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Database: PDB
Entry: 4XNE
LinkDB: 4XNE
Original site: 4XNE 
HEADER    TRANSFERASE                             15-JAN-15   4XNE              
TITLE     CRYSTAL STRUCTURE OF ERK2 IN COMPLEX WITH AN INHIBITOR                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 9-354;                                        
COMPND   5 SYNONYM: MAPK 1,ERT1,EXTRACELLULAR SIGNAL-REGULATED KINASE 2,ERK-2,  
COMPND   6 MAP KINASE ISOFORM P42,P42-MAPK,MITOGEN-ACTIVATED PROTEIN KINASE 2,  
COMPND   7 MAPK 2;                                                              
COMPND   8 EC: 2.7.11.24;                                                       
COMPND   9 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 GENE: MAPK1, ERK2, MAPK, PRKM1;                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SERINE THREONINE KINASE INHIBITOR, TRANSFERASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.GELIN,F.ALLEMAND,G.LABESSE,J.F.GUICHOU                              
REVDAT   2   19-AUG-15 4XNE    1       JRNL                                     
REVDAT   1   12-AUG-15 4XNE    0                                                
JRNL        AUTH   M.GELIN,V.DELFOSSE,F.ALLEMAND,F.HOH,Y.SALLAZ-DAMAZ,          
JRNL        AUTH 2 M.PIROCCHI,W.BOURGUET,J.L.FERRER,G.LABESSE,J.F.GUICHOU       
JRNL        TITL   COMBINING `DRY' CO-CRYSTALLIZATION AND IN SITU DIFFRACTION   
JRNL        TITL 2 TO FACILITATE LIGAND SCREENING BY X-RAY CRYSTALLOGRAPHY.     
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  71  1777 2015              
JRNL        REFN                   ESSN 1399-0047                               
JRNL        PMID   26249358                                                     
JRNL        DOI    10.1107/S1399004715010342                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 34272                          
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) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1804                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2541                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.85                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 134                          
REMARK   3   BIN FREE R VALUE                    : 0.2710                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2839                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 18                                      
REMARK   3   SOLVENT ATOMS            : 126                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.57000                                             
REMARK   3    B22 (A**2) : 0.54000                                              
REMARK   3    B33 (A**2) : 0.06000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.11000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.121         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.120         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.082         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.609         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2984 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2889 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4056 ; 1.417 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6666 ; 0.784 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   364 ; 5.442 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   143 ;39.175 ;24.056       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   538 ;17.129 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;20.951 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   446 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3333 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   692 ; 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):  1403 ; 2.135 ; 3.083       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1402 ; 2.135 ; 3.081       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1757 ; 3.255 ; 4.613       
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 U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 4XNE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000205998.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM30A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9797                             
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34272                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.8000                             
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: NULL                         
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MES 100MM, (NH4)2SO4 200MM, BETA         
REMARK 280  -MERCAPTOETHANOL 20MM AND 26% (W/V) PEG MME2000, PH 6.5, VAPOR      
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
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       35.78000            
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.                         
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 TOTAL BURIED SURFACE AREA: 190 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 16660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
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 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    LEU A 110   CB  -  CG  -  CD2 ANGL. DEV. =  10.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  13       51.64     38.48                                   
REMARK 500    ALA A  33       22.54    -74.37                                   
REMARK 500    TYR A  34      -53.82   -130.53                                   
REMARK 500    ARG A 146       -2.65     76.63                                   
REMARK 500    ASP A 147       42.42   -142.21                                   
REMARK 500    ASP A 165       82.73     62.87                                   
REMARK 500    ASN A 199       14.64   -157.37                                   
REMARK 500    LEU A 292       56.11    -94.82                                   
REMARK 500    LEU A 333      -48.48     88.50                                   
REMARK 500    LYS A 338      -51.31    -25.83                                   
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 TT4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402                 
DBREF  4XNE A    9   354  UNP    P63086   MK01_RAT         9    354             
SEQRES   1 A  346  PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL GLY PRO          
SEQRES   2 A  346  ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY ALA TYR          
SEQRES   3 A  346  GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN LYS VAL          
SEQRES   4 A  346  ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU HIS GLN          
SEQRES   5 A  346  THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS ILE LEU          
SEQRES   6 A  346  LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN ASP          
SEQRES   7 A  346  ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS ASP VAL          
SEQRES   8 A  346  TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU TYR LYS          
SEQRES   9 A  346  LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS ILE CYS          
SEQRES  10 A  346  TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE          
SEQRES  11 A  346  HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO SER          
SEQRES  12 A  346  ASN LEU LEU LEU ASN THR THR CME ASP LEU LYS ILE CYS          
SEQRES  13 A  346  ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP HIS ASP          
SEQRES  14 A  346  HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR ARG TRP          
SEQRES  15 A  346  TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS GLY TYR          
SEQRES  16 A  346  THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS ILE LEU          
SEQRES  17 A  346  ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO GLY LYS          
SEQRES  18 A  346  HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE LEU          
SEQRES  19 A  346  GLY SER PRO SER GLN GLU ASP LEU ASN CME ILE ILE ASN          
SEQRES  20 A  346  LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO HIS LYS          
SEQRES  21 A  346  ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA ASP          
SEQRES  22 A  346  SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU THR PHE          
SEQRES  23 A  346  ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU ALA          
SEQRES  24 A  346  HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER ASP GLU          
SEQRES  25 A  346  PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET GLU LEU          
SEQRES  26 A  346  ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE PHE          
SEQRES  27 A  346  GLU GLU THR ALA ARG PHE GLN PRO                              
MODRES 4XNE CME A  159  CYS  MODIFIED RESIDUE                                   
MODRES 4XNE CME A  252  CYS  MODIFIED RESIDUE                                   
HET    CME  A 159      10                                                       
HET    CME  A 252      10                                                       
HET    TT4  A 401      13                                                       
HET    SO4  A 402       5                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     TT4 1-PHENYL-1H-1,2,4-TRIAZOLE-3,5-DIAMINE                           
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  CME    2(C5 H11 N O3 S2)                                            
FORMUL   2  TT4    C8 H9 N5                                                     
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  HOH   *126(H2 O)                                                    
HELIX    1 AA1 HIS A   59  PHE A   76  1                                  18    
HELIX    2 AA2 THR A   92  MET A   96  5                                   5    
HELIX    3 AA3 LEU A  110  GLN A  117  1                                   8    
HELIX    4 AA4 SER A  120  ALA A  141  1                                  22    
HELIX    5 AA5 LYS A  149  SER A  151  5                                   3    
HELIX    6 AA6 ASP A  173  ASP A  177  5                                   5    
HELIX    7 AA7 THR A  188  ALA A  193  5                                   6    
HELIX    8 AA8 PRO A  194  ASN A  199  1                                   6    
HELIX    9 AA9 LYS A  205  ASN A  222  1                                  18    
HELIX   10 AB1 LEU A  232  GLY A  243  1                                  12    
HELIX   11 AB2 SER A  246  CME A  252  1                                   7    
HELIX   12 AB3 ASN A  255  LEU A  265  1                                  11    
HELIX   13 AB4 PRO A  272  PHE A  277  1                                   6    
HELIX   14 AB5 ASP A  281  LEU A  292  1                                  12    
HELIX   15 AB6 ASN A  295  ARG A  299  5                                   5    
HELIX   16 AB7 GLU A  301  ALA A  307  1                                   7    
HELIX   17 AB8 HIS A  308  GLU A  312  5                                   5    
HELIX   18 AB9 ASP A  316  GLU A  320  5                                   5    
HELIX   19 AC1 PRO A  337  ALA A  350  1                                  14    
HELIX   20 AC2 ARG A  351  GLN A  353  5                                   3    
SHEET    1 AA1 5 TYR A  23  GLU A  31  0                                        
SHEET    2 AA1 5 MET A  36  ASP A  42 -1  O  TYR A  41   N  THR A  24           
SHEET    3 AA1 5 VAL A  47  ILE A  54 -1  O  VAL A  47   N  ASP A  42           
SHEET    4 AA1 5 VAL A  99  ASP A 104 -1  O  GLN A 103   N  ALA A  50           
SHEET    5 AA1 5 ASP A  86  ILE A  88 -1  N  ILE A  88   O  TYR A 100           
SHEET    1 AA2 3 THR A 108  ASP A 109  0                                        
SHEET    2 AA2 3 LEU A 153  LEU A 155 -1  O  LEU A 155   N  THR A 108           
SHEET    3 AA2 3 LEU A 161  ILE A 163 -1  O  LYS A 162   N  LEU A 154           
SHEET    1 AA3 2 VAL A 143  LEU A 144  0                                        
SHEET    2 AA3 2 ARG A 170  VAL A 171 -1  O  ARG A 170   N  LEU A 144           
LINK         C   THR A 158                 N   CME A 159     1555   1555  1.33  
LINK         C   CME A 159                 N   ASP A 160     1555   1555  1.33  
LINK         C   ASN A 251                 N   CME A 252     1555   1555  1.33  
LINK         C   CME A 252                 N   ILE A 253     1555   1555  1.33  
SITE     1 AC1  5 ALA A  50  LYS A  52  GLN A 103  ASP A 104                    
SITE     2 AC1  5 MET A 106                                                     
SITE     1 AC2  3 ARG A 189  ARG A 192  TYR A 231                               
CRYST1   49.150   71.560   60.940  90.00 109.13  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      0.020346  0.000000  0.007058        0.00000                         
SCALE2      0.000000  0.013974  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017369        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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