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Database: PDB
Entry: 3ZU7
LinkDB: 3ZU7
Original site: 3ZU7 
HEADER    TRANSFERASE/DE NOVO PROTEIN             16-JUL-11   3ZU7              
TITLE     CRYSTAL STRUCTURE OF A DESIGNED SELECTED ANKYRIN REPEAT PROTEIN IN    
TITLE    2 COMPLEX WITH THE MAP KINASE ERK2                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 3-358;                                            
COMPND   5 SYNONYM: MAP KINASE 1, MAPK 1, ERT1, EXTRACELLULAR SIGNAL-REGULATED  
COMPND   6 KINASE 2, ERK-2, MAP KINASE ISOFORM P42, P42-MAPK, MITOGEN-ACTIVATED 
COMPND   7 PROTEIN KINASE 2, MAP KINASE 2, MAPK 2;                              
COMPND   8 EC: 2.7.11.24;                                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: DESIGNED ANKYRIN REPEAT PROTEIN;                           
COMPND  12 CHAIN: B;                                                            
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: NPT75-ERK2;                               
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  12 ORGANISM_TAXID: 32630;                                               
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: K-12;                                      
SOURCE  16 EXPRESSION_SYSTEM_VARIANT: XL1-BLUE;                                 
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PDST67_E40                                
KEYWDS    TRANSFERASE-DE NOVO PROTEIN COMPLEX, TRANSFERASE, SELECTED BINDER,    
KEYWDS   2 PROTEIN DESIGN                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.KUMMER,P.R.MITTL,A.PLUCKTHUN                                        
REVDAT   4   05-JUL-17 3ZU7    1       REMARK                                   
REVDAT   3   10-OCT-12 3ZU7    1       JRNL                                     
REVDAT   2   05-SEP-12 3ZU7    1                                                
REVDAT   1   27-JUN-12 3ZU7    0                                                
JRNL        AUTH   L.KUMMER,P.PARIZEK,P.RUBE,B.MILLGRAMM,A.PRINZ,P.R.MITTL,     
JRNL        AUTH 2 M.KAUFHOLZ,B.ZIMMERMANN,F.W.HERBERG,A.PLUCKTHUN              
JRNL        TITL   STRUCTURAL AND FUNCTIONAL ANALYSIS OF                        
JRNL        TITL 2 PHOSPHORYLATION-SPECIFIC BINDERS OF THE KINASE ERK FROM      
JRNL        TITL 3 DESIGNED ANKYRIN REPEAT PROTEIN LIBRARIES.                   
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109 E2248 2012              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   22843676                                                     
JRNL        DOI    10.1073/PNAS.1205399109                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.97 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 1.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.43                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 38887                          
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) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2040                            
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) : 1.97                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2965                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.90                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2650                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 148                          
REMARK   3   BIN FREE R VALUE                    : 0.3610                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3984                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 236                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 0.00                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.02000                                              
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): 0.196         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.182         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.130         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.110        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.894                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4071 ; 0.023 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5522 ; 1.957 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   496 ; 6.634 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   201 ;39.413 ;24.726       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   710 ;18.549 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;17.354 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   615 ; 0.164 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3097 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2482 ; 1.159 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4001 ; 1.922 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1589 ; 2.882 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1521 ; 4.327 ; 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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    10        A   353                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.0921   4.9240   5.5126              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0271 T22:   0.0147                                     
REMARK   3      T33:   0.0456 T12:   0.0090                                     
REMARK   3      T13:   0.0278 T23:   0.0199                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5190 L22:   0.4728                                     
REMARK   3      L33:   0.9507 L12:   0.0831                                     
REMARK   3      L13:   0.0896 L23:   0.2409                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0623 S12:  -0.0647 S13:  -0.0992                       
REMARK   3      S21:   0.0575 S22:  -0.0149 S23:  -0.0091                       
REMARK   3      S31:   0.0998 S32:  -0.0349 S33:   0.0773                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    13        B   166                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.7783  -6.1663  14.2984              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0611 T22:   0.0268                                     
REMARK   3      T33:   0.0427 T12:   0.0200                                     
REMARK   3      T13:  -0.0148 T23:   0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9635 L22:   0.4504                                     
REMARK   3      L33:   2.5805 L12:   0.3227                                     
REMARK   3      L13:  -1.0922 L23:   0.3587                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0470 S12:   0.1263 S13:  -0.0971                       
REMARK   3      S21:  -0.0613 S22:  -0.0053 S23:  -0.0259                       
REMARK   3      S31:   0.0710 S32:  -0.0624 S33:  -0.0417                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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. RESIDUES A 175 - A 179 LIE IN A REGION OF WEAK           
REMARK   3  ELECTRON DENSITY                                                    
REMARK   4                                                                      
REMARK   4 3ZU7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-JUL-11.                  
REMARK 100 THE DEPOSITION ID IS D_1290048979.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JAN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
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                         : ELECTRON OPTICS                    
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   : 42412                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.870                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 5.410                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.9                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.2100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 44.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.16000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.300                              
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 ENTRIES 1ERK, 1MJ0                               
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HOAC (PH 8.5), 20% PEG4K,    
REMARK 280  5 MM CDCL2                                                          
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       34.02000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.77000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.68500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.77000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.02000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.68500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.6 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     MET A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     PRO A     9                                                      
REMARK 465     PRO A   354                                                      
REMARK 465     GLY A   355                                                      
REMARK 465     TYR A   356                                                      
REMARK 465     ARG A   357                                                      
REMARK 465     SER A   358                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     HIS B     9                                                      
REMARK 465     HIS B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     LYS B   167                                                      
REMARK 465     LEU B   168                                                      
REMARK 465     ASN B   169                                                      
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   NZ   LYS A   229     OD2  ASP B    79              2.03            
REMARK 500   OD2  ASP A   289     O    HOH A  2161              2.17            
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    PRO A  21   C   -  N   -  CA  ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    LEU A 144   CA  -  CB  -  CG  ANGL. DEV. =  14.4 DEGREES          
REMARK 500    LEU A 148   CB  -  CG  -  CD1 ANGL. DEV. =  13.4 DEGREES          
REMARK 500    ARG A 299   NE  -  CZ  -  NH1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG A 299   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ASP B  77   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP B  77   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP B 110   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    LEU B 114   CA  -  CB  -  CG  ANGL. DEV. =  15.2 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    PHE A  17       85.59   -155.77                                   
REMARK 500    ILE A  29       54.33   -143.63                                   
REMARK 500    THR A 108     -157.73   -153.39                                   
REMARK 500    ARG A 146       -7.81     72.88                                   
REMARK 500    ASN A 156     -158.96    -95.50                                   
REMARK 500    ASP A 165       80.99     90.39                                   
REMARK 500    HIS A 176     -168.10     73.11                                   
REMARK 500    ASP A 177       85.87    -35.74                                   
REMARK 500    THR A 179      150.68    -30.38                                   
REMARK 500    THR A 183       35.33    -93.86                                   
REMARK 500    GLU A 184       64.43   -114.97                                   
REMARK 500    LYS A 201      -97.72    -77.54                                   
REMARK 500    THR A 204     -168.07   -128.01                                   
REMARK 500    ASP A 316       86.48   -150.52                                   
REMARK 500    ASP A 330      129.80    -38.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A   35     MET A   36                  148.00                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ERK   RELATED DB: PDB                                   
REMARK 900 THE COMPLEX STRUCTURE OF THE MAP KINASE ERK2/SB220025                
REMARK 900 RELATED ID: 2GPH   RELATED DB: PDB                                   
REMARK 900 DOCKING MOTIF INTERACTIONS IN THE MAP KINASE ERK2                    
REMARK 900 RELATED ID: 1GOL   RELATED DB: PDB                                   
REMARK 900 COORDINATES OF RAT MAP KINASE ERK2 WITH AN ARGININE MUTATION AT      
REMARK 900 POSITION 52                                                          
REMARK 900 RELATED ID: 4ERK   RELATED DB: PDB                                   
REMARK 900 THE COMPLEX STRUCTURE OF THE MAP KINASE ERK2/ OLOMOUCINE             
REMARK 900 RELATED ID: 1ERK   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF SIGNAL-REGULATED KINASE                                 
REMARK 900 RELATED ID: 2ERK   RELATED DB: PDB                                   
REMARK 900 PHOSPHORYLATED MAP KINASE ERK2                                       
REMARK 900 RELATED ID: 3ZUV   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A DESIGNED SELECTED ANKYRIN REPEAT PROTEIN IN   
REMARK 900 COMPLEX WITH THE PHOSPHORYLATED MAP KINASE ERK2                      
DBREF  3ZU7 A    3   358  UNP    P63086   MK01_RAT         3    358             
DBREF  3ZU7 B    1   169  PDB    3ZU7     3ZU7             1    169             
SEQADV 3ZU7 ALA A   -6  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZU7 HIS A   -5  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZU7 HIS A   -4  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZU7 HIS A   -3  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZU7 HIS A   -2  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZU7 HIS A   -1  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZU7 HIS A    0  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZU7 ALA A    1  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZU7 MET A    2  UNP  P63086              EXPRESSION TAG                 
SEQRES   1 A  365  ALA HIS HIS HIS HIS HIS HIS ALA MET ALA ALA ALA ALA          
SEQRES   2 A  365  ALA GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL          
SEQRES   3 A  365  GLY PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY          
SEQRES   4 A  365  ALA TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN          
SEQRES   5 A  365  LYS VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU          
SEQRES   6 A  365  HIS GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS          
SEQRES   7 A  365  ILE LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE          
SEQRES   8 A  365  ASN ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS          
SEQRES   9 A  365  ASP VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU          
SEQRES  10 A  365  TYR LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS          
SEQRES  11 A  365  ILE CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS          
SEQRES  12 A  365  TYR ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS          
SEQRES  13 A  365  PRO SER ASN LEU LEU LEU ASN THR THR CYS ASP LEU LYS          
SEQRES  14 A  365  ILE CYS ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP          
SEQRES  15 A  365  HIS ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR          
SEQRES  16 A  365  ARG TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS          
SEQRES  17 A  365  GLY TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS          
SEQRES  18 A  365  ILE LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO          
SEQRES  19 A  365  GLY LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY          
SEQRES  20 A  365  ILE LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE          
SEQRES  21 A  365  ILE ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO          
SEQRES  22 A  365  HIS LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN          
SEQRES  23 A  365  ALA ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU          
SEQRES  24 A  365  THR PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA          
SEQRES  25 A  365  LEU ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER          
SEQRES  26 A  365  ASP GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET          
SEQRES  27 A  365  GLU LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU          
SEQRES  28 A  365  ILE PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR ARG          
SEQRES  29 A  365  SER                                                          
SEQRES   1 B  169  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP          
SEQRES   2 B  169  LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN          
SEQRES   3 B  169  ASP ASP GLU VAL ARG ILE LEU MET ALA ASN GLY ALA ASP          
SEQRES   4 B  169  VAL ASN ALA HIS ASP ASP GLN GLY SER THR PRO LEU HIS          
SEQRES   5 B  169  LEU ALA ALA TRP ILE GLY HIS PRO GLU ILE VAL GLU VAL          
SEQRES   6 B  169  LEU LEU LYS HIS GLY ALA ASP VAL ASN ALA ARG ASP THR          
SEQRES   7 B  169  ASP GLY TRP THR PRO LEU HIS LEU ALA ALA ASP ASN GLY          
SEQRES   8 B  169  HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS TYR GLY ALA          
SEQRES   9 B  169  ASP VAL ASN ALA GLN ASP ALA TYR GLY LEU THR PRO LEU          
SEQRES  10 B  169  HIS LEU ALA ALA ASP ARG GLY HIS LEU GLU ILE VAL GLU          
SEQRES  11 B  169  VAL LEU LEU LYS HIS GLY ALA ASP VAL ASN ALA GLN ASP          
SEQRES  12 B  169  LYS PHE GLY LYS THR ALA PHE ASP ILE SER ILE ASP ASN          
SEQRES  13 B  169  GLY ASN GLU ASP LEU ALA GLU ILE LEU GLN LYS LEU ASN          
FORMUL   3  HOH   *236(H2 O)                                                    
HELIX    1   1 HIS A   59  PHE A   76  1                                  18    
HELIX    2   2 LEU A  110  GLN A  117  1                                   8    
HELIX    3   3 SER A  120  ALA A  141  1                                  22    
HELIX    4   4 LYS A  149  SER A  151  5                                   3    
HELIX    5   5 ALA A  193  LEU A  198  1                                   6    
HELIX    6   6 LYS A  205  ASN A  222  1                                  18    
HELIX    7   7 HIS A  230  GLY A  243  1                                  14    
HELIX    8   8 SER A  246  CYS A  252  1                                   7    
HELIX    9   9 ASN A  255  SER A  264  1                                  10    
HELIX   10  10 PRO A  272  PHE A  277  1                                   6    
HELIX   11  11 ASP A  281  LEU A  292  1                                  12    
HELIX   12  12 GLU A  301  ALA A  307  1                                   7    
HELIX   13  13 HIS A  308  GLU A  312  5                                   5    
HELIX   14  14 ASP A  316  GLU A  320  5                                   5    
HELIX   15  15 PRO A  337  THR A  349  1                                  13    
HELIX   16  16 ALA A  350  GLN A  353  5                                   4    
HELIX   17  17 ASP B   13  GLY B   25  1                                  13    
HELIX   18  18 GLN B   26  ASN B   36  1                                  11    
HELIX   19  19 THR B   49  GLY B   58  1                                  10    
HELIX   20  20 HIS B   59  HIS B   69  1                                  11    
HELIX   21  21 THR B   82  GLY B   91  1                                  10    
HELIX   22  22 HIS B   92  TYR B  102  1                                  11    
HELIX   23  23 THR B  115  ARG B  123  1                                   9    
HELIX   24  24 HIS B  125  HIS B  135  1                                  11    
HELIX   25  25 THR B  148  GLY B  157  1                                  10    
HELIX   26  26 ASN B  158  LEU B  165  1                                   8    
SHEET    1  AA 2 MET A  11  VAL A  12  0                                        
SHEET    2  AA 2 GLN A  15  VAL A  16 -1  O  GLN A  15   N  VAL A  12           
SHEET    1  AB 5 TYR A  23  TYR A  28  0                                        
SHEET    2  AB 5 MET A  36  ASP A  42 -1  O  SER A  39   N  SER A  27           
SHEET    3  AB 5 VAL A  47  ILE A  54 -1  O  VAL A  47   N  ASP A  42           
SHEET    4  AB 5 VAL A  99  ASP A 104 -1  O  VAL A  99   N  ILE A  54           
SHEET    5  AB 5 ASP A  86  ARG A  89 -1  O  ASP A  86   N  VAL A 102           
SHEET    1  AC 3 THR A 108  ASP A 109  0                                        
SHEET    2  AC 3 LEU A 153  LEU A 155 -1  O  LEU A 155   N  THR A 108           
SHEET    3  AC 3 LEU A 161  ILE A 163 -1  O  LYS A 162   N  LEU A 154           
SHEET    1  AD 2 VAL A 143  LEU A 144  0                                        
SHEET    2  AD 2 ARG A 170  VAL A 171 -1  O  ARG A 170   N  LEU A 144           
CISPEP   1 THR A  179    GLY A  180          0         0.12                     
CRYST1   68.040   89.370   99.540  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014697  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011189  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010046        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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