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Database: PDB
Entry: 3ZUV
LinkDB: 3ZUV
Original site: 3ZUV 
HEADER    DE NOVO PROTEIN/TRANSFERASE             20-JUL-11   3ZUV              
TITLE     CRYSTAL STRUCTURE OF A DESIGNED SELECTED ANKYRIN REPEAT               
TITLE    2 PROTEIN IN COMPLEX WITH THE PHOSPHORYLATED MAP KINASE ERK2           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;                        
COMPND   3 CHAIN: A, C;                                                         
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,                  
COMPND   7  MITOGEN-ACTIVATED 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, D;                                                         
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: PETHIS6/MEK1R4F_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_PE59                               
KEYWDS    DE NOVO PROTEIN-TRANSFERASE COMPLEX, ANKYRIN REPEAT PROTEIN,          
KEYWDS   2 SELECTED BINDER, PROTEIN DESIGN                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.KUMMER,P.R.MITTL,A.PLUCKTHUN                                        
REVDAT   2   05-SEP-12 3ZUV    1       JRNL                                     
REVDAT   1   27-JUN-12 3ZUV    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 PHOSPHORYLATION-       
JRNL        TITL 2 SPECIFIC BINDERS OF THE KINASE ERK FROM DESIGNED ANKYRIN     
JRNL        TITL 3 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.    2.72 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) : 2.72                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 77.12                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.00                         
REMARK   3   NUMBER OF REFLECTIONS             : 45852                          
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) : 0.17837                         
REMARK   3   R VALUE            (WORKING SET) : 0.17572                         
REMARK   3   FREE R VALUE                     : 0.22975                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2413                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.717                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.788                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2979                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.263                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 157                          
REMARK   3   BIN FREE R VALUE                    : 0.352                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7790                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 203                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 0                              
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.145                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00                                                 
REMARK   3    B22 (A**2) : 0.03                                                 
REMARK   3    B33 (A**2) : -0.03                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.369         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.265         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.193         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.148        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7969 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10822 ; 1.939 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   980 ; 6.624 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   391 ;39.368 ;24.629       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1393 ;20.100 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;23.284 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1195 ; 0.128 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6078 ; 0.008 ; 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):  4862 ; 0.796 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7844 ; 1.592 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3107 ; 2.705 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2978 ; 4.458 ; 4.500       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
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     0        A   358                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.0750 -20.3303  -9.2115              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0071 T22:   0.0481                                     
REMARK   3      T33:   0.0504 T12:  -0.0080                                     
REMARK   3      T13:  -0.0159 T23:   0.0056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1361 L22:   1.4441                                     
REMARK   3      L33:   1.6035 L12:   0.2458                                     
REMARK   3      L13:   0.1262 L23:  -0.3946                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0392 S12:  -0.2197 S13:  -0.0679                       
REMARK   3      S21:  -0.0743 S22:  -0.0549 S23:   0.2151                       
REMARK   3      S31:   0.0489 S32:  -0.1107 S33:   0.0157                       
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   134                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.2429 -42.3081  -8.1964              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0741 T22:   0.0701                                     
REMARK   3      T33:   0.2991 T12:   0.0224                                     
REMARK   3      T13:   0.0099 T23:   0.0725                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5998 L22:   1.5318                                     
REMARK   3      L33:   4.3771 L12:  -0.3436                                     
REMARK   3      L13:   0.8260 L23:   0.9814                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1849 S12:   0.2049 S13:  -0.1332                       
REMARK   3      S21:   0.0468 S22:   0.1513 S23:  -0.2553                       
REMARK   3      S31:   0.4086 S32:   0.3523 S33:   0.0336                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     0        C   358                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.4225 -11.1680  15.6214              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1077 T22:   0.0333                                     
REMARK   3      T33:   0.1163 T12:  -0.0135                                     
REMARK   3      T13:   0.0262 T23:  -0.0453                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9036 L22:   1.0547                                     
REMARK   3      L33:   1.8838 L12:  -0.4035                                     
REMARK   3      L13:   0.1163 L23:   0.0096                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1182 S12:   0.0776 S13:  -0.3107                       
REMARK   3      S21:   0.1896 S22:   0.0781 S23:  -0.1365                       
REMARK   3      S31:   0.0948 S32:   0.1244 S33:   0.0400                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    12        D   133                          
REMARK   3    ORIGIN FOR THE GROUP (A):  72.3274   6.4193  17.0940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2037 T22:   0.2269                                     
REMARK   3      T33:   0.6478 T12:  -0.1698                                     
REMARK   3      T13:   0.0823 T23:  -0.0844                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5943 L22:   6.2888                                     
REMARK   3      L33:   4.8608 L12:  -0.7347                                     
REMARK   3      L13:  -0.8955 L23:   0.1019                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1021 S12:   0.3112 S13:   0.9895                       
REMARK   3      S21:  -0.0837 S22:   0.2028 S23:  -0.6572                       
REMARK   3      S31:  -0.6910 S32:   0.4437 S33:  -0.3048                       
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          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 3ZUV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-JUL-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-49012.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-MAY-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0015                             
REMARK 200  MONOCHROMATOR                  : BARTELS MONOCHROMATOR              
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (MAR225)                       
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 84304                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.72                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 8.12                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.8                               
REMARK 200  DATA REDUNDANCY                : 2.2                                
REMARK 200  R MERGE                    (I) : 0.05                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.43                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.72                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.2                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.41                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.41                               
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 2ERK, 1MJ0                               
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HOAC (PH 7.5), 2 M           
REMARK 280  SODIUM FORMATE                                                      
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       56.83500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.48500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       75.22450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.48500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       56.83500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       75.22450            
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                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.1 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     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     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     LEU B   135                                                      
REMARK 465     ASN B   136                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     HIS C    -2                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ARG D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     HIS D     5                                                      
REMARK 465     HIS D     6                                                      
REMARK 465     HIS D     7                                                      
REMARK 465     HIS D     8                                                      
REMARK 465     HIS D     9                                                      
REMARK 465     HIS D    10                                                      
REMARK 465     GLY D    11                                                      
REMARK 465     LYS D   134                                                      
REMARK 465     LEU D   135                                                      
REMARK 465     ASN D   136                                                      
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   OE2  GLU A   107     CG2  THR A   157              2.05            
REMARK 500   OD1  ASN A   269     O    HOH A  2094              2.20            
REMARK 500   O    HOH A  2036     O    HOH A  2038              2.12            
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 303   CB    GLU A 303   CG      0.135                       
REMARK 500    GLU A 303   CG    GLU A 303   CD      0.097                       
REMARK 500    GLU A 347   CG    GLU A 347   CD      0.120                       
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  22   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A 192   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 192   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ARG A 357   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG A 357   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    LEU B  57   CA  -  CB  -  CG  ANGL. DEV. = -17.2 DEGREES          
REMARK 500    ARG B  90   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    LEU C  26   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    CYS C  38   CB  -  CA  -  C   ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ARG C 351   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG C 357   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 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    MET A   2       93.44    -49.01                                   
REMARK 500    ALA A   3       74.82    -64.71                                   
REMARK 500    ALA A   7     -131.09     47.39                                   
REMARK 500    ASP A 147       39.10   -157.43                                   
REMARK 500    ASP A 165       79.28     47.31                                   
REMARK 500    ALA A 187      153.30     66.75                                   
REMARK 500    LEU A 198      -57.33   -125.99                                   
REMARK 500    LEU A 292       57.69   -100.67                                   
REMARK 500    LEU A 333       59.48    -90.62                                   
REMARK 500    ALA B  42      131.29    -37.83                                   
REMARK 500    GLU B  45       -9.05    -53.95                                   
REMARK 500    ASN B  78        3.77    -59.77                                   
REMARK 500    ALA C   4     -146.02   -117.46                                   
REMARK 500    ASP C 147       42.35   -158.42                                   
REMARK 500    CYS C 159       -1.21     89.74                                   
REMARK 500    ASP C 165       75.95     55.02                                   
REMARK 500    ALA C 187      113.14     66.94                                   
REMARK 500    THR C 188      138.15    -36.38                                   
REMARK 500    LEU C 198      -61.64    -97.26                                   
REMARK 500    SER C 221       -1.93   -141.94                                   
REMARK 500    LEU C 292       40.11    -91.42                                   
REMARK 500    PRO C 309      -37.90    -35.39                                   
REMARK 500    ASP C 316       90.02   -164.96                                   
REMARK 500    MET D  34      -70.72    -63.29                                   
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    8     PRO A    9                  135.96                    
REMARK 500 VAL A   19     GLY A   20                  149.40                    
REMARK 500 ILE C  253     ILE C  254                 -146.91                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLU A 347        23.8      L          L   OUTSIDE RANGE           
REMARK 500    ALA C   5        23.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1359                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1359                 
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: 3ZU7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF A DESIGNED SELECTED ANKYRIN REPEAT             
REMARK 900   PROTEIN IN COMPLEX WITH THE MAP KINASE ERK2                        
REMARK 900 RELATED ID: 1GOL   RELATED DB: PDB                                   
REMARK 900  COORDINATES OF RAT MAP KINASE ERK2 WITH AN ARGININE                 
REMARK 900  MUTATION AT POSITION 52                                             
REMARK 900 RELATED ID: 4ERK   RELATED DB: PDB                                   
REMARK 900  THE COMPLEX STRUCTURE OF THE MAP KINASE ERK2/                       
REMARK 900  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                                      
DBREF  3ZUV A    3   358  UNP    P63086   MK01_RAT         3    358             
DBREF  3ZUV B    1   136  PDB    3ZUV     3ZUV             1    136             
DBREF  3ZUV C    3   358  UNP    P63086   MK01_RAT         3    358             
DBREF  3ZUV D    1   136  PDB    3ZUV     3ZUV             1    136             
SEQADV 3ZUV HIS A   -5  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZUV HIS A   -4  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZUV HIS A   -3  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZUV HIS A   -2  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZUV HIS A   -1  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZUV HIS A    0  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZUV ALA A    1  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZUV MET A    2  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZUV HIS C   -5  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZUV HIS C   -4  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZUV HIS C   -3  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZUV HIS C   -2  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZUV HIS C   -1  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZUV HIS C    0  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZUV ALA C    1  UNP  P63086              EXPRESSION TAG                 
SEQADV 3ZUV MET C    2  UNP  P63086              EXPRESSION TAG                 
SEQRES   1 A  364  HIS HIS HIS HIS HIS HIS ALA MET ALA ALA ALA ALA ALA          
SEQRES   2 A  364  GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL GLY          
SEQRES   3 A  364  PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY ALA          
SEQRES   4 A  364  TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN LYS          
SEQRES   5 A  364  VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU HIS          
SEQRES   6 A  364  GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS ILE          
SEQRES   7 A  364  LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN          
SEQRES   8 A  364  ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS ASP          
SEQRES   9 A  364  VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU TYR          
SEQRES  10 A  364  LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS ILE          
SEQRES  11 A  364  CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR          
SEQRES  12 A  364  ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  13 A  364  SER ASN LEU LEU LEU ASN THR THR CYS ASP LEU LYS ILE          
SEQRES  14 A  364  CYS ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP HIS          
SEQRES  15 A  364  ASP HIS THR GLY PHE LEU TPO GLU PTR VAL ALA THR ARG          
SEQRES  16 A  364  TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS GLY          
SEQRES  17 A  364  TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS ILE          
SEQRES  18 A  364  LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO GLY          
SEQRES  19 A  364  LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE          
SEQRES  20 A  364  LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE ILE          
SEQRES  21 A  364  ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO HIS          
SEQRES  22 A  364  LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA          
SEQRES  23 A  364  ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU THR          
SEQRES  24 A  364  PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU          
SEQRES  25 A  364  ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER ASP          
SEQRES  26 A  364  GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET GLU          
SEQRES  27 A  364  LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE          
SEQRES  28 A  364  PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR ARG SER          
SEQRES   1 B  136  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP          
SEQRES   2 B  136  LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN          
SEQRES   3 B  136  ASP ASP GLU VAL ARG ILE LEU MET ALA ASN GLY ALA ASP          
SEQRES   4 B  136  VAL ASN ALA LEU ASP GLU ASP GLY LEU THR PRO LEU HIS          
SEQRES   5 B  136  LEU ALA ALA GLN LEU GLY HIS LEU GLU ILE VAL GLU VAL          
SEQRES   6 B  136  LEU LEU LYS TYR GLY ALA ASP VAL ASN ALA GLU ASP ASN          
SEQRES   7 B  136  PHE GLY ILE THR PRO LEU HIS LEU ALA ALA ILE ARG GLY          
SEQRES   8 B  136  HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS HIS GLY ALA          
SEQRES   9 B  136  ASP VAL ASN ALA GLN ASP LYS PHE GLY LYS THR ALA PHE          
SEQRES  10 B  136  ASP ILE SER ILE ASP ASN GLY ASN GLU ASP LEU ALA GLU          
SEQRES  11 B  136  ILE LEU GLN LYS LEU ASN                                      
SEQRES   1 C  364  HIS HIS HIS HIS HIS HIS ALA MET ALA ALA ALA ALA ALA          
SEQRES   2 C  364  GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL GLY          
SEQRES   3 C  364  PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY ALA          
SEQRES   4 C  364  TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN LYS          
SEQRES   5 C  364  VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU HIS          
SEQRES   6 C  364  GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS ILE          
SEQRES   7 C  364  LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN          
SEQRES   8 C  364  ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS ASP          
SEQRES   9 C  364  VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU TYR          
SEQRES  10 C  364  LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS ILE          
SEQRES  11 C  364  CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR          
SEQRES  12 C  364  ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  13 C  364  SER ASN LEU LEU LEU ASN THR THR CYS ASP LEU LYS ILE          
SEQRES  14 C  364  CYS ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP HIS          
SEQRES  15 C  364  ASP HIS THR GLY PHE LEU TPO GLU PTR VAL ALA THR ARG          
SEQRES  16 C  364  TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS GLY          
SEQRES  17 C  364  TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS ILE          
SEQRES  18 C  364  LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO GLY          
SEQRES  19 C  364  LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE          
SEQRES  20 C  364  LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE ILE          
SEQRES  21 C  364  ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO HIS          
SEQRES  22 C  364  LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA          
SEQRES  23 C  364  ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU THR          
SEQRES  24 C  364  PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU          
SEQRES  25 C  364  ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER ASP          
SEQRES  26 C  364  GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET GLU          
SEQRES  27 C  364  LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE          
SEQRES  28 C  364  PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR ARG SER          
SEQRES   1 D  136  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP          
SEQRES   2 D  136  LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN          
SEQRES   3 D  136  ASP ASP GLU VAL ARG ILE LEU MET ALA ASN GLY ALA ASP          
SEQRES   4 D  136  VAL ASN ALA LEU ASP GLU ASP GLY LEU THR PRO LEU HIS          
SEQRES   5 D  136  LEU ALA ALA GLN LEU GLY HIS LEU GLU ILE VAL GLU VAL          
SEQRES   6 D  136  LEU LEU LYS TYR GLY ALA ASP VAL ASN ALA GLU ASP ASN          
SEQRES   7 D  136  PHE GLY ILE THR PRO LEU HIS LEU ALA ALA ILE ARG GLY          
SEQRES   8 D  136  HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS HIS GLY ALA          
SEQRES   9 D  136  ASP VAL ASN ALA GLN ASP LYS PHE GLY LYS THR ALA PHE          
SEQRES  10 D  136  ASP ILE SER ILE ASP ASN GLY ASN GLU ASP LEU ALA GLU          
SEQRES  11 D  136  ILE LEU GLN LYS LEU ASN                                      
MODRES 3ZUV TPO A  183  THR  PHOSPHOTHREONINE                                   
MODRES 3ZUV TPO C  183  THR  PHOSPHOTHREONINE                                   
MODRES 3ZUV PTR A  185  TYR  O-PHOSPHOTYROSINE                                  
MODRES 3ZUV PTR C  185  TYR  O-PHOSPHOTYROSINE                                  
HET    TPO  A 183      11                                                       
HET    PTR  A 185      16                                                       
HET    TPO  C 183      11                                                       
HET    PTR  C 185      16                                                       
HET    SO4  A1359       5                                                       
HET    SO4  C1359       5                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     SO4 SULFATE ION                                                      
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   5  TPO    2(C4 H10 N O6 P)                                             
FORMUL   6  PTR    2(C9 H12 N O6 P)                                             
FORMUL   7  SO4    2(O4 S 2-)                                                   
FORMUL   8  HOH   *203(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 THR A  188  ARG A  192  5                                   5    
HELIX    6   6 ALA A  193  LEU A  198  5                                   6    
HELIX    7   7 LYS A  205  ASN A  222  1                                  18    
HELIX    8   8 HIS A  230  GLY A  243  1                                  14    
HELIX    9   9 SER A  246  ASN A  251  1                                   6    
HELIX   10  10 ASN A  255  SER A  264  1                                  10    
HELIX   11  11 PRO A  272  PHE A  277  1                                   6    
HELIX   12  12 ASP A  281  LEU A  292  1                                  12    
HELIX   13  13 ASN A  295  ARG A  299  5                                   5    
HELIX   14  14 GLU A  301  ALA A  307  1                                   7    
HELIX   15  15 HIS A  308  GLU A  312  5                                   5    
HELIX   16  16 ASP A  316  GLU A  320  5                                   5    
HELIX   17  17 LYS A  328  LEU A  333  5                                   6    
HELIX   18  18 PRO A  337  ALA A  350  1                                  14    
HELIX   19  19 ARG A  351  GLN A  353  5                                   3    
HELIX   20  20 ASP B   13  ALA B   24  1                                  12    
HELIX   21  21 GLN B   26  ASN B   36  1                                  11    
HELIX   22  22 THR B   49  GLY B   58  1                                  10    
HELIX   23  23 HIS B   59  TYR B   69  1                                  11    
HELIX   24  24 THR B   82  ARG B   90  1                                   9    
HELIX   25  25 HIS B   92  HIS B  102  1                                  11    
HELIX   26  26 THR B  115  ASN B  123  1                                   9    
HELIX   27  27 ASN B  125  LYS B  134  1                                  10    
HELIX   28  28 HIS C   59  PHE C   76  1                                  18    
HELIX   29  29 LEU C  110  GLN C  117  1                                   8    
HELIX   30  30 SER C  120  ALA C  141  1                                  22    
HELIX   31  31 LYS C  149  SER C  151  5                                   3    
HELIX   32  32 THR C  188  ARG C  192  5                                   5    
HELIX   33  33 ALA C  193  ASN C  199  1                                   7    
HELIX   34  34 SER C  206  ASN C  222  1                                  17    
HELIX   35  35 HIS C  230  GLY C  243  1                                  14    
HELIX   36  36 SER C  246  CYS C  252  1                                   7    
HELIX   37  37 ASN C  255  LEU C  265  1                                  11    
HELIX   38  38 PRO C  272  PHE C  277  1                                   6    
HELIX   39  39 ASP C  281  LEU C  292  1                                  12    
HELIX   40  40 GLU C  301  HIS C  308  1                                   8    
HELIX   41  41 PRO C  309  GLU C  312  5                                   4    
HELIX   42  42 ASP C  316  GLU C  320  5                                   5    
HELIX   43  43 LYS C  328  LEU C  333  5                                   6    
HELIX   44  44 PRO C  337  ALA C  350  1                                  14    
HELIX   45  45 ARG C  351  GLN C  353  5                                   3    
HELIX   46  46 ASP D   13  ALA D   24  1                                  12    
HELIX   47  47 GLN D   26  ASN D   36  1                                  11    
HELIX   48  48 THR D   49  LEU D   57  1                                   9    
HELIX   49  49 HIS D   59  LYS D   68  1                                  10    
HELIX   50  50 THR D   82  ARG D   90  1                                   9    
HELIX   51  51 HIS D   92  HIS D  102  1                                  11    
HELIX   52  52 THR D  115  GLY D  124  1                                  10    
HELIX   53  53 ASN D  125  GLN D  133  1                                   9    
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  GLU A  31  0                                        
SHEET    2  AB 5 MET A  36  ASP A  42 -1  O  VAL A  37   N  ILE A  29           
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  ILE A  88 -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           
SHEET    1  CA 5 TYR C  23  GLU C  31  0                                        
SHEET    2  CA 5 MET C  36  ASP C  42 -1  O  VAL C  37   N  ILE C  29           
SHEET    3  CA 5 VAL C  47  ILE C  54 -1  O  VAL C  47   N  ASP C  42           
SHEET    4  CA 5 VAL C  99  ASP C 104 -1  O  VAL C  99   N  ILE C  54           
SHEET    5  CA 5 ASP C  86  ARG C  89 -1  O  ASP C  86   N  VAL C 102           
SHEET    1  CB 3 THR C 108  ASP C 109  0                                        
SHEET    2  CB 3 LEU C 153  LEU C 155 -1  O  LEU C 155   N  THR C 108           
SHEET    3  CB 3 LEU C 161  ILE C 163 -1  O  LYS C 162   N  LEU C 154           
SHEET    1  CC 2 VAL C 143  LEU C 144  0                                        
SHEET    2  CC 2 ARG C 170  VAL C 171 -1  O  ARG C 170   N  LEU C 144           
LINK         C   LEU A 182                 N   TPO A 183     1555   1555  1.34  
LINK         C   TPO A 183                 N   GLU A 184     1555   1555  1.33  
LINK         C   GLU A 184                 N   PTR A 185     1555   1555  1.32  
LINK         C   PTR A 185                 N   VAL A 186     1555   1555  1.31  
LINK         C   LEU C 182                 N   TPO C 183     1555   1555  1.32  
LINK         C   TPO C 183                 N   GLU C 184     1555   1555  1.32  
LINK         C   GLU C 184                 N   PTR C 185     1555   1555  1.33  
LINK         C   PTR C 185                 N   VAL C 186     1555   1555  1.33  
SITE     1 AC1  3 TYR A  41  ARG A  48  HOH A2119                               
SITE     1 AC2  4 ASN C  25  TYR C  41  ARG C  48  HOH C2069                    
CRYST1  113.670  150.449  104.970  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008797  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006647  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009527        0.00000                         
MTRIX1   1  0.036430  0.998300  0.046520       25.69180    1                    
MTRIX2   1 -0.998200  0.034130  0.049360       28.67220    1                    
MTRIX3   1  0.047690 -0.004824  0.997700      -27.84800    1                    
MTRIX1   2  0.058120  0.996900  0.052660       23.90080    1                    
MTRIX2   2 -0.997000  0.055210  0.055100       28.58930    1                    
MTRIX3   2  0.052030 -0.055700  0.997100      -28.45000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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