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Database: PDB
Entry: 4IZA
LinkDB: 4IZA
Original site: 4IZA 
HEADER    TRANSFERASE                             29-JAN-13   4IZA              
TITLE     STRUCTURE OF DUALLY PHOSPHORYLATED ERK2 BOUND TO THE PEA-15 DEATH     
TITLE    2 EFFECTOR DOMAIN                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;                        
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES  8-360;                                       
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: ASTROCYTIC PHOSPHOPROTEIN PEA-15;                          
COMPND  12 CHAIN: B;                                                            
COMPND  13 FRAGMENT: UNP RESIDUES 1-96;                                         
COMPND  14 SYNONYM: 15 KDA PHOSPHOPROTEIN ENRICHED IN ASTROCYTES, PHOSPHOPROTEIN
COMPND  15 ENRICHED IN DIABETES, PED;                                           
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MAPK1, ERK2, PRKM1, PRKM2;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: PEA15;                                                         
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    MAP KINASE, DEATH EFFECTOR DOMAIN, TRANSFERASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.D.MACE,H.ROBINSON,S.J.RIEDL                                         
REVDAT   2   24-APR-13 4IZA    1       JRNL                                     
REVDAT   1   10-APR-13 4IZA    0                                                
JRNL        AUTH   P.D.MACE,Y.WALLEZ,M.F.EGGER,M.K.DOBACZEWSKA,H.ROBINSON,      
JRNL        AUTH 2 E.B.PASQUALE,S.J.RIEDL                                       
JRNL        TITL   STRUCTURE OF ERK2 BOUND TO PEA-15 REVEALS A MECHANISM FOR    
JRNL        TITL 2 RAPID RELEASE OF ACTIVATED MAPK.                             
JRNL        REF    NAT COMMUN                    V.   4  1681 2013              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   23575685                                                     
JRNL        DOI    10.1038/NCOMMS2687                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.93 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0107                                      
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) : 1.93                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.72                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 66545                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3515                            
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) : 1.93                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4726                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.51                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2480                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 255                          
REMARK   3   BIN FREE R VALUE                    : 0.2960                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6230                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 633                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.07000                                             
REMARK   3    B22 (A**2) : -0.03000                                             
REMARK   3    B33 (A**2) : 0.10000                                              
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): 0.163         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.154         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6430 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8735 ; 1.319 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   778 ; 5.513 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   304 ;39.069 ;24.145       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1106 ;14.025 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    38 ;21.463 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   973 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4868 ; 0.006 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4IZA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB077397.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66545                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.930                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.720                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 12.600                             
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM PHOSPHATE MONOBASIC      
REMARK 280  AND 20% W/V POLYETHYLENE GLYCOL 3,350, PH 5.0, VAPOR DIFFUSION,     
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.87900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      102.01200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.87900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      102.01200            
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: 1170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     ARG A   359                                                      
REMARK 465     SER A   360                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     PRO C     6                                                      
REMARK 465     GLY C     7                                                      
REMARK 465     GLY C     8                                                      
REMARK 465     ALA C     9                                                      
REMARK 465     GLY C    10                                                      
REMARK 465     ASP C   177                                                      
REMARK 465     HIS C   178                                                      
REMARK 465     ASP C   179                                                      
REMARK 465     HIS C   180                                                      
REMARK 465     THR C   181                                                      
REMARK 465     GLY C   182                                                      
REMARK 465     PHE C   183                                                      
REMARK 465     LEU C   184                                                      
REMARK 465     TPO C   185                                                      
REMARK 465     GLU C   186                                                      
REMARK 465     PTR C   187                                                      
REMARK 465     VAL C   188                                                      
REMARK 465     ALA C   189                                                      
REMARK 465     ARG C   359                                                      
REMARK 465     SER C   360                                                      
REMARK 465     LEU B    95                                                      
REMARK 465     ASP B    96                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  77    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  79    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A  99    CD   CE   NZ                                        
REMARK 470     LYS A 117    CD   CE   NZ                                        
REMARK 470     LYS A 203    CE   NZ                                             
REMARK 470     LYS A 231    CE   NZ                                             
REMARK 470     GLU A 326    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 330    CG   CD   CE   NZ                                   
REMARK 470     ASP A 337    CG   OD1  OD2                                       
REMARK 470     LYS C  54    CG   CD   CE   NZ                                   
REMARK 470     GLU C  60    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  67    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS C  73    CG   CD   CE   NZ                                   
REMARK 470     ARG C  77    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU C  96    CG   CD   OE1  OE2                                  
REMARK 470     GLN C  97    CG   CD   OE1  NE2                                  
REMARK 470     LYS C  99    CG   CD   CE   NZ                                   
REMARK 470     ARG C 172    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP C 175    CG   OD1  OD2                                       
REMARK 470     LYS C 203    CG   CD   CE   NZ                                   
REMARK 470     LYS C 231    CE   NZ                                             
REMARK 470     GLU C 250    CD   OE1  OE2                                       
REMARK 470     LYS C 259    CG   CD   CE   NZ                                   
REMARK 470     LYS C 270    CD   CE   NZ                                        
REMARK 470     GLU C 305    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 326    CD   OE1  OE2                                       
REMARK 470     LYS C 330    CD   CE   NZ                                        
REMARK 470     ASP C 332    CG   OD1  OD2                                       
REMARK 470     ASP C 337    CG   OD1  OD2                                       
REMARK 470     LYS C 342    CD   CE   NZ                                        
REMARK 470     GLU C 349    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  28    CG   CD   CE   NZ                                   
REMARK 470     GLU B  29    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  35    CG   CD   CE   NZ                                   
REMARK 470     GLU B  37    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  38    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  88    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD2  ASP A   177     O    HOH A   457     2655     2.11            
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    CYS B  27   CB    CYS B  27   SG     -0.098                       
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    ASP A 251   CB  -  CG  -  OD1 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ASP A 251   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG C 301   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG C 301   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    TYR A  36       10.49     56.77                                   
REMARK 500    ARG A 148       -1.94     77.26                                   
REMARK 500    ASP A 149       36.26   -143.12                                   
REMARK 500    ASN A 158     -155.32    -98.70                                   
REMARK 500    ASP A 167       73.87     68.35                                   
REMARK 500    ASP A 175       82.87   -156.34                                   
REMARK 500    ASN A 257       97.45    -56.41                                   
REMARK 500    LEU A 294       50.80    -99.85                                   
REMARK 500    ASP A 318       80.13   -160.83                                   
REMARK 500    ARG C 148       -9.06     80.03                                   
REMARK 500    ASP C 149       40.94   -140.08                                   
REMARK 500    ASP C 167       75.04     69.86                                   
REMARK 500    ASP C 175       43.28   -161.77                                   
REMARK 500    SER C 223       -0.94   -145.98                                   
REMARK 500    ASN C 257      105.51   -170.22                                   
REMARK 500    LEU C 294       58.84   -105.21                                   
REMARK 500    ASP C 318       82.75   -156.93                                   
REMARK 500    ASP C 332       -3.62    -57.70                                   
REMARK 500    ARG C 353       -8.61    -59.21                                   
REMARK 500    GLU B  38       50.85   -100.20                                   
REMARK 500    ARG B  72       68.62   -119.88                                   
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    TYR A  36        24.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4IZ7   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF NON-PHOSPHORYLATED ERK2 BOUND TO THE PEA-15             
REMARK 900 DEATH EFFECTOR DOMAIN                                                
REMARK 900 RELATED ID: 4IZ5   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE COMPLEX BETWEEN ERK2 PHOSPHOMIMETIC MUTANT          
REMARK 900 AND PEA-15                                                           
DBREF  4IZA A    8   360  UNP    P28482   MK01_HUMAN       8    360             
DBREF  4IZA C    8   360  UNP    P28482   MK01_HUMAN       8    360             
DBREF  4IZA B    1    96  UNP    Q15121   PEA15_HUMAN      1     96             
SEQADV 4IZA GLY A    5  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZA PRO A    6  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZA GLY A    7  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZA GLY C    5  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZA PRO C    6  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZA GLY C    7  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZA GLY B    0  UNP  Q15121              EXPRESSION TAG                 
SEQRES   1 A  356  GLY PRO GLY GLY ALA GLY PRO GLU MET VAL ARG GLY GLN          
SEQRES   2 A  356  VAL PHE ASP VAL GLY PRO ARG TYR THR ASN LEU SER TYR          
SEQRES   3 A  356  ILE GLY GLU GLY ALA TYR GLY MET VAL CYS SER ALA TYR          
SEQRES   4 A  356  ASP ASN VAL ASN LYS VAL ARG VAL ALA ILE LYS LYS ILE          
SEQRES   5 A  356  SER PRO PHE GLU HIS GLN THR TYR CYS GLN ARG THR LEU          
SEQRES   6 A  356  ARG GLU ILE LYS ILE LEU LEU ARG PHE ARG HIS GLU ASN          
SEQRES   7 A  356  ILE ILE GLY ILE ASN ASP ILE ILE ARG ALA PRO THR ILE          
SEQRES   8 A  356  GLU GLN MET LYS ASP VAL TYR ILE VAL GLN ASP LEU MET          
SEQRES   9 A  356  GLU THR ASP LEU TYR LYS LEU LEU LYS THR GLN HIS LEU          
SEQRES  10 A  356  SER ASN ASP HIS ILE CYS TYR PHE LEU TYR GLN ILE LEU          
SEQRES  11 A  356  ARG GLY LEU LYS TYR ILE HIS SER ALA ASN VAL LEU HIS          
SEQRES  12 A  356  ARG ASP LEU LYS PRO SER ASN LEU LEU LEU ASN THR THR          
SEQRES  13 A  356  CYS ASP LEU LYS ILE CYS ASP PHE GLY LEU ALA ARG VAL          
SEQRES  14 A  356  ALA ASP PRO ASP HIS ASP HIS THR GLY PHE LEU TPO GLU          
SEQRES  15 A  356  PTR VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET          
SEQRES  16 A  356  LEU ASN SER LYS GLY TYR THR LYS SER ILE ASP ILE TRP          
SEQRES  17 A  356  SER VAL GLY CYS ILE LEU ALA GLU MET LEU SER ASN ARG          
SEQRES  18 A  356  PRO ILE PHE PRO GLY LYS HIS TYR LEU ASP GLN LEU ASN          
SEQRES  19 A  356  HIS ILE LEU GLY ILE LEU GLY SER PRO SER GLN GLU ASP          
SEQRES  20 A  356  LEU ASN CYS ILE ILE ASN LEU LYS ALA ARG ASN TYR LEU          
SEQRES  21 A  356  LEU SER LEU PRO HIS LYS ASN LYS VAL PRO TRP ASN ARG          
SEQRES  22 A  356  LEU PHE PRO ASN ALA ASP SER LYS ALA LEU ASP LEU LEU          
SEQRES  23 A  356  ASP LYS MET LEU THR PHE ASN PRO HIS LYS ARG ILE GLU          
SEQRES  24 A  356  VAL GLU GLN ALA LEU ALA HIS PRO TYR LEU GLU GLN TYR          
SEQRES  25 A  356  TYR ASP PRO SER ASP GLU PRO ILE ALA GLU ALA PRO PHE          
SEQRES  26 A  356  LYS PHE ASP MET GLU LEU ASP ASP LEU PRO LYS GLU LYS          
SEQRES  27 A  356  LEU LYS GLU LEU ILE PHE GLU GLU THR ALA ARG PHE GLN          
SEQRES  28 A  356  PRO GLY TYR ARG SER                                          
SEQRES   1 C  356  GLY PRO GLY GLY ALA GLY PRO GLU MET VAL ARG GLY GLN          
SEQRES   2 C  356  VAL PHE ASP VAL GLY PRO ARG TYR THR ASN LEU SER TYR          
SEQRES   3 C  356  ILE GLY GLU GLY ALA TYR GLY MET VAL CYS SER ALA TYR          
SEQRES   4 C  356  ASP ASN VAL ASN LYS VAL ARG VAL ALA ILE LYS LYS ILE          
SEQRES   5 C  356  SER PRO PHE GLU HIS GLN THR TYR CYS GLN ARG THR LEU          
SEQRES   6 C  356  ARG GLU ILE LYS ILE LEU LEU ARG PHE ARG HIS GLU ASN          
SEQRES   7 C  356  ILE ILE GLY ILE ASN ASP ILE ILE ARG ALA PRO THR ILE          
SEQRES   8 C  356  GLU GLN MET LYS ASP VAL TYR ILE VAL GLN ASP LEU MET          
SEQRES   9 C  356  GLU THR ASP LEU TYR LYS LEU LEU LYS THR GLN HIS LEU          
SEQRES  10 C  356  SER ASN ASP HIS ILE CYS TYR PHE LEU TYR GLN ILE LEU          
SEQRES  11 C  356  ARG GLY LEU LYS TYR ILE HIS SER ALA ASN VAL LEU HIS          
SEQRES  12 C  356  ARG ASP LEU LYS PRO SER ASN LEU LEU LEU ASN THR THR          
SEQRES  13 C  356  CYS ASP LEU LYS ILE CYS ASP PHE GLY LEU ALA ARG VAL          
SEQRES  14 C  356  ALA ASP PRO ASP HIS ASP HIS THR GLY PHE LEU TPO GLU          
SEQRES  15 C  356  PTR VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET          
SEQRES  16 C  356  LEU ASN SER LYS GLY TYR THR LYS SER ILE ASP ILE TRP          
SEQRES  17 C  356  SER VAL GLY CYS ILE LEU ALA GLU MET LEU SER ASN ARG          
SEQRES  18 C  356  PRO ILE PHE PRO GLY LYS HIS TYR LEU ASP GLN LEU ASN          
SEQRES  19 C  356  HIS ILE LEU GLY ILE LEU GLY SER PRO SER GLN GLU ASP          
SEQRES  20 C  356  LEU ASN CYS ILE ILE ASN LEU LYS ALA ARG ASN TYR LEU          
SEQRES  21 C  356  LEU SER LEU PRO HIS LYS ASN LYS VAL PRO TRP ASN ARG          
SEQRES  22 C  356  LEU PHE PRO ASN ALA ASP SER LYS ALA LEU ASP LEU LEU          
SEQRES  23 C  356  ASP LYS MET LEU THR PHE ASN PRO HIS LYS ARG ILE GLU          
SEQRES  24 C  356  VAL GLU GLN ALA LEU ALA HIS PRO TYR LEU GLU GLN TYR          
SEQRES  25 C  356  TYR ASP PRO SER ASP GLU PRO ILE ALA GLU ALA PRO PHE          
SEQRES  26 C  356  LYS PHE ASP MET GLU LEU ASP ASP LEU PRO LYS GLU LYS          
SEQRES  27 C  356  LEU LYS GLU LEU ILE PHE GLU GLU THR ALA ARG PHE GLN          
SEQRES  28 C  356  PRO GLY TYR ARG SER                                          
SEQRES   1 B   97  GLY MET ALA GLU TYR GLY THR LEU LEU GLN ASP LEU THR          
SEQRES   2 B   97  ASN ASN ILE THR LEU GLU ASP LEU GLU GLN LEU LYS SER          
SEQRES   3 B   97  ALA CYS LYS GLU ASP ILE PRO SER GLU LYS SER GLU GLU          
SEQRES   4 B   97  ILE THR THR GLY SER ALA TRP PHE SER PHE LEU GLU SER          
SEQRES   5 B   97  HIS ASN LYS LEU ASP LYS ASP ASN LEU SER TYR ILE GLU          
SEQRES   6 B   97  HIS ILE PHE GLU ILE SER ARG ARG PRO ASP LEU LEU THR          
SEQRES   7 B   97  MET VAL VAL ASP TYR ARG THR ARG VAL LEU LYS ILE SER          
SEQRES   8 B   97  GLU GLU ASP GLU LEU ASP                                      
MODRES 4IZA TPO A  185  THR  PHOSPHOTHREONINE                                   
MODRES 4IZA PTR A  187  TYR  O-PHOSPHOTYROSINE                                  
HET    TPO  A 185      11                                                       
HET    PTR  A 187      16                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   1  PTR    C9 H12 N O6 P                                                
FORMUL   4  HOH   *633(H2 O)                                                    
HELIX    1   1 HIS A   61  PHE A   78  1                                  18    
HELIX    2   2 LEU A  112  GLN A  119  1                                   8    
HELIX    3   3 SER A  122  ALA A  143  1                                  22    
HELIX    4   4 LYS A  151  SER A  153  5                                   3    
HELIX    5   5 THR A  190  ARG A  194  5                                   5    
HELIX    6   6 ALA A  195  ASN A  201  1                                   7    
HELIX    7   7 LYS A  207  ASN A  224  1                                  18    
HELIX    8   8 HIS A  232  GLY A  245  1                                  14    
HELIX    9   9 SER A  248  ASN A  253  1                                   6    
HELIX   10  10 ASN A  257  LEU A  267  1                                  11    
HELIX   11  11 PRO A  274  PHE A  279  1                                   6    
HELIX   12  12 ASP A  283  LEU A  294  1                                  12    
HELIX   13  13 GLU A  303  ALA A  309  1                                   7    
HELIX   14  14 HIS A  310  GLU A  314  5                                   5    
HELIX   15  15 ASP A  318  GLU A  322  5                                   5    
HELIX   16  16 PRO A  339  ALA A  352  1                                  14    
HELIX   17  17 ARG A  353  GLN A  355  5                                   3    
HELIX   18  18 HIS C   61  PHE C   78  1                                  18    
HELIX   19  19 LEU C  112  GLN C  119  1                                   8    
HELIX   20  20 SER C  122  ALA C  143  1                                  22    
HELIX   21  21 LYS C  151  SER C  153  5                                   3    
HELIX   22  22 ALA C  195  LEU C  200  1                                   6    
HELIX   23  23 LYS C  207  LEU C  222  1                                  16    
HELIX   24  24 HIS C  232  GLY C  245  1                                  14    
HELIX   25  25 SER C  248  CYS C  254  1                                   7    
HELIX   26  26 ASN C  257  SER C  266  1                                  10    
HELIX   27  27 PRO C  274  PHE C  279  1                                   6    
HELIX   28  28 ASP C  283  LEU C  294  1                                  12    
HELIX   29  29 ASN C  297  ARG C  301  5                                   5    
HELIX   30  30 GLU C  303  ALA C  309  1                                   7    
HELIX   31  31 HIS C  310  GLU C  314  5                                   5    
HELIX   32  32 ASP C  318  GLU C  322  5                                   5    
HELIX   33  33 GLU C  334  LEU C  338  5                                   5    
HELIX   34  34 PRO C  339  THR C  351  1                                  13    
HELIX   35  35 ALA C  352  GLN C  355  5                                   4    
HELIX   36  36 MET B    1  ASN B   14  1                                  14    
HELIX   37  37 THR B   16  LYS B   28  1                                  13    
HELIX   38  38 ILE B   31  LYS B   35  5                                   5    
HELIX   39  39 THR B   41  HIS B   52  1                                  12    
HELIX   40  40 LEU B   60  SER B   70  1                                  11    
HELIX   41  41 ARG B   72  GLU B   91  1                                  20    
SHEET    1   A 2 MET A  13  VAL A  14  0                                        
SHEET    2   A 2 GLN A  17  VAL A  18 -1  O  GLN A  17   N  VAL A  14           
SHEET    1   B 5 TYR A  25  GLY A  34  0                                        
SHEET    2   B 5 GLY A  37  ASP A  44 -1  O  TYR A  43   N  THR A  26           
SHEET    3   B 5 VAL A  49  ILE A  56 -1  O  LYS A  55   N  MET A  38           
SHEET    4   B 5 VAL A 101  ASP A 106 -1  O  VAL A 101   N  ILE A  56           
SHEET    5   B 5 ASP A  88  ILE A  90 -1  N  ILE A  90   O  TYR A 102           
SHEET    1   C 3 THR A 110  ASP A 111  0                                        
SHEET    2   C 3 LEU A 155  LEU A 157 -1  O  LEU A 157   N  THR A 110           
SHEET    3   C 3 LEU A 163  ILE A 165 -1  O  LYS A 164   N  LEU A 156           
SHEET    1   D 2 VAL A 145  LEU A 146  0                                        
SHEET    2   D 2 ARG A 172  VAL A 173 -1  O  ARG A 172   N  LEU A 146           
SHEET    1   E 2 MET C  13  VAL C  14  0                                        
SHEET    2   E 2 GLN C  17  VAL C  18 -1  O  GLN C  17   N  VAL C  14           
SHEET    1   F 5 TYR C  25  GLU C  33  0                                        
SHEET    2   F 5 MET C  38  ASP C  44 -1  O  TYR C  43   N  THR C  26           
SHEET    3   F 5 VAL C  49  ILE C  56 -1  O  VAL C  49   N  ASP C  44           
SHEET    4   F 5 VAL C 101  ASP C 106 -1  O  VAL C 101   N  ILE C  56           
SHEET    5   F 5 ASP C  88  ILE C  90 -1  N  ILE C  90   O  TYR C 102           
SHEET    1   G 3 THR C 110  ASP C 111  0                                        
SHEET    2   G 3 LEU C 155  LEU C 157 -1  O  LEU C 157   N  THR C 110           
SHEET    3   G 3 LEU C 163  ILE C 165 -1  O  LYS C 164   N  LEU C 156           
SHEET    1   H 2 VAL C 145  LEU C 146  0                                        
SHEET    2   H 2 ARG C 172  VAL C 173 -1  O  ARG C 172   N  LEU C 146           
LINK         C   LEU A 184                 N   TPO A 185     1555   1555  1.33  
LINK         C   TPO A 185                 N   GLU A 186     1555   1555  1.34  
LINK         C   GLU A 186                 N   PTR A 187     1555   1555  1.33  
LINK         C   PTR A 187                 N   VAL A 188     1555   1555  1.34  
CISPEP   1 GLY A   22    PRO A   23          0         2.72                     
CRYST1   73.758  204.024   61.135  90.00  90.00  90.00 P 21 21 2     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      0.013558  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004901  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016357        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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