GenomeNet

Database: PDB
Entry: 4S34
LinkDB: 4S34
Original site: 4S34 
HEADER    TRANSFERASE                             26-JAN-15   4S34              
TITLE     ERK2 (I84A) IN COMPLEX WITH AMP-PNP                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MAP KINASE 1, MAPK 1, ERT1, EXTRACELLULAR SIGNAL-REGULATED  
COMPND   5 KINASE 2, ERK-2, MAP KINASE ISOFORM P42, P42-MAPK, MITOGEN-ACTIVATED 
COMPND   6 PROTEIN KINASE 2, MAP KINASE 2, MAPK 2;                              
COMPND   7 EC: 2.7.11.24;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;                                 
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: MAPK1, ERK2, MAPK, PRKM1;                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SIGNAL TRANSDUCTION, PHOSPHORYLATION, TRANSFERASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.LIVNAH,Y.KARAMANSHA,N.TZARUM                                        
REVDAT   1   27-JAN-16 4S34    0                                                
JRNL        AUTH   O.LIVNAH,Y.KARAMANSHA,N.TZARUM                               
JRNL        TITL   MULTIPLE MECHANISMS RENDER ERK PROTEINS MEK-INDEPENDENT      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 12558                          
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) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 651                             
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 691                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.01                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2430                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 38                           
REMARK   3   BIN FREE R VALUE                    : 0.3660                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2782                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 37                                      
REMARK   3   SOLVENT ATOMS            : 70                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.40000                                             
REMARK   3    B22 (A**2) : 0.25000                                              
REMARK   3    B33 (A**2) : 0.16000                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.14000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.793         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.314         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.219         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.561         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2898 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2765 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3939 ; 1.704 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6369 ; 0.865 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   342 ; 6.895 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   137 ;39.342 ;24.161       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   501 ;17.501 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;22.596 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   433 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3213 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   666 ; 0.001 ; 0.020       
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   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4S34 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-15.                  
REMARK 100 THE RCSB ID CODE IS RCSB088119.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13244                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 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: AMORE                                                 
REMARK 200 STARTING MODEL: 1ERK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 61 MM AMMONIUM SULFATE, 100MM BIS TRIS   
REMARK 280  PH 7.0, 12-15% (V/V) PEG 3350, VAPOR DIFFUSION, SITTING DROP,       
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       35.18900            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     GLU A    10                                                      
REMARK 465     MET A    11                                                      
REMARK 465     VAL A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     ASP A   330                                                      
REMARK 465     MET A   331                                                      
REMARK 465     GLU A   332                                                      
REMARK 465     GLY A   355                                                      
REMARK 465     TYR A   356                                                      
REMARK 465     ARG A   357                                                      
REMARK 465     SER A   358                                                      
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 223    CG   CD   NE   CZ   NH1  NH2                        
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  89   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 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  28      156.88    -46.10                                   
REMARK 500    ILE A  29      -60.08   -136.12                                   
REMARK 500    TYR A  34       41.85     32.57                                   
REMARK 500    ALA A  40      135.77   -170.86                                   
REMARK 500    ARG A 146       -4.35     83.90                                   
REMARK 500    ASP A 147       37.81   -149.03                                   
REMARK 500    ASP A 165       81.84     70.56                                   
REMARK 500    ASP A 173       73.52   -151.64                                   
REMARK 500    ASN A 199       13.82   -165.58                                   
REMARK 500    ASN A 255      104.15    -38.28                                   
REMARK 500    LEU A 292       56.06   -103.15                                   
REMARK 500    ASP A 316       88.65   -176.17                                   
REMARK 500    ASP A 334      -73.81     26.06                                   
REMARK 500    LYS A 338      -48.04    -21.96                                   
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 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 403                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ERK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4S2Z   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4S30   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4S31   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4S32   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4S33   RELATED DB: PDB                                   
DBREF  4S34 A    1   358  UNP    P63086   MK01_RAT         1    358             
SEQADV 4S34 ALA A   84  UNP  P63086    ILE    84 ENGINEERED MUTATION            
SEQRES   1 A  358  MET ALA ALA ALA ALA ALA ALA GLY PRO GLU MET VAL ARG          
SEQRES   2 A  358  GLY GLN VAL PHE ASP VAL GLY PRO ARG TYR THR ASN LEU          
SEQRES   3 A  358  SER TYR ILE GLY GLU GLY ALA TYR GLY MET VAL CYS SER          
SEQRES   4 A  358  ALA TYR ASP ASN LEU ASN LYS VAL ARG VAL ALA ILE LYS          
SEQRES   5 A  358  LYS ILE SER PRO PHE GLU HIS GLN THR TYR CYS GLN ARG          
SEQRES   6 A  358  THR LEU ARG GLU ILE LYS ILE LEU LEU ARG PHE ARG HIS          
SEQRES   7 A  358  GLU ASN ILE ILE GLY ALA ASN ASP ILE ILE ARG ALA PRO          
SEQRES   8 A  358  THR ILE GLU GLN MET LYS ASP VAL TYR ILE VAL GLN ASP          
SEQRES   9 A  358  LEU MET GLU THR ASP LEU TYR LYS LEU LEU LYS THR GLN          
SEQRES  10 A  358  HIS LEU SER ASN ASP HIS ILE CYS TYR PHE LEU TYR GLN          
SEQRES  11 A  358  ILE LEU ARG GLY LEU LYS TYR ILE HIS SER ALA ASN VAL          
SEQRES  12 A  358  LEU HIS ARG ASP LEU LYS PRO SER ASN LEU LEU LEU ASN          
SEQRES  13 A  358  THR THR CYS ASP LEU LYS ILE CYS ASP PHE GLY LEU ALA          
SEQRES  14 A  358  ARG VAL ALA ASP PRO ASP HIS ASP HIS THR GLY PHE LEU          
SEQRES  15 A  358  THR GLU TYR VAL ALA THR ARG TRP TYR ARG ALA PRO GLU          
SEQRES  16 A  358  ILE MET LEU ASN SER LYS GLY TYR THR LYS SER ILE ASP          
SEQRES  17 A  358  ILE TRP SER VAL GLY CYS ILE LEU ALA GLU MET LEU SER          
SEQRES  18 A  358  ASN ARG PRO ILE PHE PRO GLY LYS HIS TYR LEU ASP GLN          
SEQRES  19 A  358  LEU ASN HIS ILE LEU GLY ILE LEU GLY SER PRO SER GLN          
SEQRES  20 A  358  GLU ASP LEU ASN CYS ILE ILE ASN LEU LYS ALA ARG ASN          
SEQRES  21 A  358  TYR LEU LEU SER LEU PRO HIS LYS ASN LYS VAL PRO TRP          
SEQRES  22 A  358  ASN ARG LEU PHE PRO ASN ALA ASP SER LYS ALA LEU ASP          
SEQRES  23 A  358  LEU LEU ASP LYS MET LEU THR PHE ASN PRO HIS LYS ARG          
SEQRES  24 A  358  ILE GLU VAL GLU GLN ALA LEU ALA HIS PRO TYR LEU GLU          
SEQRES  25 A  358  GLN TYR TYR ASP PRO SER ASP GLU PRO ILE ALA GLU ALA          
SEQRES  26 A  358  PRO PHE LYS PHE ASP MET GLU LEU ASP ASP LEU PRO LYS          
SEQRES  27 A  358  GLU LYS LEU LYS GLU LEU ILE PHE GLU GLU THR ALA ARG          
SEQRES  28 A  358  PHE GLN PRO GLY TYR ARG SER                                  
HET    SO4  A 401       5                                                       
HET    ANP  A 402      31                                                       
HET     MG  A 403       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  ANP    C10 H17 N6 O12 P3                                            
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  HOH   *70(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 ASP A  173  ASP A  177  5                                   5    
HELIX    6   6 THR A  188  ARG A  192  5                                   5    
HELIX    7   7 ALA A  193  ASN A  199  1                                   7    
HELIX    8   8 LYS A  205  ASN A  222  1                                  18    
HELIX    9   9 LEU A  232  GLY A  243  1                                  12    
HELIX   10  10 SER A  246  ILE A  253  1                                   8    
HELIX   11  11 ASN A  255  LEU A  265  1                                  11    
HELIX   12  12 PRO A  272  PHE A  277  1                                   6    
HELIX   13  13 ASP A  281  LEU A  292  1                                  12    
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 PRO A  337  THR A  349  1                                  13    
HELIX   18  18 ALA A  350  GLN A  353  5                                   4    
SHEET    1   A 5 TYR A  23  GLU A  31  0                                        
SHEET    2   A 5 MET A  36  ASP A  42 -1  O  SER A  39   N  SER A  27           
SHEET    3   A 5 VAL A  47  ILE A  54 -1  O  LYS A  53   N  MET A  36           
SHEET    4   A 5 VAL A  99  GLN A 103 -1  O  GLN A 103   N  ALA A  50           
SHEET    5   A 5 ASP A  86  ILE A  88 -1  N  ILE A  88   O  TYR A 100           
SHEET    1   B 3 THR A 108  ASP A 109  0                                        
SHEET    2   B 3 LEU A 153  LEU A 155 -1  O  LEU A 155   N  THR A 108           
SHEET    3   B 3 LEU A 161  ILE A 163 -1  O  LYS A 162   N  LEU A 154           
SHEET    1   C 2 VAL A 143  LEU A 144  0                                        
SHEET    2   C 2 ARG A 170  VAL A 171 -1  O  ARG A 170   N  LEU A 144           
SITE     1 AC1  4 ARG A 189  ARG A 192  TYR A 231  HOH A 532                    
SITE     1 AC2 13 ILE A  29  GLY A  30  GLU A  31  GLY A  32                    
SITE     2 AC2 13 ALA A  33  VAL A  37  GLN A 103  ASP A 104                    
SITE     3 AC2 13 MET A 106  ASN A 152  LEU A 154  ASP A 165                    
SITE     4 AC2 13  MG A 403                                                     
SITE     1 AC3  2 LYS A 149  ANP A 402                                          
CRYST1   49.186   70.378   59.873  90.00 109.08  90.00 P 1 21 1      2          
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      0.020331  0.000000  0.007034        0.00000                         
SCALE2      0.000000  0.014209  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017673        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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