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Database: PDB
Entry: 4NTT
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Original site: 4NTT 
HEADER    TRANSFERASE                             02-DEC-13   4NTT              
TITLE     STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE   
TITLE    2 BOUND TO ADP AND ONE MAGNESIUM ION                                   
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, KINASE, TRANSFERASE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.BASTIDAS,J.WU,S.S.TAYLOR                                          
REVDAT   2   28-JAN-15 4NTT    1       JRNL                                     
REVDAT   1   15-OCT-14 4NTT    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.    3.50 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) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 71.58                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 10114                          
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) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 516                             
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) : 3.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 767                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.41                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 38                           
REMARK   3   BIN FREE R VALUE                    : 0.4930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5206                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
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) : 93.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.48000                                              
REMARK   3    B22 (A**2) : -4.63000                                             
REMARK   3    B33 (A**2) : -2.11000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.68000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.735         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.643         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 92.329        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.893                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5400 ; 0.007 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7370 ; 1.114 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   680 ; 5.766 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   239 ;38.907 ;23.891       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   767 ;19.256 ;15.039       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;20.999 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   804 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4169 ; 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      4                      
REMARK   3           1     B     10       B     126      4                      
REMARK   3           2     A    327       A     350      4                      
REMARK   3           2     B    327       B     350      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1002 ; 0.540 ; 0.500           
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):   1571 ; 0.510 ; 0.500           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    10        A   126                          
REMARK   3    RESIDUE RANGE :   A   127        A   300                          
REMARK   3    RESIDUE RANGE :   A   301        A   326                          
REMARK   3    RESIDUE RANGE :   A   327        A   350                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.5402  49.5433  18.4871              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7153 T22:   0.7978                                     
REMARK   3      T33:   0.8516 T12:  -0.0634                                     
REMARK   3      T13:   0.0124 T23:   0.0703                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2560 L22:   3.3724                                     
REMARK   3      L33:   3.8608 L12:  -0.5111                                     
REMARK   3      L13:  -0.0327 L23:   1.0201                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0106 S12:  -0.1699 S13:  -0.1015                       
REMARK   3      S21:   0.1739 S22:   0.0118 S23:  -0.0346                       
REMARK   3      S31:   0.2769 S32:  -0.2515 S33:  -0.0012                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    10        B   126                          
REMARK   3    RESIDUE RANGE :   B   127        B   300                          
REMARK   3    RESIDUE RANGE :   B   301        B   326                          
REMARK   3    RESIDUE RANGE :   B   327        B   350                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.2262  19.4777 -20.0632              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7124 T22:   0.7437                                     
REMARK   3      T33:   0.8124 T12:  -0.0515                                     
REMARK   3      T13:  -0.0156 T23:  -0.0732                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4180 L22:   3.8565                                     
REMARK   3      L33:   4.3193 L12:  -0.7734                                     
REMARK   3      L13:   0.1621 L23:  -2.0669                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0189 S12:  -0.3315 S13:   0.0576                       
REMARK   3      S21:   0.2259 S22:   0.0628 S23:   0.2501                       
REMARK   3      S31:  -0.1590 S32:  -0.2047 S33:  -0.0438                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   401        A   401                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.3727  46.1927  28.5532              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4199 T22:   1.8281                                     
REMARK   3      T33:   1.6881 T12:   0.5143                                     
REMARK   3      T13:   0.5233 T23:   0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  59.4528 L22:   6.9773                                     
REMARK   3      L33:  53.7699 L12:  20.3540                                     
REMARK   3      L13:  56.5302 L23:  19.3603                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2458 S12:  -3.3969 S13:   1.2720                       
REMARK   3      S21:  -0.0874 S22:  -1.0417 S23:   0.3440                       
REMARK   3      S31:  -0.1950 S32:  -3.0604 S33:   1.2875                       
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 :   A   402        A   402                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.5510  46.7001  24.3552              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7689 T22:   0.8279                                     
REMARK   3      T33:   0.0073 T12:   0.1476                                     
REMARK   3      T13:   0.0412 T23:   0.0718                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:   0.0000                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   401        B   401                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.1474  20.1646 -12.1457              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5412 T22:   1.2350                                     
REMARK   3      T33:   0.9454 T12:  -0.0936                                     
REMARK   3      T13:  -0.2196 T23:   0.2457                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  34.2789 L22:   1.1389                                     
REMARK   3      L33:  12.7603 L12:  -6.2241                                     
REMARK   3      L13: -20.9116 L23:   3.7986                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8598 S12:   2.1324 S13:   0.5335                       
REMARK   3      S21:  -0.0580 S22:  -0.4448 S23:  -0.0795                       
REMARK   3      S31:  -0.5055 S32:  -1.3241 S33:  -0.4150                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   402        B   402                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.7422  17.6528 -17.9002              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7157 T22:   0.7779                                     
REMARK   3      T33:   0.7415 T12:   0.5716                                     
REMARK   3      T13:  -0.5425 T23:  -0.1074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:   0.0000                       
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 4NTT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-DEC-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB083647.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAR-12                          
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   : 10660                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.150                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
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 4NTS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
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, PH 8.0, VAPOR    
REMARK 280  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       71.57500            
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     LYS A     8                                                      
REMARK 465     GLY A     9                                                      
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 465     LYS B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A  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     GLN A  39    CG   CD   OE1  NE2                                  
REMARK 470     LEU A  40    CG   CD1  CD2                                       
REMARK 470     ASP A  41    CG   OD1  OD2                                       
REMARK 470     ASP A  44    CG   OD1  OD2                                       
REMARK 470     ARG A  45    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A  46    CG1  CG2  CD1                                       
REMARK 470     LYS A  47    CG   CD   CE   NZ                                   
REMARK 470     LEU A  49    CG   CD1  CD2                                       
REMARK 470     THR A  51    OG1  CG2                                            
REMARK 470     ARG A  56    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A  58    CG   SD   CE                                        
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     ILE A  73    CD1                                                 
REMARK 470     LYS A  78    CG   CD   CE   NZ                                   
REMARK 470     LYS A  81    CG   CD   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     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 A 342    CG   CD   CE   NZ                                   
REMARK 470     THR A 348    OG1  CG2                                            
REMARK 470     GLU B  11    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  12    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  13    CG   CD   OE1  OE2                                  
REMARK 470     SER B  14    OG                                                  
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     GLU B  24    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  29    CG   CD   CE   NZ                                   
REMARK 470     ASP B  44    CG   OD1  OD2                                       
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     LEU B  49    CG   CD1  CD2                                       
REMARK 470     ARG B  56    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B  60    CG1  CG2                                            
REMARK 470     LYS B  61    CG   CD   CE   NZ                                   
REMARK 470     LYS B  63    CG   CD   CE   NZ                                   
REMARK 470     GLU B  64    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  72    CG   CD   CE   NZ                                   
REMARK 470     ILE B  73    CD1                                                 
REMARK 470     LYS B  78    CG   CD   CE   NZ                                   
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 114    OG                                                  
REMARK 470     GLU B 127    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 135    CD1                                                 
REMARK 470     VAL B 191    CG1  CG2                                            
REMARK 470     ILE B 210    CD1                                                 
REMARK 470     LYS B 213    CG   CD   CE   NZ                                   
REMARK 470     ILE B 228    CD1                                                 
REMARK 470     GLN B 242    CD   OE1  NE2                                       
REMARK 470     ILE B 246    CD1                                                 
REMARK 470     LYS B 249    CG   CD   CE   NZ                                   
REMARK 470     SER B 252    OG                                                  
REMARK 470     VAL B 255    CG1  CG2                                            
REMARK 470     ARG B 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 263    OG                                                  
REMARK 470     VAL B 275    CG1  CG2                                            
REMARK 470     LYS B 285    CG   CD   CE   NZ                                   
REMARK 470     ILE B 291    CD1                                                 
REMARK 470     LYS B 295    CG   CD   CE   NZ                                   
REMARK 470     ILE B 303    CD1                                                 
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     PHE B 318    CG   CD1  CD2  CE1  CE2  CZ                         
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     ASP B 328    CG   OD1  OD2                                       
REMARK 470     ASP B 329    CG   OD1  OD2                                       
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     ARG B 336    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 337    CG1  CG2                                            
REMARK 470     LYS B 342    CG   CD   CE   NZ                                   
REMARK 470     THR B 348    OG1  CG2                                            
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   OH   TYR B   204     OE2  GLU B   230              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A 137   CZ    ARG A 137   NH2     0.087                       
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    ASN A  36       57.83     37.61                                   
REMARK 500    ILE A  46      -63.95    -93.71                                   
REMARK 500    LEU A  74      107.57   -162.35                                   
REMARK 500    ASN A  99      114.94   -169.03                                   
REMARK 500    ASP A 112     -125.14   -141.20                                   
REMARK 500    THR A 183     -132.96     58.00                                   
REMARK 500    LYS A 309       49.65    -79.53                                   
REMARK 500    ASP A 329     -167.32     74.30                                   
REMARK 500    GLU A 334     -150.34     57.97                                   
REMARK 500    LYS B  83       71.55     44.80                                   
REMARK 500    ASN B  99       98.84   -166.42                                   
REMARK 500    PRO B 101      -35.73    -37.65                                   
REMARK 500    PHE B 110      148.99   -175.17                                   
REMARK 500    ASP B 166       46.04   -140.43                                   
REMARK 500    ASP B 175      174.82    -55.95                                   
REMARK 500    SER B 212        6.86     59.05                                   
REMARK 500    ASP B 241      -73.89    -70.23                                   
REMARK 500    HIS B 260        5.45    -68.35                                   
REMARK 500    LEU B 273       53.17    -95.09                                   
REMARK 500    ASN B 283       56.48   -109.12                                   
REMARK 500    PHE B 297       50.99    -93.83                                   
REMARK 500    ARG B 308       18.47     58.55                                   
REMARK 500    LYS B 309       46.37    -94.44                                   
REMARK 500    ASN B 326       49.21     32.60                                   
REMARK 500    ASP B 328      151.58     74.14                                   
REMARK 500    TYR B 330       -8.55     77.22                                   
REMARK 500    GLU B 331       14.72     52.87                                   
REMARK 500    GLU B 334      176.34     64.88                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 VAL A  182     THR A  183                  142.43                    
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                              MG A 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 401   O2A                                                    
REMARK 620 2 ASP A 184   OD2 103.2                                              
REMARK 620 3 ADP A 401   O3B  69.1  76.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP B 401   O2A                                                    
REMARK 620 2 ADP B 401   O3B  62.6                                              
REMARK 620 3 ASP B 184   OD2 105.2  68.4                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 402                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4NTS   RELATED DB: PDB                                   
REMARK 900 APO STRUCTURE OF THE C-SUBUNIT                                       
REMARK 900 RELATED ID: 1J3H   RELATED DB: PDB                                   
REMARK 900 ANOTHER APO STRUCTURE OF THE C-SUBUNIT                               
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 ANOTHER APO STRUCTURE OF THE C-SUBUNIT WITH E230Q MUTATION           
REMARK 900 RELATED ID: 1ATP   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE C-SUBUNIT BOUND TO ATP AND IP20                     
DBREF  4NTT A    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  4NTT B    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
SEQADV 4NTT CYS A    7  UNP  P05132    LYS     8 EXPRESSION TAG                 
SEQADV 4NTT 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 4NTT TPO A  197  THR  PHOSPHOTHREONINE                                   
MODRES 4NTT SEP A  338  SER  PHOSPHOSERINE                                      
MODRES 4NTT TPO B  197  THR  PHOSPHOTHREONINE                                   
MODRES 4NTT 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    ADP  A 401      27                                                       
HET     MG  A 402       1                                                       
HET    ADP  B 401      27                                                       
HET     MG  B 402       1                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
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  ADP    2(C10 H15 N5 O10 P2)                                         
FORMUL   4   MG    2(MG 2+)                                                     
HELIX    1   1 GLU A   13  THR A   32  1                                  20    
HELIX    2   2 LYS A   76  LEU A   82  1                                   7    
HELIX    3   3 GLN A   84  VAL A   98  1                                  15    
HELIX    4   4 GLU A  127  ILE A  135  1                                   9    
HELIX    5   5 SER A  139  LEU A  160  1                                  22    
HELIX    6   6 ALA A  206  LEU A  211  1                                   6    
HELIX    7   7 ALA A  218  GLY A  234  1                                  17    
HELIX    8   8 GLN A  242  SER A  252  1                                  11    
HELIX    9   9 SER A  262  LEU A  273  1                                  12    
HELIX   10  10 VAL A  288  ASN A  293  1                                   6    
HELIX   11  11 HIS A  294  ALA A  298  5                                   5    
HELIX   12  12 ASP A  301  GLN A  307  1                                   7    
HELIX   13  13 GLU B   13  THR B   32  1                                  20    
HELIX   14  14 GLN B   39  ASP B   41  5                                   3    
HELIX   15  15 LYS B   76  LEU B   82  1                                   7    
HELIX   16  16 GLN B   84  VAL B   98  1                                  15    
HELIX   17  17 GLU B  127  GLY B  136  1                                  10    
HELIX   18  18 SER B  139  LEU B  160  1                                  22    
HELIX   19  19 ALA B  206  LEU B  211  1                                   6    
HELIX   20  20 ALA B  218  GLY B  234  1                                  17    
HELIX   21  21 GLN B  242  SER B  252  1                                  11    
HELIX   22  22 SER B  262  LEU B  273  1                                  12    
HELIX   23  23 VAL B  288  ASN B  293  1                                   6    
HELIX   24  24 HIS B  294  ALA B  298  5                                   5    
HELIX   25  25 ASP B  301  GLN B  307  1                                   7    
SHEET    1   A 5 PHE A  43  THR A  51  0                                        
SHEET    2   A 5 ARG A  56  HIS A  62 -1  O  LEU A  59   N  ILE A  46           
SHEET    3   A 5 HIS A  68  ASP A  75 -1  O  TYR A  69   N  VAL A  60           
SHEET    4   A 5 ASN A 115  GLU A 121 -1  O  MET A 118   N  LYS A  72           
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  GLY B  50  0                                        
SHEET    2   D 5 VAL B  57  HIS B  62 -1  O  VAL B  57   N  GLY B  50           
SHEET    3   D 5 HIS B  68  ASP B  75 -1  O  MET B  71   N  MET B  58           
SHEET    4   D 5 ASN B 115  GLU B 121 -1  O  MET B 120   N  ALA B  70           
SHEET    5   D 5 LEU B 106  LYS B 111 -1  N  GLU B 107   O  VAL B 119           
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  1.34  
LINK         C   SEP A 338                 N   ILE A 339     1555   1555  1.33  
LINK         C   TRP B 196                 N   TPO B 197     1555   1555  1.33  
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  
LINK         O2A ADP A 401                MG    MG A 402     1555   1555  1.91  
LINK         OD2 ASP A 184                MG    MG A 402     1555   1555  2.39  
LINK         O2A ADP B 401                MG    MG B 402     1555   1555  2.40  
LINK         O3B ADP A 401                MG    MG A 402     1555   1555  2.65  
LINK         O3B ADP B 401                MG    MG B 402     1555   1555  2.67  
LINK         OD2 ASP B 184                MG    MG B 402     1555   1555  2.70  
SITE     1 AC1  8 SER A  53  ALA A  70  GLU A 121  TYR A 122                    
SITE     2 AC1  8 VAL A 123  THR A 183  ASP A 184   MG A 402                    
SITE     1 AC2  3 ASN A 171  ASP A 184  ADP A 401                               
SITE     1 AC3  8 SER B  53  VAL B  57  ALA B  70  GLU B 121                    
SITE     2 AC3  8 VAL B 123  THR B 183  ASP B 184   MG B 402                    
SITE     1 AC4  3 ASN B 171  ASP B 184  ADP B 401                               
CRYST1   50.480  143.150   62.570  90.00 103.61  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      0.019810  0.000000  0.004796        0.00000                         
SCALE2      0.000000  0.006986  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016444        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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