                                     
SITE     1 AC8  5 ARG B 239  ARG B 315  ARG B 340  HOH B 504                    
SITE     2 AC8  5 HOH B 506                                                     
SITE     1 AC9  7 ARG B  93  MET B 329  ASN B 330  ARG B 350                    
SITE     2 AC9  7 HOH B 415  HOH B 443  HOH B 480                               
SITE     1 BC1 29 GLY A  50  GLY A  52  SER A  53  PHE A  54                    
SITE     2 BC1 29 GLY A  55  VAL A  57  ALA A  70  LYS A  72                    
SITE     3 BC1 29 MET A 120  GLU A 121  VAL A 123  GLU A 127                    
SITE     4 BC1 29 ASP A 166  LYS A 168  GLU A 170  ASN A 171                    
SITE     5 BC1 29 LEU A 173  THR A 183  ASP A 184  PHE A 327                    
SITE     6 BC1 29  MN A 401   MN A 402  HOH A 424  HOH A 550                    
SITE     7 BC1 29 HOH A 555  HOH A 564  ARG B  94  GLY B  96                    
SITE     8 BC1 29 ALA B  97                                                     
SITE     1 BC2  8 LYS A 189  ARG A 194  THR A 195  TRP A 196                    
SITE     2 BC2  8 TPO A 197  TYR B 103  THR B 104  GLU B 105                    
SITE     1 BC3  6 GLU A 121  TYR A 122  VAL A 123  ALA A 124                    
SITE     2 BC3  6 ASP A 175  GLN A 176                                          
SITE     1 BC4  3 ASP A 329  TYR A 330  HOH A 548                               
SITE     1 BC5  6 LYS A  83  SER B  99  ALA B 100  GLU B 101                    
SITE     2 BC5  6 GLY B 206  ARG B 226                                          
CRYST1  125.809  125.809  140.941  90.00  90.00 120.00 P 32 2 1      6          
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      0.007949  0.004589  0.000000        0.00000                         
SCALE2      0.000000  0.009178  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007095        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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