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Database: PDB
Entry: 3NKX
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Original site: 3NKX 
HEADER    PROTEIN BINDING, SIGNALING PROTEIN      21-JUN-10   3NKX              
TITLE     IMPAIRED BINDING OF 14-3-3 TO RAF1 IS LINKED TO NOONAN AND LEOPARD    
TITLE    2 SYNDROME                                                             
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: PEPTIDE OF RAF PROTO-ONCOGENE SERINE/THREONINE-PROTEIN     
COMPND   8 KINASE;                                                              
COMPND   9 CHAIN: P, Q;                                                         
COMPND  10 FRAGMENT: PHOSPHORYLATED C-RAF PEPTIDE, UNP RESIDUES 255-264;        
COMPND  11 SYNONYM: PROTO-ONCOGENE C-RAF, CRAF, RAF-1;                          
COMPND  12 EC: 2.7.11.1;                                                        
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: YWHAZ;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.             
KEYWDS    PROTEIN BINDING, SIGNALING PROTEIN                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.SCHUMACHER,M.WEYAND,C.OTTMANN                                       
REVDAT   3   08-NOV-17 3NKX    1       REMARK                                   
REVDAT   2   26-FEB-14 3NKX    1       JRNL   VERSN                             
REVDAT   1   15-SEP-10 3NKX    0                                                
JRNL        AUTH   M.MOLZAN,B.SCHUMACHER,C.OTTMANN,A.BALJULS,L.POLZIEN,         
JRNL        AUTH 2 M.WEYAND,P.THIEL,R.ROSE,M.ROSE,P.KUHENNE,M.KAISER,U.R.RAPP,  
JRNL        AUTH 3 J.KUHLMANN,C.OTTMANN                                         
JRNL        TITL   IMPAIRED BINDING OF 14-3-3 TO C-RAF IN NOONAN SYNDROME       
JRNL        TITL 2 SUGGESTS NEW APPROACHES IN DISEASES WITH INCREASED RAS       
JRNL        TITL 3 SIGNALING                                                    
JRNL        REF    MOL.CELL.BIOL.                V.  30  4698 2010              
JRNL        REFN                   ISSN 0270-7306                               
JRNL        PMID   20679480                                                     
JRNL        DOI    10.1128/MCB.01636-09                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 60.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 25804                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.247                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1359                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1889                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 100                          
REMARK   3   BIN FREE R VALUE                    : 0.3750                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3730                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 183                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.20000                                             
REMARK   3    B22 (A**2) : 2.10000                                              
REMARK   3    B33 (A**2) : -1.90000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.236         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.161         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.827         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3797 ; 0.022 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5126 ; 1.990 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   473 ; 6.697 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   183 ;38.035 ;25.246       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   699 ;21.029 ;15.043       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;17.139 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   579 ; 0.161 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2829 ; 0.009 ; 0.020       
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):  2368 ; 1.148 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3788 ; 2.227 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1429 ; 3.553 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1336 ; 5.881 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 3NKX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000059958.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-AUG-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97809                            
REMARK 200  MONOCHROMATOR                  : LN2 COOLED FIXED-EXIT SI(111)      
REMARK 200                                   MONOCHROMATOR, SAGITTAL-           
REMARK 200                                   HORIZONTAL; DYNAMICALLY BENDABLE   
REMARK 200                                   MIRROR, MERIDIONAL-VERTICAL        
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27180                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.760                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : 0.04950                            
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) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.020                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1QJB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M (SODIUM PROPIONATE, SODIUM          
REMARK 280  CACODYLATE, BIS-TRIS PROPANE), 27% PEG 1500, 2MM DTT, PH 8.0,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       36.20500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.83500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.92500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.83500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.20500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.92500            
REMARK 290   SMTRY3   4  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: 4470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P, Q                            
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     1                                                      
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     GLY B    71                                                      
REMARK 465     ALA B    72                                                      
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 465     GLN P   255                                                      
REMARK 465     GLN Q   255                                                      
REMARK 465     HIS Q   264                                                      
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     ASP A   2    CG   OD1  OD2                                       
REMARK 470     LYS A   3    CG   CD   CE   NZ                                   
REMARK 470     GLU A   5    CG   CD   OE1  OE2                                  
REMARK 470     GLN A   8    CG   CD   OE1  NE2                                  
REMARK 470     LYS A   9    CG   CD   CE   NZ                                   
REMARK 470     LYS A  68    CE   NZ                                             
REMARK 470     GLN A  77    CD   OE1  NE2                                       
REMARK 470     LYS A 157    CE   NZ                                             
REMARK 470     LYS B   3    CG   CD   CE   NZ                                   
REMARK 470     LYS B  68    CG   CD   CE   NZ                                   
REMARK 470     GLU B  73    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  74    CG   CD   CE   NZ                                   
REMARK 470     LYS B  75    NZ                                                  
REMARK 470     GLN B  77    CD   OE1  NE2                                       
REMARK 470     ARG B  80    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP B 136    CG   OD1  OD2                                       
REMARK 470     LYS B 139    CG   CD   CE   NZ                                   
REMARK 470     LYS B 157    CD   CE   NZ                                        
REMARK 470     LYS B 158    CG   CD   CE   NZ                                   
REMARK 470     GLU B 208    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 212    CG   CD   CE   NZ                                   
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   OG   SER A   114     O    HOH A   276              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OH   TYR A   211     O    ILE B   200     4545     1.94            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  41   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    PRO A 165   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    LEU A 206   CA  -  CB  -  CG  ANGL. DEV. =  15.9 DEGREES          
REMARK 500    VAL B  52   CB  -  CA  -  C   ANGL. DEV. = -11.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A   3      -23.06    -34.28                                   
REMARK 500    GLN A  32        2.97    -57.73                                   
REMARK 500    SER A  37     -179.02    -60.23                                   
REMARK 500    ALA A  72       54.36     30.36                                   
REMARK 500    ASN A 183       44.27     35.11                                   
REMARK 500    LYS B  68       31.99    156.85                                   
REMARK 500    ILE B 181      -61.85    -97.70                                   
REMARK 500    SER B 184       77.15   -106.45                                   
REMARK 500    GLU B 202       30.71   -145.55                                   
REMARK 500    ASP B 204      -84.23    -46.17                                   
REMARK 500    THR B 205       12.34    -33.72                                   
REMARK 500    THR B 229       50.95    -94.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PPI A 247                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3M50   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE 14-3-3/PMA2 COMPLEX STABILIZED BY EPIBESTATIN       
REMARK 900 RELATED ID: 3M51   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE 14-3-3/PMA2 COMPLEX STABILIZED BY PYRROLIDONE1      
REMARK 900 RELATED ID: 3LW1   RELATED DB: PDB                                   
REMARK 900 BINARY COMPLEX OF 14-3-3 SIGMA AND P53 PT387-PEPTIDE                 
REMARK 900 RELATED ID: 3E6Y   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF 14-3-3 IN COMPLEX WITH THE DIFFERENTIATION-INDUCING     
REMARK 900 AGENT COTYLENIN A                                                    
REMARK 900 RELATED ID: 2O02   RELATED DB: PDB                                   
REMARK 900 PHOSPHORYLATION INDEPENDENT INTERACTIONS BETWEEN 14-3-3 AND          
REMARK 900 EXOENZYME S: FROM STRUCTURE TO PATHOGENESIS                          
REMARK 900 RELATED ID: 2O98   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE 14-3-3 / H+-ATPASE PLANT COMPLEX                    
DBREF  3NKX A    1   245  UNP    P63104   1433Z_HUMAN      1    245             
DBREF  3NKX B    1   245  UNP    P63104   1433Z_HUMAN      1    245             
DBREF  3NKX P  255   264  UNP    P04049   RAF1_HUMAN     255    264             
DBREF  3NKX Q  255   264  UNP    P04049   RAF1_HUMAN     255    264             
SEQRES   1 A  245  MET ASP LYS ASN GLU LEU VAL GLN LYS ALA LYS LEU ALA          
SEQRES   2 A  245  GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA CYS MET          
SEQRES   3 A  245  LYS SER VAL THR GLU GLN GLY ALA GLU LEU SER ASN GLU          
SEQRES   4 A  245  GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL          
SEQRES   5 A  245  GLY ALA ARG ARG SER SER TRP ARG VAL VAL SER SER ILE          
SEQRES   6 A  245  GLU GLN LYS THR GLU GLY ALA GLU LYS LYS GLN GLN MET          
SEQRES   7 A  245  ALA ARG GLU TYR ARG GLU LYS ILE GLU THR GLU LEU ARG          
SEQRES   8 A  245  ASP ILE CYS ASN ASP VAL LEU SER LEU LEU GLU LYS PHE          
SEQRES   9 A  245  LEU ILE PRO ASN ALA SER GLN ALA GLU SER LYS VAL PHE          
SEQRES  10 A  245  TYR LEU LYS MET LYS GLY ASP TYR TYR ARG TYR LEU ALA          
SEQRES  11 A  245  GLU VAL ALA ALA GLY ASP ASP LYS LYS GLY ILE VAL ASP          
SEQRES  12 A  245  GLN SER GLN GLN ALA TYR GLN GLU ALA PHE GLU ILE SER          
SEQRES  13 A  245  LYS LYS GLU MET GLN PRO THR HIS PRO ILE ARG LEU GLY          
SEQRES  14 A  245  LEU ALA LEU ASN PHE SER VAL PHE TYR TYR GLU ILE LEU          
SEQRES  15 A  245  ASN SER PRO GLU LYS ALA CYS SER LEU ALA LYS THR ALA          
SEQRES  16 A  245  PHE ASP GLU ALA ILE ALA GLU LEU ASP THR LEU SER GLU          
SEQRES  17 A  245  GLU SER TYR LYS ASP SER THR LEU ILE MET GLN LEU LEU          
SEQRES  18 A  245  ARG ASP ASN LEU THR LEU TRP THR SER ASP THR GLN GLY          
SEQRES  19 A  245  ASP GLU ALA GLU ALA GLY GLU GLY GLY GLU ASN                  
SEQRES   1 B  245  MET ASP LYS ASN GLU LEU VAL GLN LYS ALA LYS LEU ALA          
SEQRES   2 B  245  GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA CYS MET          
SEQRES   3 B  245  LYS SER VAL THR GLU GLN GLY ALA GLU LEU SER ASN GLU          
SEQRES   4 B  245  GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL          
SEQRES   5 B  245  GLY ALA ARG ARG SER SER TRP ARG VAL VAL SER SER ILE          
SEQRES   6 B  245  GLU GLN LYS THR GLU GLY ALA GLU LYS LYS GLN GLN MET          
SEQRES   7 B  245  ALA ARG GLU TYR ARG GLU LYS ILE GLU THR GLU LEU ARG          
SEQRES   8 B  245  ASP ILE CYS ASN ASP VAL LEU SER LEU LEU GLU LYS PHE          
SEQRES   9 B  245  LEU ILE PRO ASN ALA SER GLN ALA GLU SER LYS VAL PHE          
SEQRES  10 B  245  TYR LEU LYS MET LYS GLY ASP TYR TYR ARG TYR LEU ALA          
SEQRES  11 B  245  GLU VAL ALA ALA GLY ASP ASP LYS LYS GLY ILE VAL ASP          
SEQRES  12 B  245  GLN SER GLN GLN ALA TYR GLN GLU ALA PHE GLU ILE SER          
SEQRES  13 B  245  LYS LYS GLU MET GLN PRO THR HIS PRO ILE ARG LEU GLY          
SEQRES  14 B  245  LEU ALA LEU ASN PHE SER VAL PHE TYR TYR GLU ILE LEU          
SEQRES  15 B  245  ASN SER PRO GLU LYS ALA CYS SER LEU ALA LYS THR ALA          
SEQRES  16 B  245  PHE ASP GLU ALA ILE ALA GLU LEU ASP THR LEU SER GLU          
SEQRES  17 B  245  GLU SER TYR LYS ASP SER THR LEU ILE MET GLN LEU LEU          
SEQRES  18 B  245  ARG ASP ASN LEU THR LEU TRP THR SER ASP THR GLN GLY          
SEQRES  19 B  245  ASP GLU ALA GLU ALA GLY GLU GLY GLY GLU ASN                  
SEQRES   1 P   10  GLN ARG SER THR SEP THR PRO ASN VAL HIS                      
SEQRES   1 Q   10  GLN ARG SER THR SEP THR PRO ASN VAL HIS                      
MODRES 3NKX SEP P  259  SER  PHOSPHOSERINE                                      
MODRES 3NKX SEP Q  259  SER  PHOSPHOSERINE                                      
HET    SEP  P 259      10                                                       
HET    SEP  Q 259      10                                                       
HET    PPI  A 247       5                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     PPI PROPANOIC ACID                                                   
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   3  SEP    2(C3 H8 N O6 P)                                              
FORMUL   5  PPI    C3 H6 O2                                                     
FORMUL   6  HOH   *183(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  THR A   69  1                                  33    
HELIX    4   4 ALA A   72  PHE A  104  1                                  33    
HELIX    5   5 GLN A  111  VAL A  132  1                                  22    
HELIX    6   6 GLY A  135  MET A  160  1                                  26    
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  210  THR A  229  1                                  20    
HELIX   11  11 ASP B    2  ALA B   16  1                                  15    
HELIX   12  12 ARG B   18  GLU B   31  1                                  14    
HELIX   13  13 SER B   37  GLN B   67  1                                  31    
HELIX   14  14 GLU B   73  PHE B  104  1                                  32    
HELIX   15  15 PHE B  104  ALA B  109  1                                   6    
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 SER B  210  THR B  229  1                                  20    
LINK         C   THR P 258                 N   SEP P 259     1555   1555  1.33  
LINK         C   SEP P 259                 N   THR P 260     1555   1555  1.31  
LINK         C   THR Q 258                 N   SEP Q 259     1555   1555  1.33  
LINK         C   SEP Q 259                 N   THR Q 260     1555   1555  1.33  
CISPEP   1 GLY A   71    ALA A   72          0        -5.52                     
CISPEP   2 VAL P  263    HIS P  264          0       -20.69                     
SITE     1 AC1  4 GLN A 219  ARG A 222  GLN B 219  ARG B 222                    
CRYST1   72.410   83.850  111.670  90.00  90.00  90.00 P 21 21 21    8          
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      0.013810  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011926  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008955        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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