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Database: PDB
Entry: 3P1R
LinkDB: 3P1R
Original site: 3P1R 
HEADER    PEPTIDE BINDING PROTEIN                 30-SEP-10   3P1R              
TITLE     CRYSTAL STRUCTURE OF HUMAN 14-3-3 SIGMA C38V/N166H IN COMPLEX WITH    
TITLE    2 TASK-3 PEPTIDE                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 14-3-3 PROTEIN SIGMA;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: STRATIFIN, EPITHELIAL CELL MARKER PROTEIN 1;                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 6-MER PEPTIDE FROM POTASSIUM CHANNEL SUBFAMILY K MEMBER 9; 
COMPND   9 CHAIN: P;                                                            
COMPND  10 SYNONYM: TASK-3 PEPTIDE;                                             
COMPND  11 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: SFN;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA DE3;                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPROEX HTB;                               
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.             
KEYWDS    HELICAL PROTEIN, PHOSPHOPROTEIN, ADAPTER PROTEIN, PEPTIDE BINDING     
KEYWDS   2 PROTEIN, NUCLEUS                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.ANDERS,Y.HIGUCHI,B.SCHUMACHER,P.THIEL,N.KATO,C.OTTMANN              
REVDAT   4   01-NOV-23 3P1R    1       REMARK SEQADV LINK                       
REVDAT   3   08-NOV-17 3P1R    1       REMARK                                   
REVDAT   2   07-JUN-17 3P1R    1       JRNL                                     
REVDAT   1   12-OCT-11 3P1R    0                                                
JRNL        AUTH   C.ANDERS,Y.HIGUCHI,K.KOSCHINSKY,M.BARTEL,B.SCHUMACHER,       
JRNL        AUTH 2 P.THIEL,H.NITTA,R.PREISIG-MULLER,G.SCHLICHTHORL,V.RENIGUNTA, 
JRNL        AUTH 3 J.OHKANDA,J.DAUT,N.KATO,C.OTTMANN                            
JRNL        TITL   A SEMISYNTHETIC FUSICOCCANE STABILIZES A PROTEIN-PROTEIN     
JRNL        TITL 2 INTERACTION AND ENHANCES THE EXPRESSION OF K+ CHANNELS AT    
JRNL        TITL 3 THE CELL SURFACE                                             
JRNL        REF    CHEM. BIOL.                   V.  20   583 2013              
JRNL        REFN                   ISSN 1879-1301                               
JRNL        PMID   23601647                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2013.03.015                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.58                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 30261                          
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) : 0.153                           
REMARK   3   R VALUE            (WORKING SET) : 0.151                           
REMARK   3   FREE R VALUE                     : 0.194                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1593                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2148                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1800                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 113                          
REMARK   3   BIN FREE R VALUE                    : 0.2330                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1907                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 9                                       
REMARK   3   SOLVENT ATOMS            : 366                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.49                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.48                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.17000                                              
REMARK   3    B22 (A**2) : -0.03000                                             
REMARK   3    B33 (A**2) : -0.14000                                             
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): 0.096         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.052         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.550         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2180 ; 0.028 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2993 ; 2.204 ; 1.992       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   309 ; 5.011 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   106 ;37.456 ;24.811       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   446 ;13.806 ;15.034       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;12.814 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   335 ; 0.175 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1666 ; 0.012 ; 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):  1320 ; 1.270 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2160 ; 2.028 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   860 ; 3.245 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   793 ; 5.211 ; 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 3P1R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-OCT-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000061848.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-MAY-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : BRUKER AXS MICROSTAR               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31854                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 3.950                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.91                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.370                              
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 3LW1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.095M HEPES NA-SALT, 25.6% PEG 400,     
REMARK 280  0.19M CACL2, 5% GLYCEROL, PH 7.4, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       31.34500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       31.34500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       41.16000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.14500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       41.16000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.14500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       31.34500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       41.16000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       56.14500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       31.34500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       41.16000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       56.14500            
REMARK 290   SMTRY3   8  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: 4100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A  67    CD   OE1  NE2                                       
REMARK 470     GLU A  72    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS A 214    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   O    HOH A   364     O    HOH A   365              2.03            
REMARK 500   O    HOH A   350     O    HOH A   469              2.13            
REMARK 500   NZ   LYS A   195     O    HOH A   322              2.15            
REMARK 500   OD1  ASP A   138     O    HOH A   288              2.16            
REMARK 500   O    HOH A   350     O    HOH A   543              2.17            
REMARK 500   O    HOH A   306     O    HOH A   353              2.18            
REMARK 500   CB   ASN A    50     O    HOH A   598              2.19            
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   OD2  ASP A   145     O    HOH A   467     6545     1.72            
REMARK 500   NE2  GLN A     8     O    HOH A   302     6544     1.73            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 182   CB    GLU A 182   CG     -0.139                       
REMARK 500    ARG P 370   CG    ARG P 370   CD      0.191                       
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   3   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A  85   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP A 104   CB  -  CG  -  OD1 ANGL. DEV. =  15.1 DEGREES          
REMARK 500    ASP A 104   CB  -  CG  -  OD2 ANGL. DEV. = -10.9 DEGREES          
REMARK 500    ASP A 139   CB  -  CG  -  OD1 ANGL. DEV. =  12.2 DEGREES          
REMARK 500    ASP A 139   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG A 148   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG A 148   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ASP A 204   CB  -  CG  -  OD2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG P 370   CG  -  CD  -  NE  ANGL. DEV. = -14.1 DEGREES          
REMARK 500    ARG P 370   CD  -  NE  -  CZ  ANGL. DEV. =  13.0 DEGREES          
REMARK 500    ARG P 370   NE  -  CZ  -  NH1 ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ARG P 370   NE  -  CZ  -  NH2 ANGL. DEV. = -10.8 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    ARG A  18       75.66   -108.86                                   
REMARK 500    HIS A 106       39.84   -144.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG P 370         0.09    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 250  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A   2   OE1                                                    
REMARK 620 2 HOH A 283   O    81.9                                              
REMARK 620 3 HOH A 364   O    89.1  62.0                                        
REMARK 620 4 HOH A 365   O    88.1 110.3  49.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 257  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A   8   OE1                                                    
REMARK 620 2 HOH A 538   O    97.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 249  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  75   OE1                                                    
REMARK 620 2 HOH A 309   O    73.8                                              
REMARK 620 3 HOH A 536   O   121.2  69.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 256  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 188   OE2                                                    
REMARK 620 2 HOH A 483   O    72.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 251  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 215   O                                                      
REMARK 620 2 HOH A 300   O   111.3                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 249                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 250                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 251                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 252                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 253                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 254                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 255                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 256                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 257                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2O98   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE 14-3-3 / H+-ATPASE PLANT COMPLEX                    
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: 3IQU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN 14-3-3 SIGMA IN COMPLEX WITH RAF1         
REMARK 900 PEPTIDE (6MER)                                                       
REMARK 900 RELATED ID: 3P1N   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P1O   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P1P   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P1Q   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P1S   RELATED DB: PDB                                   
DBREF  3P1R A    1   231  UNP    P31947   1433S_HUMAN      1    231             
DBREF  3P1R P  369   374  UNP    Q9NPC2   KCNK9_HUMAN    369    374             
SEQADV 3P1R GLY A   -4  UNP  P31947              EXPRESSION TAG                 
SEQADV 3P1R ALA A   -3  UNP  P31947              EXPRESSION TAG                 
SEQADV 3P1R MET A   -2  UNP  P31947              EXPRESSION TAG                 
SEQADV 3P1R GLY A   -1  UNP  P31947              EXPRESSION TAG                 
SEQADV 3P1R SER A    0  UNP  P31947              EXPRESSION TAG                 
SEQADV 3P1R VAL A   38  UNP  P31947    CYS    38 ENGINEERED MUTATION            
SEQADV 3P1R HIS A  166  UNP  P31947    ASN   166 ENGINEERED MUTATION            
SEQRES   1 A  236  GLY ALA MET GLY SER MET GLU ARG ALA SER LEU ILE GLN          
SEQRES   2 A  236  LYS ALA LYS LEU ALA GLU GLN ALA GLU ARG TYR GLU ASP          
SEQRES   3 A  236  MET ALA ALA PHE MET LYS GLY ALA VAL GLU LYS GLY GLU          
SEQRES   4 A  236  GLU LEU SER VAL GLU GLU ARG ASN LEU LEU SER VAL ALA          
SEQRES   5 A  236  TYR LYS ASN VAL VAL GLY GLY GLN ARG ALA ALA TRP ARG          
SEQRES   6 A  236  VAL LEU SER SER ILE GLU GLN LYS SER ASN GLU GLU GLY          
SEQRES   7 A  236  SER GLU GLU LYS GLY PRO GLU VAL ARG GLU TYR ARG GLU          
SEQRES   8 A  236  LYS VAL GLU THR GLU LEU GLN GLY VAL CYS ASP THR VAL          
SEQRES   9 A  236  LEU GLY LEU LEU ASP SER HIS LEU ILE LYS GLU ALA GLY          
SEQRES  10 A  236  ASP ALA GLU SER ARG VAL PHE TYR LEU LYS MET LYS GLY          
SEQRES  11 A  236  ASP TYR TYR ARG TYR LEU ALA GLU VAL ALA THR GLY ASP          
SEQRES  12 A  236  ASP LYS LYS ARG ILE ILE ASP SER ALA ARG SER ALA TYR          
SEQRES  13 A  236  GLN GLU ALA MET ASP ILE SER LYS LYS GLU MET PRO PRO          
SEQRES  14 A  236  THR HIS PRO ILE ARG LEU GLY LEU ALA LEU ASN PHE SER          
SEQRES  15 A  236  VAL PHE HIS TYR GLU ILE ALA ASN SER PRO GLU GLU ALA          
SEQRES  16 A  236  ILE SER LEU ALA LYS THR THR PHE ASP GLU ALA MET ALA          
SEQRES  17 A  236  ASP LEU HIS THR LEU SER GLU ASP SER TYR LYS ASP SER          
SEQRES  18 A  236  THR LEU ILE MET GLN LEU LEU ARG ASP ASN LEU THR LEU          
SEQRES  19 A  236  TRP THR                                                      
SEQRES   1 P    6  LYS ARG ARG LYS SEP VAL                                      
MODRES 3P1R SEP P  373  SER  PHOSPHOSERINE                                      
HET    SEP  P 373      10                                                       
HET     MG  A 249       1                                                       
HET     MG  A 250       1                                                       
HET     MG  A 251       1                                                       
HET     CL  A 252       1                                                       
HET     CL  A 253       1                                                       
HET     CL  A 254       1                                                       
HET     CL  A 255       1                                                       
HET     CA  A 256       1                                                       
HET     MG  A 257       1                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM      CA CALCIUM ION                                                      
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   2  SEP    C3 H8 N O6 P                                                 
FORMUL   3   MG    4(MG 2+)                                                     
FORMUL   6   CL    4(CL 1-)                                                     
FORMUL  10   CA    CA 2+                                                        
FORMUL  12  HOH   *366(H2 O)                                                    
HELIX    1   1 GLU A    2  ALA A   16  1                                  15    
HELIX    2   2 ARG A   18  LYS A   32  1                                  15    
HELIX    3   3 SER A   37  ASN A   70  1                                  34    
HELIX    4   4 PRO A   79  SER A  105  1                                  27    
HELIX    5   5 HIS A  106  ALA A  111  1                                   6    
HELIX    6   6 ASP A  113  ALA A  135  1                                  23    
HELIX    7   7 ASP A  139  MET A  162  1                                  24    
HELIX    8   8 HIS A  166  ILE A  183  1                                  18    
HELIX    9   9 SER A  186  ALA A  203  1                                  18    
HELIX   10  10 ASP A  204  LEU A  208  5                                   5    
HELIX   11  11 SER A  209  THR A  231  1                                  23    
LINK         C   LYS P 372                 N   SEP P 373     1555   1555  1.35  
LINK         C   SEP P 373                 N   VAL P 374     1555   1555  1.34  
LINK         OE1 GLU A   2                MG    MG A 250     1555   1555  2.31  
LINK         OE1BGLN A   8                MG    MG A 257     1555   1555  2.45  
LINK         OE1 GLU A  75                MG    MG A 249     1555   1555  2.26  
LINK         OE2 GLU A 188                CA    CA A 256     1555   1555  2.36  
LINK         O   ASP A 215                MG    MG A 251     1555   1555  2.84  
LINK        MG    MG A 249                 O   HOH A 309     1555   1555  2.54  
LINK        MG    MG A 249                 O   HOH A 536     1555   1555  2.38  
LINK        MG    MG A 250                 O   HOH A 283     1555   1555  2.57  
LINK        MG    MG A 250                 O   HOH A 364     1555   1555  2.19  
LINK        MG    MG A 250                 O   HOH A 365     1555   1555  2.61  
LINK        MG    MG A 251                 O   HOH A 300     1555   1555  2.71  
LINK        CA    CA A 256                 O   HOH A 483     1555   1555  2.32  
LINK        MG    MG A 257                 O   HOH A 538     1555   1555  2.41  
CISPEP   1 SER A  105    HIS A  106          0        10.62                     
SITE     1 AC1  5 GLU A  75  GLU A 161  HOH A 309  HOH A 498                    
SITE     2 AC1  5 HOH A 536                                                     
SITE     1 AC2  4 GLU A   2  HOH A 283  HOH A 364  HOH A 365                    
SITE     1 AC3  5 ASP A 215  LEU A 218  ILE A 219  HOH A 300                    
SITE     2 AC3  5 HOH A 496                                                     
SITE     1 AC4  4 LYS A   9  LYS A  87  HOH A 456  HOH A 478                    
SITE     1 AC5  4 LYS A 124  ALA A 150  GLU A 153  HOH A 409                    
SITE     1 AC6  4 TYR A  19  GLU A  20  HOH A 367  HOH A 499                    
SITE     1 AC7  4 THR A 228  THR A 231  HOH A 277  HOH A 291                    
SITE     1 AC8  6 GLU A  35  GLU A 110  GLU A 188  HOH A 444                    
SITE     2 AC8  6 HOH A 457  HOH A 483                                          
SITE     1 AC9  6 GLN A   8  LYS A  77  GLU A  80  HOH A 438                    
SITE     2 AC9  6 HOH A 538  HOH A 590                                          
CRYST1   82.320  112.290   62.690  90.00  90.00  90.00 C 2 2 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      0.012148  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008906  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015952        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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