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Database: PDB
Entry: 2C1J
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Original site: 2C1J 
HEADER    SIGNALING PROTEIN                       15-SEP-05   2C1J              
TITLE     MOLECULAR BASIS FOR THE RECOGNITION OF PHOSPHORYLATED AND             
TITLE    2 PHOSPHOACETYLATED HISTONE H3 BY 14-3-3                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 14-3-3 PROTEIN ZETA/DELTA;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PROTEIN KINASE C INHIBITOR PROTEIN 1, KCIP-1;               
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: HISTONE H3 ACETYLPHOSPHOPEPTIDE;                           
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 FRAGMENT: 14-3-3, HISTONE H3 ACETYLPHOSPHOPEPTIDE (RESIDUES 7-14)    
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: B834 PLYS/S;                               
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PACYC;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES                                                       
KEYWDS    SIGNALING PROTEIN-COMPLEX, NUCLEOSOME, SIGNALING PROTEIN              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.P.I.WELBURN,N.MACDONALD,M.E.M.NOBLE,A.NGUYEN,M.B.YAFFE,D.CLYNES,    
AUTHOR   2 J.G.MOGGS,G.ORPHANIDES,S.THOMSON,J.W.EDMUNDS,A.L.CLAYTON,            
AUTHOR   3 J.A.ENDICOTT,L.C.MAHADEVAN                                           
REVDAT   4   18-SEP-13 2C1J    1       KEYWDS REMARK                            
REVDAT   3   13-JUL-11 2C1J    1       VERSN                                    
REVDAT   2   24-FEB-09 2C1J    1       VERSN                                    
REVDAT   1   02-NOV-05 2C1J    0                                                
JRNL        AUTH   N.MACDONALD,J.P.I.WELBURN,M.E.M.NOBLE,A.NGUYEN,M.B.YAFFE,    
JRNL        AUTH 2 D.CLYNES,J.G.MOGGS,G.ORPHANIDES,S.THOMSON,J.W.EDMUNDS,       
JRNL        AUTH 3 A.L.CLAYTON,J.A.ENDICOTT,L.C.MAHADEVAN                       
JRNL        TITL   MOLECULAR BASIS FOR THE RECOGNITION OF PHOSPHORYLATED AND    
JRNL        TITL 2 PHOSPHOACETYLATED HISTONE H3 BY 14-3-3.                      
JRNL        REF    MOL.CELL                      V.  20   199 2005              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   16246723                                                     
JRNL        DOI    10.1016/J.MOLCEL.2005.08.032                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 69.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 20689                          
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                     : 0.292                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1113                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1492                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 87                           
REMARK   3   BIN FREE R VALUE                    : 0.4050                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3762                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 86                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : UNVERIFIED                                          
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.67000                                              
REMARK   3    B22 (A**2) : -3.11000                                             
REMARK   3    B33 (A**2) : 2.92000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 7.76000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.525         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.336         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.296         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.333        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.890                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3852 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5164 ; 1.527 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   468 ; 6.601 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   188 ;41.963 ;25.319       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   748 ;21.680 ;15.040       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;21.378 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   570 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2834 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1988 ; 0.271 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2651 ; 0.312 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   198 ; 0.197 ; 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):    56 ; 0.250 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.144 ; 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):  2420 ; 0.479 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3768 ; 0.859 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1615 ; 1.380 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1396 ; 2.261 ; 4.500       
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 : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     230      2                      
REMARK   3           1     B      1       B     230      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    920 ;   .04 ;   .05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):    920 ;   .04 ;   .05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    921 ;   .26 ;   .50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    921 ;   .26 ;   .50           
REMARK   3   TIGHT THERMAL      1    A (A**2):    920 ;   .06 ;   .50           
REMARK   3   TIGHT THERMAL      1    B (A**2):    920 ;   .06 ;   .50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    921 ;   .47 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):    921 ;   .47 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C      7       C      14      2                      
REMARK   3           1     D      7       D      14      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    C    (A):     32 ;   .12 ;   .05           
REMARK   3   TIGHT POSITIONAL   2    D    (A):     32 ;   .12 ;   .05           
REMARK   3   MEDIUM POSITIONAL  2    C    (A):     30 ;   .45 ;   .50           
REMARK   3   MEDIUM POSITIONAL  2    D    (A):     30 ;   .45 ;   .50           
REMARK   3   TIGHT THERMAL      2    C (A**2):     32 ;   .06 ;   .50           
REMARK   3   TIGHT THERMAL      2    D (A**2):     32 ;   .06 ;   .50           
REMARK   3   MEDIUM THERMAL     2    C (A**2):     30 ;   .55 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    D (A**2):     30 ;   .55 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   230                          
REMARK   3    RESIDUE RANGE :   C     7        C    14                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.7910   -.0840  12.3520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   -.0944 T22:    .0299                                     
REMARK   3      T33:   -.0500 T12:   -.0099                                     
REMARK   3      T13:   -.0544 T23:   -.0938                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4529 L22:   2.4902                                     
REMARK   3      L33:   1.9700 L12:    .9249                                     
REMARK   3      L13:   -.9665 L23:  -1.7620                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .4054 S12:   -.2752 S13:    .2820                       
REMARK   3      S21:    .2436 S22:    .0230 S23:   -.0329                       
REMARK   3      S31:   -.4959 S32:    .1852 S33:   -.4284                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   230                          
REMARK   3    RESIDUE RANGE :   D     7        D    14                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.6550 -34.2530  22.1320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   -.0793 T22:    .0231                                     
REMARK   3      T33:    .0134 T12:    .0862                                     
REMARK   3      T13:   -.0142 T23:    .0434                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2674 L22:   2.1352                                     
REMARK   3      L33:   1.0948 L12:   1.6453                                     
REMARK   3      L13:   -.7089 L23:   -.2676                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.4607 S12:   -.2623 S13:   -.6693                       
REMARK   3      S21:    .0308 S22:    .0667 S23:   -.2847                       
REMARK   3      S31:    .2197 S32:    .2246 S33:    .3940                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2C1J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-SEP-05.                  
REMARK 100 THE PDBE ID CODE IS EBI-25634.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-OCT-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21834                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 21.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1QJA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.2                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.2                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH7.0, 23% ETHYLENE          
REMARK 280  GLYCOL                                                              
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       36.20650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, C                            
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     MET A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     GLN A    -1                                                      
REMARK 465     ASP A     0                                                      
REMARK 465     ASP A   231                                                      
REMARK 465     THR A   232                                                      
REMARK 465     GLN A   233                                                      
REMARK 465     GLY A   234                                                      
REMARK 465     ASP A   235                                                      
REMARK 465     GLU A   236                                                      
REMARK 465     ALA A   237                                                      
REMARK 465     GLU A   238                                                      
REMARK 465     ALA A   239                                                      
REMARK 465     GLY A   240                                                      
REMARK 465     GLU A   241                                                      
REMARK 465     GLY A   242                                                      
REMARK 465     GLY A   243                                                      
REMARK 465     GLU A   244                                                      
REMARK 465     ASN A   245                                                      
REMARK 465     MET B   -12                                                      
REMARK 465     GLY B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     GLN B    -1                                                      
REMARK 465     ASP B     0                                                      
REMARK 465     ASP B   231                                                      
REMARK 465     THR B   232                                                      
REMARK 465     GLN B   233                                                      
REMARK 465     GLY B   234                                                      
REMARK 465     ASP B   235                                                      
REMARK 465     GLU B   236                                                      
REMARK 465     ALA B   237                                                      
REMARK 465     GLU B   238                                                      
REMARK 465     ALA B   239                                                      
REMARK 465     GLY B   240                                                      
REMARK 465     GLU B   241                                                      
REMARK 465     GLY B   242                                                      
REMARK 465     GLY B   243                                                      
REMARK 465     GLU B   244                                                      
REMARK 465     ASN B   245                                                      
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     SER A 230    OG                                                  
REMARK 470     SER B 230    OG                                                  
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    ALA A  23      -75.28    -57.25                                   
REMARK 500    ALA A  24      -37.23    -37.84                                   
REMARK 500    SER A  57      -76.07    -62.85                                   
REMARK 500    SER A  58      -55.71    -23.70                                   
REMARK 500    ASP A  96      -76.50    -24.19                                   
REMARK 500    PHE A 104      -73.13   -105.65                                   
REMARK 500    ALA A 134      -26.70    152.05                                   
REMARK 500    ASP A 136      -64.16     85.95                                   
REMARK 500    ILE A 181      -64.58    -96.13                                   
REMARK 500    SER A 210        4.88   -150.53                                   
REMARK 500    ALA B  23      -72.08    -61.87                                   
REMARK 500    SER B  28      -73.82    -55.27                                   
REMARK 500    VAL B  29      -62.61    -27.38                                   
REMARK 500    THR B  88      -70.53    -50.79                                   
REMARK 500    ASP B  96      -78.23    -19.15                                   
REMARK 500    PHE B 104      -77.91   -102.85                                   
REMARK 500    ALA B 134      -29.42    159.83                                   
REMARK 500    ASP B 136      -63.00     86.49                                   
REMARK 500    ILE B 181      -64.50    -95.99                                   
REMARK 500    ASP B 204        0.92    -69.28                                   
REMARK 500    GLU B 209       -4.45    -56.56                                   
REMARK 500    SER B 210       -0.34   -145.99                                   
REMARK 500    ARG C   8      158.49    -44.42                                   
REMARK 500    THR C  11      -54.19    -23.79                                   
REMARK 500    ARG D   8      157.45    -40.89                                   
REMARK 500    THR D  11      -50.73    -24.94                                   
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 GLY D   13     LYS D   14                 -128.04                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ARG C   8        -35.18                                           
REMARK 500    ALY C   9         31.17                                           
REMARK 500    ARG D   8        -32.34                                           
REMARK 500    ALY D   9         24.35                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LYS D  14        22.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1IB1   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE 14-3-3 ZETA:                               
REMARK 900  SEROTONIN N-ACETYLTRANSFERASE COMPLEX                               
REMARK 900 RELATED ID: 1QJA   RELATED DB: PDB                                   
REMARK 900  14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 2)                         
REMARK 900 RELATED ID: 1QJB   RELATED DB: PDB                                   
REMARK 900  14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 1)                         
DBREF  2C1J A  -12     0  PDB    2C1J     2C1J           -12      0             
DBREF  2C1J A    1   245  UNP    P63104   1433Z_HUMAN      1    245             
DBREF  2C1J B  -12     0  PDB    2C1J     2C1J           -12      0             
DBREF  2C1J B    1   245  UNP    P63104   1433Z_HUMAN      1    245             
DBREF  2C1J C    7    14  PDB    2C1J     2C1J             7     14             
DBREF  2C1J D    7    14  PDB    2C1J     2C1J             7     14             
SEQRES   1 A  258  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 A  258  MET ASP LYS ASN GLU LEU VAL GLN LYS ALA LYS LEU ALA          
SEQRES   3 A  258  GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA CYS MET          
SEQRES   4 A  258  LYS SER VAL THR GLU GLN GLY ALA GLU LEU SER ASN GLU          
SEQRES   5 A  258  GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL          
SEQRES   6 A  258  GLY ALA ARG ARG SER SER TRP ARG VAL VAL SER SER ILE          
SEQRES   7 A  258  GLU GLN LYS THR GLU GLY ALA GLU LYS LYS GLN GLN MET          
SEQRES   8 A  258  ALA ARG GLU TYR ARG GLU LYS ILE GLU THR GLU LEU ARG          
SEQRES   9 A  258  ASP ILE CYS ASN ASP VAL LEU SER LEU LEU GLU LYS PHE          
SEQRES  10 A  258  LEU ILE PRO ASN ALA SER GLN ALA GLU SER LYS VAL PHE          
SEQRES  11 A  258  TYR LEU LYS MET LYS GLY ASP TYR TYR ARG TYR LEU ALA          
SEQRES  12 A  258  GLU VAL ALA ALA GLY ASP ASP LYS LYS GLY ILE VAL ASP          
SEQRES  13 A  258  GLN SER GLN GLN ALA TYR GLN GLU ALA PHE GLU ILE SER          
SEQRES  14 A  258  LYS LYS GLU MET GLN PRO THR HIS PRO ILE ARG LEU GLY          
SEQRES  15 A  258  LEU ALA LEU ASN PHE SER VAL PHE TYR TYR GLU ILE LEU          
SEQRES  16 A  258  ASN SER PRO GLU LYS ALA CYS SER LEU ALA LYS THR ALA          
SEQRES  17 A  258  PHE ASP GLU ALA ILE ALA GLU LEU ASP THR LEU SER GLU          
SEQRES  18 A  258  GLU SER TYR LYS ASP SER THR LEU ILE MET GLN LEU LEU          
SEQRES  19 A  258  ARG ASP ASN LEU THR LEU TRP THR SER ASP THR GLN GLY          
SEQRES  20 A  258  ASP GLU ALA GLU ALA GLY GLU GLY GLY GLU ASN                  
SEQRES   1 B  258  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 B  258  MET ASP LYS ASN GLU LEU VAL GLN LYS ALA LYS LEU ALA          
SEQRES   3 B  258  GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA CYS MET          
SEQRES   4 B  258  LYS SER VAL THR GLU GLN GLY ALA GLU LEU SER ASN GLU          
SEQRES   5 B  258  GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL          
SEQRES   6 B  258  GLY ALA ARG ARG SER SER TRP ARG VAL VAL SER SER ILE          
SEQRES   7 B  258  GLU GLN LYS THR GLU GLY ALA GLU LYS LYS GLN GLN MET          
SEQRES   8 B  258  ALA ARG GLU TYR ARG GLU LYS ILE GLU THR GLU LEU ARG          
SEQRES   9 B  258  ASP ILE CYS ASN ASP VAL LEU SER LEU LEU GLU LYS PHE          
SEQRES  10 B  258  LEU ILE PRO ASN ALA SER GLN ALA GLU SER LYS VAL PHE          
SEQRES  11 B  258  TYR LEU LYS MET LYS GLY ASP TYR TYR ARG TYR LEU ALA          
SEQRES  12 B  258  GLU VAL ALA ALA GLY ASP ASP LYS LYS GLY ILE VAL ASP          
SEQRES  13 B  258  GLN SER GLN GLN ALA TYR GLN GLU ALA PHE GLU ILE SER          
SEQRES  14 B  258  LYS LYS GLU MET GLN PRO THR HIS PRO ILE ARG LEU GLY          
SEQRES  15 B  258  LEU ALA LEU ASN PHE SER VAL PHE TYR TYR GLU ILE LEU          
SEQRES  16 B  258  ASN SER PRO GLU LYS ALA CYS SER LEU ALA LYS THR ALA          
SEQRES  17 B  258  PHE ASP GLU ALA ILE ALA GLU LEU ASP THR LEU SER GLU          
SEQRES  18 B  258  GLU SER TYR LYS ASP SER THR LEU ILE MET GLN LEU LEU          
SEQRES  19 B  258  ARG ASP ASN LEU THR LEU TRP THR SER ASP THR GLN GLY          
SEQRES  20 B  258  ASP GLU ALA GLU ALA GLY GLU GLY GLY GLU ASN                  
SEQRES   1 C    8  ALA ARG ALY SEP THR GLY GLY LYS                              
SEQRES   1 D    8  ALA ARG ALY SEP THR GLY GLY LYS                              
MODRES 2C1J SEP C   10  SER  PHOSPHOSERINE                                      
MODRES 2C1J SEP D   10  SER  PHOSPHOSERINE                                      
MODRES 2C1J ALY C    9  LYS  N(6)-ACETYLLYSINE                                  
MODRES 2C1J ALY D    9  LYS  N(6)-ACETYLLYSINE                                  
HET    ALY  C   9      12                                                       
HET    SEP  C  10      10                                                       
HET    ALY  D   9      12                                                       
HET    SEP  D  10      10                                                       
HETNAM     ALY N(6)-ACETYLLYSINE                                                
HETNAM     SEP PHOSPHOSERINE                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     ALY NZ-ACETYL LYSINE                                                 
FORMUL   3  ALY    2(C8 H16 N2 O3)                                              
FORMUL   3  SEP    2(C3 H8 N O6 P)                                              
FORMUL   5  HOH   *86(H2 O)                                                     
HELIX    1   1 ASP A    2  ALA A   16  1                                  15    
HELIX    2   2 ARG A   18  GLN A   32  1                                  15    
HELIX    3   3 SER A   37  GLN A   67  1                                  31    
HELIX    4   4 ALA A   72  PHE A  104  1                                  33    
HELIX    5   5 GLN A  111  GLU A  131  1                                  21    
HELIX    6   6 ASP A  136  MET A  160  1                                  25    
HELIX    7   7 HIS A  164  ILE A  181  1                                  18    
HELIX    8   8 SER A  184  ALA A  201  1                                  18    
HELIX    9   9 GLU A  202  LEU A  206  5                                   5    
HELIX   10  10 SER A  207  GLU A  209  5                                   3    
HELIX   11  11 SER A  210  SER A  230  1                                  21    
HELIX   12  12 ASP B    2  ALA B   16  1                                  15    
HELIX   13  13 ARG B   18  GLN B   32  1                                  15    
HELIX   14  14 SER B   37  THR B   69  1                                  33    
HELIX   15  15 ALA B   72  PHE B  104  1                                  33    
HELIX   16  16 GLN B  111  GLU B  131  1                                  21    
HELIX   17  17 ASP B  136  MET B  160  1                                  25    
HELIX   18  18 HIS B  164  ILE B  181  1                                  18    
HELIX   19  19 SER B  184  ALA B  201  1                                  18    
HELIX   20  20 GLU B  202  LEU B  206  5                                   5    
HELIX   21  21 SER B  207  GLU B  209  5                                   3    
HELIX   22  22 SER B  210  SER B  230  1                                  21    
LINK         C   ARG C   8                 N   ALY C   9     1555   1555  1.84  
LINK         C   ALY C   9                 N   SEP C  10     1555   1555  1.79  
LINK         C   SEP C  10                 N   THR C  11     1555   1555  1.33  
LINK         C   ARG D   8                 N   ALY D   9     1555   1555  1.36  
LINK         C   ALY D   9                 N   SEP D  10     1555   1555  1.34  
LINK         C   SEP D  10                 N   THR D  11     1555   1555  1.32  
CISPEP   1 ALA A  133    ALA A  134          0        -6.39                     
CISPEP   2 ALA B  133    ALA B  134          0       -11.19                     
CISPEP   3 GLY C   13    LYS C   14          0       -21.66                     
CRYST1   71.191   72.413   71.160  90.00 102.96  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      0.014047  0.000000  0.003233        0.00000                         
SCALE2      0.000000  0.013810  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014420        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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