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Database: PDB
Entry: 4GSB
LinkDB: 4GSB
Original site: 4GSB 
HEADER    TRANSFERASE                             27-AUG-12   4GSB              
TITLE     MONOCLINIC CRYSTAL FORM OF THE APO-ERK2                               
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                                                      
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    KINASE, TRANSFERASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.POZHARSKI,J.ZHANG,P.SHAPIRO                                         
REVDAT   1   12-SEP-12 4GSB    0                                                
JRNL        AUTH   J.ZHANG,E.POZHARSKI,P.SHAPIRO                                
JRNL        TITL   MONOCLINIC CRYSTAL FORM OF THE APO-ERK2                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 35048                          
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) : 0.156                           
REMARK   3   R VALUE            (WORKING SET) : 0.154                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1752                            
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) : 2446                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2230                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 132                          
REMARK   3   BIN FREE R VALUE                    : 0.2350                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2793                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 51                                      
REMARK   3   SOLVENT ATOMS            : 271                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.38                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.92000                                             
REMARK   3    B22 (A**2) : 1.47000                                              
REMARK   3    B33 (A**2) : -0.34000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.35000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.115         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.115         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.069         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.242         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3119 ; 0.022 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4249 ; 2.132 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   390 ; 6.319 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   148 ;40.517 ;24.122       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   541 ;13.991 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;21.591 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   471 ; 0.165 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2375 ; 0.012 ; 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  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     9        A   107                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.0027  11.4774   3.1646              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1873 T22:   0.0978                                     
REMARK   3      T33:   0.0533 T12:   0.0148                                     
REMARK   3      T13:  -0.0401 T23:   0.0424                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3938 L22:   1.0144                                     
REMARK   3      L33:   7.3729 L12:  -0.4177                                     
REMARK   3      L13:   0.2008 L23:  -1.6553                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0779 S12:   0.0587 S13:   0.0644                       
REMARK   3      S21:   0.1430 S22:   0.1580 S23:   0.0240                       
REMARK   3      S31:  -0.8367 S32:  -0.4711 S33:  -0.0801                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   108        A   328                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.4227   6.5753  27.8768              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0609 T22:   0.0070                                     
REMARK   3      T33:   0.0733 T12:   0.0173                                     
REMARK   3      T13:   0.0151 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4912 L22:   0.6898                                     
REMARK   3      L33:   0.8395 L12:   0.5737                                     
REMARK   3      L13:   0.4167 L23:   0.2669                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0274 S12:  -0.0073 S13:   0.0996                       
REMARK   3      S21:   0.0106 S22:  -0.0206 S23:   0.0050                       
REMARK   3      S31:   0.0011 S32:   0.0005 S33:  -0.0069                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   329        A   356                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.6191   4.8941  -3.1728              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1317 T22:   0.2983                                     
REMARK   3      T33:   0.1336 T12:   0.0316                                     
REMARK   3      T13:  -0.0403 T23:   0.0305                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5113 L22:   3.5184                                     
REMARK   3      L33:   7.5634 L12:   0.1277                                     
REMARK   3      L13:   1.2820 L23:   0.3410                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0249 S12:   0.3216 S13:  -0.3721                       
REMARK   3      S21:  -0.0870 S22:   0.0601 S23:  -0.4344                       
REMARK   3      S31:   0.4997 S32:   1.1597 S33:  -0.0851                       
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 U VALUES: WITH TLS ADDED                                  
REMARK   4                                                                      
REMARK   4 4GSB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-SEP-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB074573.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35077                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.024                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.14700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.14700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1ERK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 5% PEG400, 2M          
REMARK 280  AMMONIUM SULFATE, SITTING DROP VAPOR DIFFUSION, TEMPERATURE 295K    
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       34.98500            
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     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     GLY A    32                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     TYR A    34                                                      
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  13    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  46    CE   NZ                                             
REMARK 470     GLN A  64    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 112    CE   NZ                                             
REMARK 470     ARG A 223    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 275    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 328    CG   CD   CE   NZ                                   
REMARK 470     GLU A 332    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 334    CG   OD1  OD2                                       
REMARK 470     ASP A 335    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG1  THR A   204     O    HOH A   693              2.05            
REMARK 500   O    PRO A    56     OD   CSO A    63              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 170   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    LEU A 242   CB  -  CG  -  CD1 ANGL. DEV. =  10.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  13       62.76     29.97                                   
REMARK 500    ARG A 146      -10.47     79.12                                   
REMARK 500    ASP A 165       78.76     65.24                                   
REMARK 500    ASP A 173       70.25   -152.33                                   
REMARK 500    ASN A 199       17.79   -157.47                                   
REMARK 500    ASN A 222       19.92     56.98                                   
REMARK 500    LEU A 292       55.95    -92.76                                   
REMARK 500    ASP A 316       94.00   -161.20                                   
REMARK 500    MET A 331      114.49    -37.41                                   
REMARK 500    ASP A 335       61.72   -112.51                                   
REMARK 500    PRO A 354      135.29    -39.09                                   
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 GOL 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                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 408                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4GT3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4GVA   RELATED DB: PDB                                   
DBREF  4GSB A    1   358  UNP    P63086   MK01_RAT         1    358             
SEQADV 4GSB HIS A   -5  UNP  P63086              EXPRESSION TAG                 
SEQADV 4GSB HIS A   -4  UNP  P63086              EXPRESSION TAG                 
SEQADV 4GSB HIS A   -3  UNP  P63086              EXPRESSION TAG                 
SEQADV 4GSB HIS A   -2  UNP  P63086              EXPRESSION TAG                 
SEQADV 4GSB HIS A   -1  UNP  P63086              EXPRESSION TAG                 
SEQADV 4GSB HIS A    0  UNP  P63086              EXPRESSION TAG                 
SEQRES   1 A  364  HIS HIS HIS HIS HIS HIS MET ALA ALA ALA ALA ALA ALA          
SEQRES   2 A  364  GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL GLY          
SEQRES   3 A  364  PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY ALA          
SEQRES   4 A  364  TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN LYS          
SEQRES   5 A  364  VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU HIS          
SEQRES   6 A  364  GLN THR TYR CSO GLN ARG THR LEU ARG GLU ILE LYS ILE          
SEQRES   7 A  364  LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN          
SEQRES   8 A  364  ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS ASP          
SEQRES   9 A  364  VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU TYR          
SEQRES  10 A  364  LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS ILE          
SEQRES  11 A  364  CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR          
SEQRES  12 A  364  ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  13 A  364  SER ASN LEU LEU LEU ASN THR THR CME ASP LEU LYS ILE          
SEQRES  14 A  364  CYS ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP HIS          
SEQRES  15 A  364  ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR ARG          
SEQRES  16 A  364  TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS GLY          
SEQRES  17 A  364  TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS ILE          
SEQRES  18 A  364  LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO GLY          
SEQRES  19 A  364  LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE          
SEQRES  20 A  364  LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE ILE          
SEQRES  21 A  364  ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO HIS          
SEQRES  22 A  364  LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA          
SEQRES  23 A  364  ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU THR          
SEQRES  24 A  364  PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU          
SEQRES  25 A  364  ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER ASP          
SEQRES  26 A  364  GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET GLU          
SEQRES  27 A  364  LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE          
SEQRES  28 A  364  PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR ARG SER          
MODRES 4GSB CSO A   63  CYS  S-HYDROXYCYSTEINE                                  
MODRES 4GSB CME A  159  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
HET    CSO  A  63       7                                                       
HET    CME  A 159      10                                                       
HET    GOL  A 401       6                                                       
HET    SO4  A 402       5                                                       
HET    GOL  A 403       6                                                       
HET    GOL  A 404       6                                                       
HET    GOL  A 405       6                                                       
HET    GOL  A 406       6                                                       
HET    GOL  A 407       6                                                       
HET    PGE  A 408      10                                                       
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  CSO    C3 H7 N O3 S                                                 
FORMUL   1  CME    C5 H11 N O3 S2                                               
FORMUL   2  GOL    6(C3 H8 O3)                                                  
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   9  PGE    C6 H14 O4                                                    
FORMUL  10  HOH   *271(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 HIS A  230  GLY A  243  1                                  14    
HELIX   10  10 SER A  246  CYS A  252  1                                   7    
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 2 MET A  11  VAL A  12  0                                        
SHEET    2   A 2 GLN A  15  VAL A  16 -1  O  GLN A  15   N  VAL A  12           
SHEET    1   B 5 TYR A  23  GLY A  30  0                                        
SHEET    2   B 5 VAL A  37  ASP A  42 -1  O  VAL A  37   N  ILE A  29           
SHEET    3   B 5 VAL A  47  ILE A  54 -1  O  VAL A  47   N  ASP A  42           
SHEET    4   B 5 VAL A  99  ASP A 104 -1  O  GLN A 103   N  ALA A  50           
SHEET    5   B 5 ASP A  86  ILE A  88 -1  N  ILE A  88   O  TYR A 100           
SHEET    1   C 3 THR A 108  ASP A 109  0                                        
SHEET    2   C 3 LEU A 153  LEU A 155 -1  O  LEU A 155   N  THR A 108           
SHEET    3   C 3 LEU A 161  ILE A 163 -1  O  LYS A 162   N  LEU A 154           
SHEET    1   D 2 VAL A 143  LEU A 144  0                                        
SHEET    2   D 2 ARG A 170  VAL A 171 -1  O  ARG A 170   N  LEU A 144           
LINK         C   TYR A  62                 N   CSO A  63     1555   1555  1.33  
LINK         C   CSO A  63                 N   GLN A  64     1555   1555  1.33  
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  
CISPEP   1 GLY A   20    PRO A   21          0         2.33                     
SITE     1 AC1  5 HIS A 230  TYR A 231  LEU A 232  ASP A 233                    
SITE     2 AC1  5 HOH A 671                                                     
SITE     1 AC2  6 TYR A 185  ARG A 189  ARG A 192  TYR A 231                    
SITE     2 AC2  6 HOH A 706  HOH A 733                                          
SITE     1 AC3  6 PRO A  91  SER A 244  HIS A 267  ASN A 269                    
SITE     2 AC3  6 HOH A 577  HOH A 578                                          
SITE     1 AC4  5 LYS A 298  ARG A 299  ILE A 300  GLN A 304                    
SITE     2 AC4  5 HOH A 669                                                     
SITE     1 AC5  7 GLU A  94  GLN A  95  LYS A  97  LEU A 263                    
SITE     2 AC5  7 LEU A 265  PRO A 266  HOH A 533                               
SITE     1 AC6  9 ASP A  18  ARG A  89  ALA A  90  MET A  96                    
SITE     2 AC6  9 LYS A  97  ASP A  98  HIS A 267  HOH A 565                    
SITE     3 AC6  9 HOH A 566                                                     
SITE     1 AC7  8 HIS A 118  LEU A 119  ILE A 124  LEU A 220                    
SITE     2 AC7  8 ASN A 279  ALA A 280  HOH A 524  HOH A 621                    
SITE     1 AC8  6 ALA A  50  LYS A  52  GLN A 103  ASP A 104                    
SITE     2 AC8  6 LEU A 105  MET A 106                                          
CRYST1   48.780   69.970   59.890  90.00 108.96  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      0.020500  0.000000  0.007043        0.00000                         
SCALE2      0.000000  0.014292  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017655        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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